Production of a compound comprising n-acetylglucosamine-beta-1,6-galactose-beta-1,4-glucose or n-acetylglucosamine-beta-1,6-galactose-beta-1,4-n-acetylglucosamine

Abstract

The present invention is in the technical field of synthetic biology, metabolic engineering and cell cultivation. The present invention describes methods for the production of a compound comprising N-acetylglucosamine-beta-1,6-galactose-beta-1,4-Z1-Z2-R, wherein Z1 is glucose or N-acetylglucosamine (GlcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid. The invention further describes a cell that is capable to produce said compound.

Description

[0001] Production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-glucose or N-acetylglucosamine-beta-l,6-galactose-beta-l,4-N-acetylglucosamine

[0002] Field of the invention

[0003] The present invention is in the technical field of synthetic biology, metabolic engineering and cell cultivation. The present invention describes methods for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine, wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid. The invention further describes a cell that is capable to produce said compound.

[0004] Background of the invention

[0005] To date saccharides are gaining more and more attention as these diverse molecules are widely distributed in all living organisms and play important roles in a variety of physiological and pathological processes including cell metastasis, signal transduction, intercellular adhesion, inflammation and immune response. Saccharides occur in free form or in a bound form, e.g. part of a glycoprotein or a glycolipid. Economical production of these different forms of saccharides is of utmost importance to fully benefit of their biological advantages. An important group of such saccharides are milk saccharides (Urashima T. et al., 2011, Milk Oligosaccharides, Nova Biomedical Books, New York ISBN 978-1-61122-831-1; Coppa et al, 2013, Ital. J. Pediatr. 2013, 39(2)), in particular milk oligosaccharides (MOs), i.e. (oligo)saccharides which are found in milk of animals such as mammals and humans (Urashima et al, 2011; Coppa et al, 2013). A replete amount of milk saccharide structures have been elucidated so far. The majority of milk oligosaccharides found in animals such as mammals and humans comprise lactose at the reducing end (Urashima et al, 2011). Other milk oligosaccharides comprise N-acetyllactosamine (Gal-pi,4-GlcNAc) or lacto-N-biose (Gal-pi,3-GlcNAc) at the reducing end (Urashima et al, 2011; Wrigglesworth et al, 2020, PLoS ONE 15(12); Urashima et al, 2013, Biosci. Biotechnol. Biochem 77(3): p. 455-466; Wei et al, 2018, Sci. Rep. 8:4688). Examples hereof are 3-FLN (Gal-pi,4-(Fuc-al,3-)GlcNAc; also known as Lewis x antigen), 3'- SLN (Neu5Ac-a2,3-Gal-pi,4-GlcNAc), 6'-SLN (Neu5Ac-a2,6-Gal-pi,4-GlcNAc) (Urashima et al, 2011; Wrigglesworth et al, 2020; Wei et al, 2018).

[0006] A compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, has been acknowledged to be of great interest for industrial production. However, it is has been found challenging to introduce the beta- 1,6-branch on the growing saccharide (free or bound to a peptide, protein or lipid). It is hence the object of the present invention to provide a suitable beta-1, 6-N-acetylglucosaminyltransferase that is capable to transfer N-aceteylglucosamine (GIcNAc) to a galactose-beta-l,4-Zi-Z2 containing acceptor such that the desired compound can be produced in an efficient way and in high amounts to meet the needs of the industry.

[0007] Summary of the invention

[0008] In a first aspect, the invention provides a method for the production of a compound comprising N- acetylglucosamine-beta-l,6-galactose-beta-l,4-glucose-Zi-Z2-R, wherein Zi is glucose or N- acetylglucosamine, wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0009] In a second aspect, the invention provides a cell that is capable to produce said compound.

[0010] Detailed description of the invention

[0011] Method for the production of a compound

[0012] In a first aspect, the invention provides a method for the production of a compound comprising N- acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, the method comprising the steps of: providing (i) an acceptor comprising galactose-beta-l,4-Zi-Z2-R, (ii) UDP-N-acetylglucosamine (UDP-GIcNAc) and (iii) a beta-1, 6-N-acetylglucosaminyltransferase; and bringing said (i), (ii) and (iii) into contact with each other under conditions such that said beta-1, 6- N-acetylglucosaminyltransferase transfers a N-acetylglucosamine (GIcNAc) from UDP-GIcNAc to said acceptor in an beta-1, 6-glycosidic linkage as to produce a compound comprising N- acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0013] Throughout the application and claims, it is particularly preferred that R is absent.

[0014] Said "compound" as disclosed in the present Section is preferably as disclosed in the Section "Compound"; said "acceptor" as disclosed in the present Section is preferably as disclosed in the Section "Acceptor"; said "beta-1, 6-N-acetylglucosaminyltransferase" as disclosed in the present Section is preferably as disclosed in the Section "Beta-1, 6-N-acetylglucosaminyltransferase".

[0015] Throughout the application and claims, said conditions are conditions relating to physical or chemical parameters as well-known to the skilled person and include but not limited to temperature, pH and acceptor concentration. Preferably, said conditions include a temperature-range of 30 + / - 20 degrees centigrade (preferably 30 + / - 10 degrees centigrade, most preferably 28-38 degrees centigrade) and / or a pH-range of 2.0 - 10.0 (preferably 3.0 - 8.5, more preferably 5.0 - 8.5, even more preferably 5.5 - 8.5, most preferably 6.0 - 8.5). As understood by the skilled person, the term "saccharide" refers to a molecule consisting of one or more monosaccharide residue(s). The term "monosaccharide" as used herein refers to a sugar that is not decomposable into simpler sugars by hydrolysis, is classed either an aldose or ketose, and contains one or more hydroxyl groups per molecule. Monosaccharides are hence saccharides containing only one simple sugar. In the context of the present invention, the term "oligosaccharide" preferably refers to a saccharide containing 3 up to and including 20 monosaccharides, i.e. the degree of polymerization (DP) is 3-20. An oligosaccharide can be a linear structure or can include branches. The linkage between two sugar units can be expressed, for example, as 1,4, l->4, or (1-4), as used interchangeably herein. Each monosaccharide can be in the cyclic form (e.g. pyranose or furanose form). An oligosaccharide can contain both alpha- and beta-glycosidic bonds or can contain only beta-glycosidic bonds. More preferably, the term "oligosaccharide" refers to a saccharide consisting of < 12, preferably < 11, more preferably < 10, most preferably < 9, monosaccharides.

[0016] Throughout the application and claims, Z2 is absent or is a saccharide; preferably Z2 is absent or is selected from the list consisting of a monosaccharide, a disaccharide and an oligosaccharide; even more preferably Z2 is absent or is a disaccharide or is an oligosaccharide; most preferably Z2 is absent.

[0017] Throughout the application and claims, when Z2 is a disaccharide, it is preferred that Z2 is lactose; when Z2 is an oligosaccharide it is preferred that Z2 is a LNT-containing oligosaccharide or a LNnT-containing oligosaccharide.

[0018] For the sake of clarity, the expression "a compound comprising N-acetylglucosamine-beta-l,6-galactose- beta-l,4-Zi-Z2-R" preferably refers to N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R that optionally consists of one or more additional monosaccharides. Examples of a compound comprising N- acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R are GlcNAc-beta-l,6-(GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R; galactose-beta-l,4-GlcNAc-beta-l,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R; galactose-beta-l,4-GlcNAc-beta-l,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R; etc.

[0019] In a preferred embodiment, said method according to the invention comprises the steps of: providing (i) an acceptor comprising galactose-beta-l,4-Zi-Z2-R, (ii) UDP-N-acetylglucosamine (UDP-GIcNAc), (iii) a beta-1, 6-N-acetylglucosaminyltransferase, and (iv) one or more additional glycosyltransferase(s) and their corresponding nucleotide sugar; and bringing: o said (i), (ii), (iii) and (iv) into contact with each other, or o said (i), (ii) an (iii) into contact with each other and subsequently with (iv), or o said (i) and (iv) into contact with each other and subsequently with (ii) and (iii), under conditions such that said beta-1, 6-N-acetylglucosaminyltransferase transfers a N- acetylglucosamine (GIcNAc) from UDP-GIcNAc to said acceptor in an beta-1, 6-glycosidic linkage as to produce a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid, preferably wherein R is absent.

[0020] In this context of the invention, and throughout the application and claims, it is a preferred embodiment that said one or more additional glycosyltransferases are involved in the production of said compound. It is a further preferred embodiment that said one or more additional glycosyltransferases are selected from the list consisting of a beta-1, 3-N-acetylglucosaminyltransferase, a beta-1, 3-galactosyltransferase, a beta- 1,4-galactosyltransferase, a fucosyltransferase and a sialyltransferase, preferably selected from the list consisting of a beta-1, 3-N-acetylglucosaminyltransferase, a beta-1, 3-galactosyltransferase, a beta-1, 4- galactosyltransferase and a sialyltransferase.

[0021] Said fucosyltransferase is preferably an alpha-1, 2-fucosyltransferase or an alpha-1, 3-fucosyltransferase. Said alpha-1, 2-fucosyltransferase is preferably FutC (preferably from Helicobacter pylori). Said alpha-1, 3- fucosyltransferase is preferably FucT (preferably from Helicobacter pylori).

[0022] Said sialyltransferase is preferably an alpha-2, 3-sialyltransferase or an alpha-2, 6-sialyltransferase, more preferably an alpha-2, 6-sialyltransferase. Said alpha-2, 3-sialyltransferase is preferably ST3 (preferable from Pasteurella multocida). Said alpha-2, 6-sialyltransferase is preferably ST6 (preferable from Photobacterium damselae).

[0023] Said beta-1, 4-galactosyltransferase is preferably selected from GalT7, gatD and LgtB, more preferably LgtB. Said GalT7 is preferably from Pasteurella multocida, more preferably Uniprot ID F47LW1 (sequence version 01). Said gatD is preferably from Pasteurella multocida, more preferably Uniprot ID DOEAD4 (sequence version 01). Said LgtB is preferably from Neisseria meningitidis, more preferably Uniprot ID Q51116 (sequence version 02).

[0024] Said beta-1, 3-galactosyltransferase is preferably WbgO, more preferably WbgO from E. coli 055:1-17, even more preferably Uniprot ID D3QY14 (sequence version 01).

[0025] Said beta-1, 3-N-acetylglucosaminyltransferase is preferably LgtA, more preferably LgtA from Neisseria meningitidis, even more preferably Uniprot ID Q9JXQ6 (sequence version 01).

[0026] If two or more additional glycosyltransferases are provided, the skilled person will understand that these can be jointly added in a method according to the invention or added in different steps.

[0027] In the context of the present invention, it is particularly preferred that said (i), (ii), (iii) and (iv) are brought into contact with each other.

[0028] In an additional and / or alternative preferred embodiment, the compound according to the invention is produced in a cell-free system. Alternatively, at least said beta-1, 6-N-acetylglucosaminyltranfserase is provided as part of a cell extract. Said cell extract is obtained from a cell comprising said beta-1, 6-N-acetylglucosaminyltranfserase; in other words said beta-1, 6-N-acetylglucosaminyltranfserase has been expressed in said cell before cell extraction.

[0029] Alternatively, at least said beta-1, 6-N-acetylglucosaminyltranfserase is provided by a cell (in this context it is preferred that said beta-1, 6-N-acetylglucosaminyltranfserase is heterologous). More preferably, at least said beta-1, 6-N-acetylglucosaminyltranfserase (in this context it is preferred that said beta-1, 6-N- acetylglucosaminyltranfserase is heterologous) and said one or more additional glycosyltransferase(s) are provided by a cell (in this context it is preferred that at least one, preferably at least two, most preferably all, of said one or more additional glycosyltransferases are heterologous).

[0030] Most preferably, said (i), (ii), (iii) and (iv) are provided by a cell. In the context of the present invention, said (i), (ii), (iii) and / or (iv) is / are preferably produced by a cell (preferably a cell according to the second aspect of the invention), either provided by the same cell or by at least two different cells. In this particular context of the invention, said "provided" is preferably replaced with "produced". Said production by a cell can be intracellularly and / or extracellularly.

[0031] In a more preferred embodiment, the invention provides a method for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, the method comprising the steps of: providing a cell in a suitable cultivation medium, wherein said cell expresses said beta-1, 6-N- acetylglucosaminyltransferase and optionally expresses said one or more additional glycosyltransferase(s); providing said acceptor intracellularly, wherein said acceptor is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; providing said UDP-GIcNAc intracellularly, wherein said UDP-GIcNAc is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; optionally providing each corresponding nucleotide sugar of said one or more additional glycosyltransferase(s) intracellularly, wherein said nucleotide sugar is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; cultivating said cell in the suitable cultivation medium under conditions such that a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R is produced, wherein R can be absent or is selected from the list consisting of a peptide, a protein and a lipid; and optionally separating the produced compound from the cultivation broth.

[0032] For the sake of clarity, the expression "cell expresses said beta-1, 6-N-acetylglucosaminyltransferase" refers to the situation wherein the cell expresses the enzyme intracellularly. Likewise, "cell expressing one or more additional glycosyltransferase(s)" refers to the situation wherein the cell expresses the one or more additional glycosyltransferase(s).

[0033] Throughout the application and claims, unless specified otherwise, the verbs "cultivate" (and its conjugations) and "culture" are interchangeably used in the context of the present invention. Said "cultivate" also comprises fermentation as understood by the skilled person.

[0034] Throughout the application and claims, unless explicitly stated otherwise, the terms "synthesize", "synthesized" and "synthesis" are interchangeably used with the features "produce", "produced" and "production", respectively.

[0035] Preferably, the method according to the invention as described herein results in the production of at least 10 g / L, preferably at least 25 g / L, more preferably at least 50 g / L, even more preferably at least 75 g / L, even more preferably at least 90 g / L, most preferably at least 100 g / L, of the compound according to the invention in the whole broth or in the supernatant.

[0036] In this context, it is preferred to cultivate said cell of the invention in a fermentation process. Hence, it is particularly preferred that a method for the production of a compound comprising N-acetylglucosamine- beta-l,6-galactose-beta-l,4-Zi-Z2-R as described herein is a method for the fermentative production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R. In other words, the expression "method for the production of a compound comprising N-acetylglucosamine-beta-1,6- galactose-beta-l,4-Zi-Z2-R" is preferably replaced with "method for the fermentative production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R".

[0037] In this context, it is preferred that said cell is selected from a list consisting of a microorganism, a plant cell, an animal cell, an algal cell, an insect cell and a protozoan cell, preferably said cell is a microorganism, more preferably said cell is a bacterium, fungus or yeast, even more preferably said cell is a bacterium, even more preferably said cell is a bacterium belonging to the genus of Escherichia or Bacillus, even more preferably said cell is a bacterium belonging to the genus of Escherichia, even more preferably said cell is Escherichia coli, even more preferably said cell is an Escherichia coli K-12 strain, most preferably said cell is Escherichia coli MG1655.

[0038] In this context, it is also preferred that said cell comprises a nucleic acid encoding said beta-1, 6-N- acetylglucosaminyltransferase as described herein and preferably as described in the Section "Beta-1, 6- N-acetylglucosaminyltransferase". Said nucleic acid is integrated into the genome of the cell or is present within a plasmid. In the context of the present invention, more than one nucleic acid encoding a beta-1, 6- N-acetylglucosaminyltransferase as described herein can be present in the cell. Hence, a nucleic acid encoding a beta-1, 6-N-acetylglucosaminyltransferase mutant according to the invention is integrated into the genome of the cell and / or is present within a plasmid. Furthermore, in the context of the invention, a cell according to the invention preferably comprises two or more, preferably three or more, nucleic acids encoding the same beta-1, 6-N-acetylglucosaminyltransferase or wherein one or more (preferably all) nucleic acids encode a different beta-1, 6-N-acetylglucosaminyltransferase as described herein. A cell comprising two or more nucleic acids encoding a beta-1, 6-N-acetylglucosaminyltransferase (either the same beta-1, 6-N-acetylglucosaminyltransferase or one or more nucleic acids encode a different beta-1, 6- N-acetylglucosaminyltransferase) is particularly advantageous in a method according to the first aspect of the invention, as the presence of 2 or more nucleic acids increases the expression level of the beta-1, 6-N- acetylglucosaminyltransferase(s) and hence generally increases the yield of the produced compound(s) (it is referred to the Section "Compound").

[0039] In this context, it is also preferred that said cell is an isolated cell. It is further preferred that said cell is a single cell. As understood by the skilled person, a single cell preferably refers to a cell culture derived from the same progenitor cell, i.e. all cells are genetically identical.

[0040] It is particularly preferred that a cell as disclosed in the first aspect of the invention is according to a cell of the second aspect of the invention.

[0041] In an embodiment, said cell according to the invention is cultivated in a suitable cultivation medium to form a cultivation broth and under conditions permissive for the production of said compound.

[0042] In a preferred embodiment, said cell according to the invention is cultivated in a minimal salt medium with a carbon source on which said cell grows. Preferably, the minimal salt medium contains sulphate, phosphate, chloride, ammonium, calcium ion, magnesium ion, sodium ion, potassium ion, iron ion, copper ion, zinc ion, manganese ion, cobalt ion, and / or selenium ion. Common main carbon sources comprise but are not limited to glucose, glycerol, fructose, maltose, lactose, arabinose, malto-oligosaccharides, maltotriose, sorbitol, xylose, rhamnose, sucrose, galactose, mannose, methanol, ethanol, trehalose, starch, cellulose, hemi-cellulose, corn-steep liquor, high-fructose syrup, acetate, citrate, lactate and pyruvate. Preferably, the carbon source is sucrose. With the term "complex medium" is meant a medium for which the exact constitution is not determined. Examples are molasses, corn steep liquor, peptone, tryptone or yeast extract.

[0043] In an additional and / or alternative preferred embodiment, said cultivation medium comprises a precursor saccharide for the synthesis of said compound, preferably wherein said precursor saccharide is lactose or lacto-N-triose II, optionally wherein said lactose or lacto-N-triose II further comprises a fucose. Preferably wherein said fucose is linked to a monosaccharide (preferably selected from the list consisting of glucose, N-acetylglucosamine and galactose, more preferably glucose or N-acetyglucosamine) in an alpha-1,2-, alpha-1,3- or alpha-1, 4-linkage, preferably an alpha-1,2- or an alpha-1, 3-linkage, more preferably an alpha-1, 3-linkage.

[0044] In the context of the present invention, the term "precursor saccharide" refers to a saccharide which lacks at least one monosaccharide compared to the corresponding acceptor (it is particularly referred to the Section "Acceptor" of the first aspect of the invention).

[0045] In another preferred embodiment, lactose is added to the cultivation medium in a concentration, such that throughout the production phase of the cultivation, a lactose concentration of at least 5 mM, preferably at last 10 mM, more preferably at least 15 mM, even more preferably at least 20 mM, even more preferably at least 25 mM, most preferably at least 30 mM is obtained.

[0046] In another preferred embodiment, said cell according to the invention is cultivated for at least 24 hours, preferably at least 36 hours, more preferably at least 48 hours, even more preferably at least 60 hours, even more preferably at least 72 hours, even more preferably at least 84 hours, even more preferably at least 96 hours, most preferably at least 120 hours.

[0047] In a more preferred embodiment, a first phase of exponential cell growth is provided by adding a carbonbased substrate, preferably glucose or sucrose, to the culture medium before the lactose is added to the culture medium in a second phase.

[0048] In an alternative more preferred embodiment, the lactose is added already in the first phase of exponential growth together with the carbon-based substrate.

[0049] In an optional embodiment, a step of separating, preferably purifying (i.e. purification step), said compound from the cultivation broth is present.

[0050] Said separation step, preferably purification step, provides a solution, preferably an aqueous solution, comprising a separated / purified compound.

[0051] In the context of the present invention, the term "separating from said cultivation broth" means harvesting, collecting or retrieving said compound from the cell and / or the medium of its growth.

[0052] In a preferred embodiment, said compound can be separated, preferably purified, in a conventional manner from the aqueous culture medium in which the cell was grown.

[0053] In an additional and / or alternative preferred embodiment, said separation step, preferably purification step, comprises at least one step selected from the list consisting of clarification, ultrafiltration, nanofiltration, reverse osmosis, microfiltration, activated charcoal or carbon treatment, tangential flow high-performance filtration, tangential flow ultrafiltration, affinity chromatography, ion exchange chromatography (such as but not limited to cation exchange, anion exchange, mixed bed ion exchange), hydrophobic interaction chromatography, gel filtration (i.e. size exclusion chromatography) and ligand exchange chromatography. With the exception of size exclusion chromatography, proteins and related impurities are retained by a chromatography medium or a selected membrane.

[0054] In an additional and / or alternative preferred embodiment, said method according to the invention further comprises the step of purifying said compound. Preferably said purifying comprises at least one of the following steps: use of activated charcoal or carbon, use of charcoal, nanofiltration, ultrafiltration or ion exchange, use of alcohols, use of aqueous alcohol mixtures, crystallization, evaporation, precipitation, drying, spray drying or lyophilization.

[0055] In an optional embodiment, a step of drying the cultivation broth obtained from step (a) and / or a step of drying the solution obtained from step (b) is present, preferably a step of drying the solution obtained from step (b) is present. Several drying techniques are known to the skilled person which can be used to obtain a slurry, preferably a solid, more preferably a powder, from a solution containing said compound. A drying step / technique is preferably selected from the list consisting of spray drying, freeze drying, spray freeze-drying, crystallization, lyophilization, band or belt drying, drum or roller drying, and agitated thin film drying, preferably selected from the list consisting of spray drying, drum or roller drying and agitated thin film drying, more preferably agitated thin film drying.

[0056] In the context of the present invention, a method for the production of a compound according to the invention can comprise one or more drying steps. The same or different drying techniques, preferably as disclosed herein, can be used as understood by the skilled person.

[0057] Beta-1, 6-N-; ucosami

[0058] It is particularly preferred that said beta-1, 6-N-acetylglucosaminyltransferase according to the invention is from an eukaryotic origin, i.e. said beta-1, 6-N-acetylglucosaminyltransferase is either naturally present in an eukaryotic cell or it is derived from a beta-1, 6-N-acetylglucosaminyltransferase that is naturally present in an eukaryotic cell. In the context of the invention, the expression "derived from a beta-1, 6-N- acetylglucosaminyltransferase that is naturally present in an eukaryote" refers to a beta-1, 6-N- acetylglucosaminyltransferase consisting of an amino acid sequence that has at least 80.0% sequence identity to the full-length sequence of the beta-1, 6-N-acetylglucosaminyltransferase that is naturally present in an eukaryote. Such beta-1, 6-N-acetylglucosaminyltransferase might be truncated (in the context of the invention, it is particularly preferred to truncate the N-terminus to remove at least 80.0%, preferably at least 85.0%, more preferably at least 90.0%, most preferably 100%, of a membrane domain if present, preferably a transmembrane domain if present) compared to the naturally occurring enzyme; and / or it might contain one or more amino acid substitutions and / or one or more amino acid deletions (amino acid substation is preferred over amino acid deletion) for example to improve expression or activity or to improve recombinant expression of the enzyme. In any case, a beta-1, 6-N- acetylglucosaminyltransferase according to the invention is functional (i.e. active), i.e. capable to transfer a N-acetylglucosamine (GIcNAc) from a suitable donor (preferably UDP-GIcNAc) to a suitable acceptor (it is referred to the Section "Acceptor") in an beta-1, 6-glycosidic linkage as described further herein.

[0059] It is further preferred that said beta-1, 6-N-acetylglucosaminyltransferase according to the invention is not naturally present in a human, more preferably is not from a human origin.

[0060] It is also further preferred that said beta-1, 6-N-acetylglucosaminyltransferase according to the invention is not naturally present in a mouse, more preferably is not from a mouse origin.

[0061] In an optional embodiment of the first aspect of the invention, throughout the application and claims, said beta-1, 6-N-acetylglucosaminyltransferase according to the invention comprises the IPR domain IPR003406 as defined by InterPro 102.0, released on 3rdOctober 2024. Whether or not a given protein fits the criteria of IPR003406 (i.e. glycosyltransferase family 14 = GT14) can be readily assessed in the public Interpro database 102.0, released on 3rdOctober 2024 or InterProScan version (5.70-102.0) as released on 3rdOctober 2024. The database and InterProScan are accessible through the link https: / / www.ebi.ac.uk / interpro (Paysan-Lafosse et al, 2022, Nucleic Acids Research 51(D1): D418-D427). The content of the database is fixed at each release. When the content of the database is changed, a new release version with a new release date is issued or one can access the content of the database as it was on the release date.

[0062] In a preferred embodiment of the first aspect of the invention, said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 238 to 472; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full- length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, and wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively.

[0063] Throughout the application and claims, the expression "list consisting of SEQ ID NO 238 to 472" is preferably replaced with "list consisting of SEQ ID NO 238 to 252", more preferably replaced with "list consisting of SEQ ID NO 238 to 248", even more preferably replaced with "list consisting of SEQ ID NO

[0064] 238, 239, 240, 241 and 242", even more preferably replaced with "SEQ ID NO 238 or 239", most preferably with "SEQ ID NO 238". In other words, in this context of the invention, throughout the application and claims, SEQ ID NO 238 to 252 are preferred; SEQ ID NO 238 to 248 are more preferred; SEQ ID NO 238,

[0065] 239, 240, 241 and 242 are even more preferred; SEQ ID NO 238 and 239 are even more preferred; and SEQ ID NO 238 is most preferred.

[0066] For the sake of clarity, "list consisting of SEQ ID NO 238 to 472" refers to a list consisting of SEQ ID NO 238, 239, 240, 241, 242, 243, 244, 245, 246, 247, 248, 249, 250, 251, 252, 253, 254, 255, 256, 257, 258,

[0067] 259, 260, 261, 262, 263, 264, 265, 266, 267, 268, 269, 270, 271, 272, 273, 274, 275, 276, Til , 278, 279,

[0068] 280, 281, 282, 283, 284, 285, 286, 287, 288, 289, 290, 291, 292, 293, 294, 295, 296, 297, 298, 299, 300,

[0069] 301, 302, 303, 304, 305, 306, 307, 308, 309, 310, 311, 312, 313, 314, 315, 316, 317, 318, 319, 320, 321,

[0070] 322, 323, 324, 325, 326, 327, 328, 329, 330, 331, 332, 333, 334, 335, 336, 337, 338, 339, 340, 341, 342,

[0071] 343, 344, 345, 346, 347, 348, 349, 350, 351, 352, 353, 354, 355, 356, 357, 358, 359, 360, 361, 362, 363,

[0072] 364, 365, 366, 367, 368, 369, 370, 371, 372, 373, 374, 375, 376, 377, 378 379, 380, 381, 382, 383, 384, 385, 386, 387, 388, 389, 390, 391, 392, 393, 394, 395, 396, 397, 398, 399, 400, 401, 402, 403, 404, 405,

[0073] 406, 407, 408, 409, 410, 411, 412, 413, 414, 415, 416, 417, 418, 419, 420, 421, 422, 423, 424, 425, 426,

[0074] 427, 428, 429, 430, 431, 432, 433, 434, 435, 436, 437, 438, 439, 440, 441, 442, 443, 444, 445, 446, 447,

[0075] 448, 449, 450, 451, 452, 453, 454, 455, 456, 457, 458, 459, 460, 461, 462, 463, 464, 465, 466, 467, 468,

[0076] 469, 470, 471 and 472.

[0077] In the context of the present invention, "% sequence identity" refers to the percentage of amino acids of an amino acid sequence that match exactly the amino acids of the reference amino acid sequence (e.g. SEQ ID NO 238) over the full-length of the reference sequence. For the sake of clarity, in the expression (or similar expression) "amino acid sequence 1 having at least 80.0% sequence identity with the full-length amino acid sequence represented by SEQ ID NO 238", the reference sequence is SEQ ID NO 238. In other words, said expression means that amino acid sequence 1 has to have at least 80.0% sequence identity with SEQ ID NO 238 over the full-length of said SEQ ID NO 238.

[0078] For the purpose of this invention, the overall sequence identity of a protein is preferably determined by the program EMBOSS Needle 5.0 (https: / / galaxy-iuc.github.io / emboss-5.0-docs / needle.html); preferably wherein the substitution matrix is BLOSUM62, the gap opening penalty 11, and the gap extension penalty 1).

[0079] Throughout the application and claims, "at least 80.0% sequence identity" is preferably replaced with "at least 82.5% sequence identity", more preferably with "at least 85.0% sequence identity", even more preferably with "at least 87.5% sequence identity", even more preferably with "at least 90.0% sequence identity, even more preferably with "at least 92.5% sequence identity", even more preferably with "at least 95.0% sequence identity", most preferably with "at least 97.5% sequence identity". Likewise, "at least 82.5% sequence identity" is preferably replaced with "at least 85.0% sequence identity", more preferably with "at least 87.5% sequence identity", even more preferably with "at least 90.0% sequence identity, even more preferably with "at least 92.5% sequence identity", even more preferably with "at least 95.0% sequence identity", most preferably with "at least 97.5% sequence identity". Likewise, "at least 85.0% sequence identity" is preferably replaced with "at least 87.5% sequence identity", more preferably with "at least 90.0% sequence identity", even more preferably with "at least 92.5% sequence identity, even more preferably with "at least 95.0% sequence identity", most preferably with "at least 97.5% sequence identity". Etc.

[0080] In the context of the present invention, when an amino acid sequence has no 100.0% sequence identity to the full-length reference amino acid sequence (e.g. any one of SEQ ID NO 03 to 472), then it is particularly preferred that the sequence difference is solely due to conservative amino acid substitution(s). The term "conservative amino acid substitution" refers to the substitution of an amino acid by another structurally-related amino acid, i.e. an amino acid having a side-chain with similar physicochemical properties. In the context of the present invention, throughout the application and claims, the amino acid classification system according to IMGT (ImMunoGeneTics) is used (Pommie et al, 2004, J. Mol. Recognit. 17(1): p. 17-32). The classification of the 20 common amino acids according to IMGT consists of several standardized classes that have been defined by the properties of their side chains (hydropathy, volume, chemical, charge, hydrogen donor or acceptor atoms, and polarity). Accordingly, a conservative amino acid substitution is preferably the substitution of an amino acid from one IMGT class to another amino acid from the same IMGT class. Preferably, said IMGT class is hydrophobic class, neutral hydropathy class, hydrophilic class, positively charged class, uncharged class, negatively charged class, polar class, non-polar class or aromatic class.

[0081] Accordingly, in the context of the present invention, a conservative amino acid substitution is more preferably the substitution of: an aromatic amino acid (i.e. W, Y, F) by another aromatic amino acid (i.e. W, Y, F); a polar amino acid (i.e. R, N, D, Q, E, H, K, S, T, Y) by another polar amino acid (i.e. R, N, D, Q, E, H,

[0082] K, S, T, Y); a non-polar amino acid (i.e. A, C, G, I, L, M, F, P, W, V) by another non-polar amino acid (i.e. A, C, G, I, L, M, F, P, W, V); a hydrophobic amino acid (i.e. I, V, L, F, C, M, A, W) by another hydrophobic amino acid (i.e. I, V,

[0083] L, F, C, M, A, W); a hydrophilic amino acid (i.e. N, D, Q, E, K, R) by another hydrophilic amino acid (i.e. N, D, Q, E, K, R); an amino acid with neither a hydrophobic nor hydrophilic side chain (i.e. G, T, S, Y, P, H) by another amino acid with neither a hydrophobic nor hydrophilic side chain (i.e. G, T, S, Y, P, H); an amino acid with a positively charged side chain at physiological pH (i.e. R, H, K) by another amino acid with a positively charged side chain at physiological pH (i.e. R, H, K); an amino acid with a negatively charged side chain at physiological pH (i.e. D, E) by another amino acid with a negatively charged side chain at physiological pH (i.e. D, E), or an amino acid with a neutral side chain at physiological pH (i.e. A, N, C, Q, G, I, L, M, F, P, S, T, W Y, V) by another amino acid with an uncharged side chain at physiological pH (A, N, C, Q, G, I, L,

[0084] M, F, P, S, T, W, Y, V).

[0085] As understood by the skilled person, "a hydrophobic amino acid" refers to an amino acid having a hydrophobic side chain. Said hydrophobic amino acid is I, V, L, F, C, M, A or W (ranked from most hydrophobic, i.e. I, to least hydrophobic, i.e. W).

[0086] As understood by the skilled person, "a hydrophilic amino acid" refers to an amino acid having a hydrophilic side chain. Said hydrophilic amino acid is R, K, E, Q, D or N (ranked from most hydrophilic, i.e. R, to least hydrophilic, i.e. N).

[0087] In the context of the present invention, the terms "amino acid with a negatively charged side chain at physiological pH" and "negatively charged amino acid" are used interchangeably herein. Likewise, the terms "amino acid with a positively charged side chain at physiological pH" are used interchangeably herein. Likewise, the terms "amino acid with a neutral side chain at physiological pH" and "uncharged amino acid" are used interchangeably herein.

[0088] The term "neutral amino acid" can refer to an amino acid having neither a hydrophobic nor a hydrophilic side chain in the context of the property "hydropathy"; or can refer to an amino acid having a neutral side chain at physiological pH in the context of the property "charge" as disclosed herein. For clarity reasons, in the context of the present invention, unless specifically stated otherwise, "neutral amino acid" refers to an amino acid having neither a hydrophobic nor a hydrophilic side chain, whereas "uncharged amino acid" refers to an amino acid having a neutral side chain at physiological pH.

[0089] For the sake of clarity, a "functional" fragment of a protein (e.g. beta-1, 6-N- acetylglucosaminyltransferase) is functional (i.e. active), i.e. capable to transfer a N-acetylglucosamine (GIcNAc) from a suitable donor (preferably UDP-GIcNAc) to a suitable acceptor (it is referred to the Section "Acceptor") in an beta-1, 6-glycosidic linkage as described further herein, preferably to a similar or greater extent (i.e. similar or greater activity) as can be routinely assessed by the skilled person as described further herein. Further, a functional "fragment" of a protein (e.g. beta-1, 6-N- acetylglucosaminyltransferase) represented by a SEQ ID NO (e.g. any one of SEQ ID NO 03 to 472) refers to a polypeptide sequence which comprises or consists of an amount of consecutive amino acid residues from said protein represented by a SEQ ID NO and wherein said amount of consecutive amino acid residues is preferably at least 70.0%, preferably at least 75.0%, more preferably at least 80.0%, even more preferably at least 85.0%, even more preferably at least 87.5%, even more preferably at least 90.0%, even more preferably at least 92.5%, most preferably at least 95.0%, of the full-length of said protein represented by a SEQ ID NO. As such, a functional fragment of a protein (e.g. beta-1, 6-N- acetylglucosaminyltransferase) represented by a SEQ ID NO (e.g. SEQ ID NO 03, 04, 05, 06, 07, 08, 09, 10, 11, 12, 13, 14, 15, 16 or 17) refers to a polypeptide sequence which comprises or consists of said protein represented by a SEQ ID NO, wherein an amount of consecutive amino acid residues is missing (preferably said amount of consecutive amino acid residues have been removed by engineering said protein, more preferably by genetically engineering the nucleotide sequence encoding for said protein) and wherein said amount is preferably no more than 30.0%, more preferably no more than 25.0%, even more preferably no more than 20.0 %, more preferably no more than 15.0 %, even more preferably no more than 12.5%, even more preferably no more than 10.0 %, even more preferably no more than 7.5%, most preferably no more than 5.0%, of the full-length of said protein represented by a SEQ ID NO.

[0090] Throughout the application and claims, "at least 70.0% of the length of SEQ ID NO" is preferably replaced with "at least 75.0% of the length of SEQ ID NO", more preferably with "at least 80.0% of the length of SEQ ID NO", even more preferably with "at least 85.0% of the length of SEQ ID NO", even more preferably with "at least 87.5% of the length of SEQ ID NO", even more preferably with "at least 90.0% of the length of SEQ ID NO", even more preferably with "at least 92.5% of the length of SEQ ID NO", most preferably with "at least 95.0% of the length of SEQ ID NO". Likewise, "at least 75.0% of the length of SEQ ID NO" is preferably replaced with "at least 80.0% of the length of SEQ ID NO", more preferably with "at least 85.0% of the length of SEQ ID NO", even more preferably with "at least 87.5% of the length of SEQ ID NO", even more preferably with "at least 90.0% of the length of SEQ ID NO", even more preferably with "at least 92.5% of the length of SEQ ID NO", most preferably with "at least 95.0% of the length of SEQ ID NO". Likewise, "at least 80.0% of the length of SEQ ID NO" is preferably replaced with "at least 85.0% of the length of SEQ ID NO", more preferably with "at least 87.5% of the length of SEQ ID NO", even more preferably with "at least 90.0% of the length of SEQ ID NO", even more preferably with "at least 92.5% of the length of SEQ ID NO", most preferably with "at least 95.0% of the length of SEQ ID NO". Etc.

[0091] For the sake of clarity, "a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively" is to be understood as follows: a functional fragment of SEQ ID NO 372 has a length of at least 70.0% of the length of SEQ ID NO 372; a functional fragment of SEQ ID NO 238 has a length of at least 70.0% of the length of SEQ ID NO 238; a functional fragment of SEQ ID NO 472 has a length of at least 70.0% of the length of SEQ ID NO 472; etc. In the context of the present invention, a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472 as disclosed herein is preferably a protein that is at least (preferably only) truncated at its N-terminus compared to the full-length protein represented by any one of SEQ ID 238 to 472, respectively. Such truncation is particularly beneficial for expression of the protein in a suitable host, in particular if said truncation removes at least 70.0%, preferably at least 75.0%, more preferably at least 80.0%, most preferably all (i.e. 100%), of the amino acids that are part of a membrane domain (preferably a transmembrane domain), if present in the full-length protein represented by any one of SEQ ID 238 to 472, respectively. Preferably, said N-truncation does not remove more than 10, preferably 5, amino acids C -terminally of said membrane domain (preferably said transmembrane domain). A membrane domain (preferably a transmembrane domain) typically consists of 15 to 25 consecutive amino acids and its presence in a protein can be predicted by routinely available software as known to the skilled person. An example is PROTEUS Structure Prediction Server 2.0 (Montgomerie et al, 2008, Nucleic Acids Res. 36 (web server issue): W202-W209). Here, amino acids are indicated with "T" in case said amino acids are involved in a membrane helix. Another example is DeepTMHMM which is a deep learning protein language modelbased algorihm that detects and predicts the topology of both alpha helical and beta barrels proteins (Hallgren et al, 2022, bioRxiv, "DeepTMHMM predicts alpha and beta (trans)membrane proteins using deep neural networks").

[0092] Hence, it is a particularly preferred embodiment of the first aspect of the invention that said beta-1, 6-N- acetylglucosaminyltransferase according to the invention comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 238 to 472; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, wherein (i) the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively, and (ii) when the full-length protein represented by any one of SEQ ID NO 238 to 472, respectively, comprises a membrane domain (preferably a transmembrane domain) then said functional fragment is truncated at its N- terminus to such extent that at least 70.0% (preferably at least 75.0%, more preferably at least 80.0%, most preferably 100%) of said membrane domain (preferably said transmembrane domain) is absent compared to said full-length protein; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full- length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, and wherein (i) the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively, and (ii) when said polypeptide having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively, comprises a membrane domain (preferably a transmembrane domain) then said functional fragment is truncated at its N- terminus to such extent that at least 70.0% (preferably at least 75.0%, more preferably at least 80.0%, most preferably 100%) of said membrane domain (preferably said transmembrane domain) is absent compared to said polypeptide having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively.

[0093] Hence, it is a particularly more preferred embodiment of the first aspect of the invention that said beta- 1,6-N-acetylglucosaminyltransferase according to the invention comprises an amino acid sequence: a) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, wherein (i) the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively, and (ii) when the full-length protein represented by any one of SEQ ID NO 238 to 472, respectively, comprises a membrane domain (preferably a transmembrane domain) then said functional fragment is truncated at its N- terminus to such extent that at least 70.0% (preferably at least 75.0%, more preferably at least 80.0%, most preferably 100%) of said membrane domain (preferably said transmembrane domain) is absent compared to said full-length protein; or b) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full- length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, and wherein (i) the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively, and (ii) when said polypeptide having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively, comprises a membrane domain (preferably a transmembrane domain) then said functional fragment is truncated at its N- terminus to such extent that at least 70.0% (preferably at least 75.0%, more preferably at least 80.0%, most preferably 100%) of said membrane domain (preferably said transmembrane domain) is absent compared to said polypeptide having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively.

[0094] Further, it is preferred that the amino acid sequence of a functional fragment as disclosed herein starts with a methionine (M).

[0095] For each beta-1, 6-N-acetylglucosaminyltransferase represented by any one of SEQ ID NO 238 to 472, a particularly preferred functional fragment in the context of the present invention (i.e. truncation at N- terminus if a membrane domain, preferably if a transmembrane domain, is present in the corresponding full-length protein; and starting with a methionine) is provided in Table 1 (with the exception for the beta- 1,6-N-acetylglucosaminyltransferase represented with SEQ ID NO 254, 259, 263, 265, 269 or 302). For example, SEQ ID NO 03 is a preferred functional fragment of SEQ ID NO 238; SEQ ID NO 04 is a preferred functional fragment of SEQ ID NO 239; SEQ ID NO 05 is a preferred functional fragment of SEQ ID NO 240; SEQ ID NO 06 is a preferred functional fragment of SEQ ID NO 241; etc.

[0096] In a more preferred embodiment of the first aspect of the invention, said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237, wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full- length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237, and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively.

[0097] Throughout the application and claims, the expression "list consisting of SEQ ID NO 03 to 237" is preferably replaced with "list consisting of SEQ ID NO 03 to 17", more preferably replaced with "list consisting of SEQ ID NO 03 to 13", even more preferably replaced with "list consisting of SEQ ID NO 03, 04, 05, 06 and 07", even more preferably replaced with "SEQ ID NO 03 or 04", most preferably with "SEQ ID NO 03". In other words, in this context of the invention, throughout the application and claims, SEQ ID NO 03 to 17 are preferred; SEQ ID NO 03 to 13 are more preferred; SEQ ID NO 03, 04, 05, 06 and 07 are even more preferred; SEQ ID NO 03 and 04 are even more preferred; and SEQ ID NO 03 is most preferred. For the sake of clarity, "list consisting of SEQ ID NO 03 to 237" refers to a list consisting of SEQ ID NO 03, 04, 05, 06, 07, 08, 09, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 , 28, 29, 30, 31, 32,

[0098] 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61,

[0099] 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90,

[0100] 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114,

[0101] 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135,

[0102] 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156,

[0103] 157, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 173, 174, 175, 176, 177,

[0104] 178, 179, 180, 181, 182, 183, 184, 185, 186, 187, 188, 189, 190, 191, 192, 193, 194, 195, 196, 197, 198,

[0105] 199, 200, 201, 202, 203, 204, 205, 206, 207, 208, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, 219,

[0106] 220, 221, 222, 223, 224, 225, 226, 227, 228, 229, 230, 231, 232, 233, 234, 235, 236 and 237.

[0107] For the sake clarity, the expression "a beta-1, 6-N-acetylglucosaminyltransferase comprises an amino acid sequence" means that the beta-1, 6-N-acetylglucosaminyltransferase consists of said amino acid sequence or consists of said amino acid sequence and one or more additional amino acid residues. It is noted that the first amino acid of any one of SEQ ID NO 03 to 237 starts with a methionine (M). When the beta-1, 6- N-acetylglucosaminyltransferase comprises additional amino acids at the N-terminus of any one of said SEQ ID NO 03 to 237, then it is preferred that the first amino acid (i.e. M) of any one of SEQ ID NO 03 to 237 is replaced with another amino acid, preferably leucine (L).

[0108] For the sake of clarity, "a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237, wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively" is to be understood as follows: a functional fragment of SEQ ID NO 03 has a length of at least 80.0% of the length of SEQ ID NO 03; a functional fragment of SEQ ID NO 04 has a length of at least 80.0% of the length of SEQ ID NO 04; a functional fragment of SEQ ID NO 05 has a length of at least 80.0% of the length of SEQ ID NO 05; etc.

[0109] Further, it is preferred that the amino acid sequence of a functional fragment as disclosed herein starts with a methionine (M).

[0110] In an even more preferred embodiment of the first aspect of the invention, said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237 , wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237 , respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full- length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237 , and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237 , respectively.

[0111] Further, it is preferred that the amino acid sequence of a functional fragment as disclosed herein starts with a methionine (M).

[0112] In an even more preferred embodiment of the first aspect of the invention, said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237.

[0113] In another preferred embodiment of the first aspect of the invention, said beta-1, 6-N- acetylglucosaminyltransferase according to the invention is functional (i.e. active), i.e. capable to transfer a N-acetylglucosamine (GIcNAc) from a suitable donor (preferably UDP-GIcNAc) to a suitable acceptor (it is referred to the Section "Acceptor") in an beta-1, 6-glycosidic linkage. The terms "functional" and "active" can be used interchangeable herein.

[0114] The skilled person can readily assess whether a beta-1, 6-N-acetylglucosaminyltransferase is active or not by bringing it into contact with a suitable donor (preferably UDP-GIcNAc) and a suitable acceptor (it is referred to the Section "Acceptor") under conditions suitable for the transfer of GIcNAc from said donor to said acceptor saccharide. Said acceptor is preferably an oligosaccharide (in other words R is preferably absent), i.e. said acceptor comprises galactose-beta-l,4-Zi-Zz, more preferably comprises N- acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-Z2, even more preferably comprises galactose-beta-N- acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-Z2, most preferably comprises galactose-beta-l,4-N- acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-Z2; wherein Zi is glucose or N-acetylglucosamine (GIcNAc) and wherein Z2 is absent or is a saccharide (preferably wherein Z2 is absent). A particularly suitable acceptor to assess whether a beta-1, 6-N-acetylglucosaminyltransferase is active or not is lacto- N-neotetraose, i.e. galactose-beta-l,4-N-acetylglucosamine-beta-l,3-galactose-beta-l,4-glucose.

[0115] A cellular method or a cell-free method (e.g. enzymatic method) are suitable. Suitable conditions include a pH of 6.0-9.0 (optimal pH range is 6.5-8.0, wherein pH 7.0 is most preferred) and a temperature of 20- 50°C (optimal temperature is 30-37°C). Further, the presence of Mn2* is not required (in contrast to a beta-1, 3-N-acetylglucosaminyltransferase), but the presence of Zn2+and Cu2+should be avoided. In the context of the invention, a beta-1, 6-N-acetylglucosaminyltransferase is active when at least 10.0 %, preferably at least 20.0%, more preferably at least 25.0%, even more preferably at least 50.0% of the acceptor is modified by the enzyme (i.e. is modified by the addition of a GIcNAc in a beta-1, 6-linkage).

[0116] In another preferred embodiment, said beta-1, 6-N-acetylglucosaminyltransferase according to the invention consists of at least 300, preferably at least 310, more preferably at least 320, even more preferably at least 330, even more preferably at least 340, most preferably at least 350, amino acids. Further, it is preferred that said beta-1, 6-N-acetylglucosaminyltransferase according to the invention consists of < 500, preferably < 490, more preferably < 480, even more preferably < 470, even more preferably < 460, even more preferably < 450, even more preferably < 440, even more preferably < 430, even more preferably < 420, even more preferably < 410, most preferably < 410, amino acids.

[0117] In an optional embodiment of the first aspect of the invention, throughout the application and claims, said beta-1, 6-N-acetylglucosaminyltransferase according to the invention further comprises a tag. As familiar to the skilled person, a tag can be useful for improving the solubility of a protein, allowing detection of a protein and / or facilitating purification of a protein (e.g. affinity tag). A tag can be present at the N-terminus of a protein. A tag can be present at the C-terminus of a protein. In the context of the invention, it is preferred that a tag, if any, is present at the N-terminus of the beta-1, 6-N- acetylglucosaminyltransferase. Numerous examples of such tags are known to the skilled person. It is for example referred to Table 9.9.1 of Kimple et al, 2013, Curr. Protoc. Protein Sci. 73: Unit-9.9 (said table is incorporated by reference herein). A preferred tag is a His tag.

[0118] For the sake of clarity, the expression "beta-1, 6-N-acetylglucosaminyltransferase further comprises a tag" refers to the situation wherein a tag is attached to a beta-1, 6-N-acetylglucosaminyltransferase as disclosed in the first aspect of the invention. In other words, a tag is not to be considered as a part of the beta-1, 6-N-acetylglucosaminyltransferase itself but as an extra element that can be bound to the enzyme. It is in this regard also referred to the Examples wherein a beta-1, 6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03, 04, 05, 06, 07, 08, 09, 10, 11, 12, 13, 14, 15, 16 or 17 is further modified with a His tag at the N-terminus.

[0119] In another preferred embodiment of the first aspect of the invention, and particularly preferred, said beta-1, 6-N-acetylglucosaminyltransferase comprises a domain represented by SEQ ID NO 01, i.e. R(X)io-2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE; wherein X is any amino acid; Xi is any amino acid except for F and P; X2is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, Xg is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y and Xg is any amino acid except for A; and wherein: (i) the first amino acid of SEQ ID NO 01 (i.e. R) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R199 of the reference beta- 1,6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03;

[0120] (ii) XsXgXyXg of SEQ ID NO 01 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with G234-T235-A236-Y237 of the reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and

[0121] (iii) the last two amino acids of SEQ ID NO 01 (i.e. DE) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with D268-E269 of the reference beta-1, 6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03.

[0122] In other words, said beta-1, 6-N-acetylglucosaminyltransferase comprises a domain represented by SEQ ID NO 01, i.e. R(X)IO-2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE; wherein X is any amino acid; Xi is any amino acid except for F and P; X2is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, Xg is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y and Xg is any amino acid except for A; and wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises (i) R (i.e. first amino acid of SEQ ID NO 01) relative to position R199 of SEQ ID NO 03, (ii) XgXgXyXg relative to positions G234-T235-A236-Y237 of SEQ ID NO 03, and (iii) DE (last two amino acids of SEQ ID NO 01) relative to positions D268-E269 of SEQ ID NO 03.

[0123] In a more preferred embodiment, said beta-1, 6-N-acetylglucosaminyltransferase comprises a domain represented by SEQ ID NO 02, i.e. R(X)io-2oXiXXXXXXX2XXX3XXXXX4XXXXXX5XgX7X8XXX9(X)2o-goDE(X)2o- 40RXXXWXX10X11; wherein X is any amino acid; Xi is any amino acid except for F and P; X2is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, Xg is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y; Xg is any amino acid except for A; X10 is E or D; and Xn is any amino acid except for F, Y, W, H, R and K; and wherein:

[0124] (i) the first amino acid of SEQ ID NO 02 (i.e. R) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R199 of the reference beta- 1,6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03; and

[0125] (ii) X5XgX7X8 of SEQ ID NO 02 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with G234-T235-A236-Y237 of the reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and

[0126] (iii) DE of SEQ ID NO 02 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with D268-E269 of the reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and

[0127] (iv) RXXXWXXIOXH of SEQ ID NO 02 should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R295-A296-V297-K298-W299- I300-D301-M302 of the reference beta-1, 6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03. In other words, said beta-1, 6-N-acetylglucosaminyltransferase comprises a domain represented by SEQ ID NO 02, i.e. R(X)IO-2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE(X)2O-4ORXXXWXXIOXII; wherein X is any amino acid; Xi is any amino acid except for F and P; X2is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, X6is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y; X9is any amino acid except for A; Xw is E or D; and Xn is any amino acid except for F, Y, W, H, R and K; and wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises (i) R (i.e. first amino acid of SEQ ID NO 02) relative to position R199 of SEQ ID NO 03, (ii) X5X6X7X8 relative to positions G234-T235-A236-Y237 of SEQ ID NO 03, (iii) DE relative to positions D268-E269 of SEQ ID NO 03, and (iv) RXXXWXXIOXH relative to positions R295-A296-V297-K298-W299-I300-D301-M302 of SEQ ID NO 03.

[0128] For the sake of clarity, the term "align" can be replaced with the term "correspond with".

[0129] For the sake of clarity, SEQ ID NO 03 is designated as a reference beta-1, 6-N- acetylglucosaminyltransferase in this specific context solely for the purpose to correctly align the domain represented by SEQ ID NO 01 or 02 with the beta-1, 6-N-acetylglucosaminyltransferase according to the invention (which includes the beta-1, 6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03). Throughout the application and claims "X" is preferably selected from the list consisting of A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, O, S, U, T, W, Y and V.

[0130] The presence of the domain represented by SEQ ID NO 02 is particularly useful when the acceptor comprises galactose-beta-N-acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-Z2-R, preferably when the acceptor comprises galactose-beta-N-acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-R, most preferably when the acceptor comprises galactose-beta-N-acetylglucosamine-beta-l,3-galactose-beta-

[0131] 1.4-glucose-R; wherein (as disclosed earlier herein) Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid, preferably wherein R is absent.

[0132] It is preferred that said "galactose-beta-N-acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-Z2-R" is replaced with "galactose-beta-l,4-N-acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-Z2-R or galactose- beta-l,3-N-acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-Z2-R", more preferably with "galactose- beta-l,4-N-acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-Z2-R". Likewise, it is preferred that said "galactose-beta-N-acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-R" is replaced with "galactose-beta-

[0133] 1.4-N-acetylglucosamine-beta-l,3-galactose-beta-l,4-Zi-R or galactose-beta-l,3-N-acetylglucosamine- beta-l,3-galactose-beta-l,4-Zi-R", more preferably with "galactose-beta-l,4-N-acetylglucosamine-beta-

[0134] 1.3-galactose-beta-l,4-Zi-R". Likewise, it is preferred that said "galactose-beta-N-acetylglucosamine- beta-l,3-galactose-beta-l,4-glucose-R" is replaced with "galactose-beta-l,4-N-acetylglucosamine-beta-

[0135] 1.3-galactose-beta-l,4-glucose-R or "galactose-beta-l,3-N-acetylglucosamine-beta-l,3-galactose-beta-

[0136] 1.4-glucose-R", more preferably with "galactose-beta-l,4-N-acetylglucosamine-beta-l,3-galactose-beta-

[0137] 1.4-glucose-R".

[0138] It is further referred to the Section "Acceptor" wherein said acceptor is further elaborated. Acceptor

[0139] In an embodiment of the first aspect of the invention, said acceptor comprises galactose-beta-l,4-Zi-Z2- R, wherein:

[0140] Zi is glucose or N-acetylglucosamine (GIcNAc); and

[0141] Z2 is absent or is a saccharide; preferably Z2 is absent or is selected from the list consisting of a monosaccharide, a disaccharide and an oligosaccharide; even more preferably Z2 is absent or is a disaccharide or is an oligosaccharide; most preferably Z2 is absent; and

[0142] R is absent or is selected from the list consisting of a peptide, a protein and a lipid; preferably wherein R is absent.

[0143] As will be apparent for the skilled person in the context of the invention, the beta-1, 6-N- acetylglucosaminyltransferase of the invention transfers a N-acetylglucosamine to the galactose bound at the non-reducing end of Zi of the acceptor, i.e. galactose-beta-l,4-Zi-Z -R (said galactose is underlined). Throughout the application and claims, when Z2 is a disaccharide, it is preferred that Z2 is lactose; when Z2 is an oligosaccharide it is preferred that Z2 is a LNT-containing oligosaccharide or a LNnT-containing oligosaccharide.

[0144] In the context of the present invention, throughout the application and claims, the expression "LNT- containing oligosaccharide" refers to an oligosaccharide that comprises LNT (lacto-N-tetraose) and optionally one or more additional monosaccharide(s). Said monosaccharide(s) is / are preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and N- acetylgalactosamine, even more preferably selected from the list consisting of galactose, fucose and N- acetylglucosamine, most preferably fucose. Preferably, throughout the application and claims, said LNT- containing oligosaccharide is on oligosaccharide comprising LNT at its reducing end.

[0145] Preferably, a LNT-containing oligosaccharide is selected from the list consisting of Lacto-N-tetraose (LNT), Gal-alpha-1, 3-Gal-beta-l,3-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, Lacto-N-pentaose, para-Lacto-N-pentaose, GlcNAc-beta-l,3-Gal-beta-l,3-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, GalNAc-beta-l,3-LNT, Gal-beta-1, 3- GalNAc-beta-l,3-LNT, Lacto-N-hexaose (LNH), para-lacto-N-neohexaose II (pLNnH II), para-lacto-N- hexaose II (pLNH II), lacto-N-heptaose, para lacto-N-heptaose, lacto-N-octaose (LNO), iso lacto-N-octaose, para lacto-N-octaose, iso lacto-N-nonaose, novo lacto-N-nonaose, lacto-N-nonaose, lacto-N-decaose, iso lacto-N-decaose and novo lacto-N-decaose; more preferably selected from the list consisting of Lacto-N- tetraose (LNT), Gal-alpha-1, 3-Gal-beta-l,3-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, Lacto-N-pentaose, para- Lacto-N-pentaose, GlcNAc-beta-l,3-Gal-beta-l,3-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, GalNAc-beta-1,3- LNT, Gal-beta-1, 3-GalNAc-beta-l,3-LNT, Lacto-N-hexaose (LNH), para-lacto-N-neohexaose II (pLNnH II), para-lacto-N-hexaose II (pLNH II), lacto-N-heptaose, para lacto-N-heptaose, lacto-N-octaose (LNO), iso lacto-N-octaose and para lacto-N-octaose; even more preferably selected from the list consisting of Lacto- N-tetraose (LNT), Gal-alpha-1, 3-Gal-beta-l,3-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, Lacto-N-pentaose, para- Lacto-N-pentaose, GlcNAc-beta-l,3-Gal-beta-l,3-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, GalNAc-beta-1,3- LNT, Gal-beta-1, 3-GalNAc-beta-l,3-LNT, Lacto-N-hexaose (LNH), para-lacto-N-neohexaose II (pLNnH II) and para-lacto-N-hexaose II (pLNH II); even more preferably selected from the list consisting of Lacto-N- tetraose (LNT), Gal-alpha-1, 3-Gal-beta-l,3-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, GlcNAc-beta-l,3-Gal-beta- l,3-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, GalNAc-beta-l,3-LNT, Gal-beta-1, 3-GalNAc-beta-l,3-LNT and Lacto-N-hexaose (LNH); even more preferably Lacto-N-tetraose (LNT) or Lacto-N-hexaose (LNH); most preferably LNT; optionally wherein said LNT-containing oligosaccharide further comprises: a fucose, preferably wherein said fucose is linked to a monosaccharide (preferably selected from the list consisting of glucose, N-acetylglucosamine and galactose) in an alpha-1,2-, alpha-1,3- or alpha-1, 4-linkage, preferably an alpha-1,2- or an alpha-1, 3-linkage, more preferably an alpha- 1,3-linkage; and / or a sialic acid, preferably wherein said sialic acid is linked to a monosaccharide (preferably selected from the list consisting of galactose, N-acetylglucosamine and sialic acid, more preferably galactose or N-acetylglucosamine, most preferably galactose) in an alpha-2,3-, alpha-2,4- or alpha-2, 8-linkage, preferably an alpha-2,3- or an alpha-2, 6-linkage, most preferably an alpha- 2,6-linkage.

[0146] It is further preferred that a LNT-containing oligosaccharide is neutral. A "neutral" oligosaccharide as used herein and as generally understood in the state of the art is an oligosaccharide that has no negative charge originating from a carboxylic acid group.

[0147] In the context of the present invention, throughout the application and claims, the expression "LNnT- containing oligosaccharide" refers to an oligosaccharide that comprises LNnT (lacto-N-neotetraose) and optionally one or more additional monosaccharide(s). Said monosaccharide(s) is / are preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and N- acetylgalactosamine, even more preferably selected from the list consisting of galactose, fucose and N- acetylglucosamine, most preferably fucose. Preferably, throughout the application and claims, said LNnT- containing oligosaccharide is on oligosaccharide comprising LNnT at its reducing end.

[0148] Preferably, a LNnT-containing oligosaccharide is selected from the list consisting of Lacto-N-neotetraose (LNnT), Gal-alpha-1, 3-Gal-beta-l,4-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, lacto-N-neopentaose, para-Lacto- N-neopentaose, para-lacto-N-hexaose (pLNH), lacto-N-neohexaose (LNnH), para-Lacto-N-neohexaose (pLNnH), lacto-N-neoheptaose, para lacto-N-neoheptaose, lacto-N-neooctaose, iso lacto-N-neooctaose, novo lacto-N-neooctaose, para lacto-N-neooctaose and lacto-N-neodecaose; more preferably selected from the list consisting of Lacto-N-neotetraose (LNnT), Gal-alpha-1, 3-Gal-beta-l,4-GlcNAc-beta-l,3-Gal- beta-l,4-Glc, lacto-N-neopentaose, para-Lacto-N-neopentaose, para-lacto-N-hexaose (pLNH), lacto-N- neohexaose (LNnH), para-Lacto-N-neohexaose (pLNnH), lacto-N-neoheptaose, para lacto-N- neoheptaose, lacto-N-neooctaose, iso lacto-N-neooctaose, novo lacto-N-neooctaose and para lacto-N- neooctaose; even more preferably selected from the list consisting of Lacto-N-neotetraose (LNnT), Gal- alpha-1, 3-Gal-beta-l,4-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, lacto-N-neopentaose, para-Lacto-N- neopentaose, para-lacto-N-hexaose (pLNH), lacto-N-neohexaose (LNnH) and para-Lacto-N-neohexaose (pLNnH); even more preferably selected from the list consisting of Lacto-N-neotetraose (LNnT), Gal-alpha- l,3-Gal-beta-l,4-GlcNAc-beta-l,3-Gal-beta-l,4-Glc, para-lacto-N-hexaose (pLNH), lacto-N-neohexaose (LNnH) and para-Lacto-N-neohexaose (pLNnH); even more preferably selected from the list consisting of Lacto-N-neotetraose (LNnT), para-lacto-N-hexaose (pLNH), lacto-N-neohexaose (LNnH) and para-Lacto-N- neohexaose (pLNnH); even more preferably Lacto-N-neotetraose (LNnT) or para-Lacto-N-neohexaose (pLNnH); most preferably LNnT; optionally wherein said LNnT-containing oligosaccharide further comprises: a fucose, preferably wherein said fucose is linked to a monosaccharide (preferably selected from the list consisting of glucose, N-acetylglucosamine and galactose) in an alpha-1,2-, alpha-1,3- or alpha-1, 4-linkage, preferably an alpha-1,2- or an alpha-1, 3-linkage, more preferably an alpha- 1,3-linkage; and / or a sialic acid, preferably wherein said sialic acid is linked to a monosaccharide (preferably selected from the list consisting of galactose, N-acetylglucosamine and sialic acid, more preferably galactose or N-acetylglucosamine, most preferably galactose) in an alpha-2,3-, alpha-2,4- or alpha-2, 8-linkage, preferably an alpha-2,3- or an alpha-2, 6-linkage, most preferably an alpha-2, 6- linkage.

[0149] It is further preferred that a LNnT-containing oligosaccharide is neutral. A "neutral" oligosaccharide as used herein and as generally understood in the state of the art is an oligosaccharide that has no negative charge originating from a carboxylic acid group.

[0150] In a preferred embodiment, said acceptor comprises GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R, wherein Zi, Z2 and R are as defined earlier herein.

[0151] The expression "acceptor comprises GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R" refers to an acceptor that comprises GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R and optionally one or more additional monosaccharide(s). Said monosaccharide(s) is / are preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and sialic acid, even more preferably selected from the list consisting of galactose, fucose and sialic acid, most preferably selected from the list consisting of galactose and fucose. Said optional additional monosaccharide(s) is / are preferably bound to the terminal GIcNAc of said acceptor (i.e. GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z -R) and / or bound to Zi (i.e. GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R). As the skilled person understands, when 2 additional monosaccharides are bound to the terminal GIcNAc, each of said monosaccharides can form a glycosidic bond with the terminal GIcNAc or one of said monosaccharides forms a glycosidic bond with the terminal GIcNAc whereas the other monosaccharide forms a glycosidic bond with the first additional monosaccharide.

[0152] An example of the former situation is lacto-N-fucopentaose II (LNFP-II) that comprises GlcNAc-beta-1,3- galactose-beta-l,4-glucose and an additional galactose and fucose bound to the terminal GIcNAC, i.e. Fucose-alpha-l,4-(galactose-beta-l,3-)GlcNAc-beta-l,3-galactose-beta-l,4-glucose; wherein the underlined GIcNAc is the terminal GIcNAc of the acceptor, whereas the monosaccharides in bold are the additional monosaccharides bound to the terminal GIcNAc of the acceptor.

[0153] An example of the latter is lacto-sialyl tetrasaccharide c (LSTc) that comprises GlcNAc-beta-l,4-galactose- beta-l,4-glucose and an additional galactose and sialic acid bound to the terminal GIcNAC, i.e. Neu5Ac- alpha-2,6-galactose-beta-l,4-GlcNAc-beta-l,3-galactose-beta-l,4-glucose; wherein the underlined GIcNAc is the terminal GIcNAc of the acceptor, whereas the monosaccharides in bold are the additional monosaccharides bound to the terminal GIcNAc of the acceptor.

[0154] As will be apparent for the skilled person and within the context of the invention, the beta-1, 6-N- acetylglucosaminyltransferase of the invention transfers a N-acetylglucosamine to the galactose bound at the non-reducing end of Zi of the acceptor, i.e. GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z;>-R (said galactose is underlined).

[0155] In a more preferred embodiment, said acceptor comprises galactose-beta-GlcNAc-beta-l,3-galactose- beta-l,4-Zi-Zz-R, preferably comprises galactose-beta-l,4-GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R or galactose-beta-l,3-GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R, most preferably comprises galactose- beta-l,4-GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R; wherein Zi, Z2 and R are as defined earlier herein.

[0156] The expression "acceptor comprises galactose-beta-GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R" refers to an acceptor that comprises galactose-GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R and optionally one or more additional monosaccharide(s). Said monosaccharide(s) is / are preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and sialic acid, even more preferably selected from the list consisting of fucose, N-acetyglucosamine and sialic acid, most preferably selected from the list consisting of fucose and sialic acid. Said optional additional monosaccharide(s) is / are preferably bound to the terminal galactose of said acceptor (i.e. galactose-beta- GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R) and / or bound to the GIcNAC (i.e. galactose-beta-GIcNAc- beta-l,3-galactose-beta-l,4-Zi-Z2-R) and / or bound to Zi (i.e. galactose-beta-GlcNAc-beta-l,3-galactose- beta-l,4-Zi-Z2-R). As the skilled person understands, when 2 additional monosaccharides are bound to the terminal galactose, each of said monosaccharides can form a glycosidic bond with the terminal galactose or one of said monosaccharides forms a glycosidic bond with the terminal galactose whereas the other monosaccharide forms a glycosidic bond with the first additional monosaccharide. An example of the former situation is Neu5Ac-alpha2,3-(fucose-alpha-l,2-)galactose-beta-l,3-GlcNAc- beta-l,3-galactose-beta-l,4-glucose that comprises galactose-GlcNAc-beta-l,4-galactose-beta-l,4- glucose and an additional fucose and sialic acid bound to the terminal galactose, i.e. Neu5Ac-alpha2,3- (fucose-alpha-l,2-)galactose-beta-l,3-GlcNAc-beta-l,3-galactose-beta-l,4-glucose; wherein the underlined galactose is the terminal GIcNAc of the acceptor, whereas the monosaccharides in bold are the additional monosaccharides bound to the terminal galactose of the acceptor.

[0157] An example of the latter is para-lacto-N-neohexaose (pLNnH) that comprises galactose-GlcNAc-beta-1,4- galactose-beta-l,4-glucose and an additional GIcNAc and galactose bound to the terminal galactose, i.e. galactose-beta-l,4-GlcNAc-beta-l,3-galactose-beta-l,3-GlcNAc-beta-l,3-galactose-beta-l,4-glucose; wherein the monosaccharides in bold are the additional monosaccharides bound to the terminal galactose of galactose-beta-GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R.

[0158] As will be apparent for the skilled person and within the context of the invention, the beta-1, 6-N- acetylglucosaminyltransferase of the invention transfers a N-acetylglucosamine to the galactose bound at the non-reducing end of Zi of the acceptor, i.e. galactose-beta-GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z;>- R (said galactose is underlined).

[0159] It is another preferred embodiment that said acceptor is charged, preferably wherein said acceptor comprises a sialic acid, more preferably wherein said acceptor comprises a sialic acid in an alpha-2, 6- linkage. Throughout the application and claims, "sialic acid" is preferably a nine-carbon sialic acid (i.e. sialic acid having a nine-carbon backbone) or an eight-carbon sialic acid (i.e. sialic acid having an eight- carbon backbone), more preferably a nine-carbon sialic acid. Preferably, said eight-carbon sialic acid is ketodeoxyoctonic acid (KDO; i.e. 2-keto-3-deoxy-D-mannooctanoic acid, also known as 2-oxo-3-deoxy-D- mannooctonic acid, 3-deoxy-D-manno-oct-2-ulosonic acid, 3-deoxy-D-manno-2-octulosonic acid or 3- deoxy-D-manno-Oct-2-ulo-Pyranosonic acid). Preferably, said nine-carbon sialic acid is selected from the list consisting of Neu5Ac; Neu4Ac; Neu4,5Ac2; Neu5,7Ac2; Neu5,8Ac2; Neu5,9Ac2; Neu4,5,9Ac3; Neu5,7,9Ac3; Neu5,8,9Ac3; Neu4,5,7,9Ac4; Neu5,7,8,9Ac4, Neu4,5,7,8,9Ac5 and Neu5Gc; more preferably said nine-carbon sialic acid is N-acetylneuraminic acid (i.e. Neu5Ac). Hence, throughout the application and claims, the term "sialic acid" is most preferably replaced with "Neu5Ac" (N- acetylneuraminate and N-acetylneuraminic acid are interchangeably used for Neu5Ac).

[0160] It is another preferred embodiment, in particular in the context of the present invention, that said acceptor is a mammalian milk oligosaccharide (MMO), optionally bound to R, wherein R is as defined earlier herein; most preferably wherein said acceptor is a mammalian milk oligosaccharide (MMO).

[0161] As understood by the skilled person, mammalian milk oligosaccharides (MMOs) comprise oligosaccharides present in milk found in any phase during lactation including colostrum milk from humans (i.e. human milk oligosaccharides or HMOs) and mammals including but not limited to cows (Bos Taurus), sheep (Ovis aries), goats (Capra aegagrus hircus), bactrian camels (Camelus bactrianus), horses (Eguus ferus caballus), pigs (Sus scropha), dogs (Canis lupus familiaris), ezo brown bears (Ursus arctos yesoensis), polar bear (Ursus maritimus), Japanese black bears (Ursus thibetanus japonicus), striped skunks (Mephitis mephitis), hooded seals (Cystophora cristata), Asian elephants (Elephas maximus), African elephant (Loxodonta africana), giant anteater (Myrmecophaga tridactyla), common bottlenose dolphins (Tursiops truncates), northern minke whales (Balaenoptera acutorostrata), tammar wallabies (Macropus eugenii), red kangaroos (Macropus rufus), common brushtail possum (Trichosurus Vulpecula), koalas (Phascolarctos cinereus), eastern quolls (Dasyurus viverrinus), platypus (Ornithorhynchus anatinus) (Urashima T. et al., 2011, Milk Oligosaccharides, Nova Biomedical Books, New York ISBN 978-1-61122- 831-1; Coppa et al, 2013, Ital. J. Pediatr. 2013, 39(2)). A replete amount of milk saccharide structures have been elucidated so far. The majority of milk oligosaccharides found in animals such as mammals and humans comprise lactose at the reducing end (Urashima et al, 2011). Other milk oligosaccharides comprise N-acetyllactosamine (Gal-pi,4-GlcNAc) or lacto-N-biose (Gal-pi,3-GlcNAc) at the reducing end (Urashima et al, 2011; Wrigglesworth et al, 2020, PLoS ONE 15(12); Urashima et al, 2013, Biosci. Biotechnol. Biochem 77(3): p. 455-466; Wei et al, 2018, Sci. Rep. 8:4688).

[0162] It is another preferred embodiment that said acceptor is provided intracellularly, wherein said acceptor is produced intracellularly by a cell as disclosed herein and / or is taken up by the cell from the cultivation medium.

[0163] A cell that is able to take up said acceptor from the cultivation medium is preferably a cell that is genetically engineered to import said acceptor, wherein said cell comprises a nucleic acid encoding a transporter that is capable to import said acceptor. Such transporter is for example a membrane protein belonging to the major facilitator superfamily (MFS), the ATP-binding cassette (ABC) transporter family or the PTS system involved in the uptake of e.g., mono-, di- and / or oligosaccharides. It is referred to the second aspect of the invention wherein this is elaborated in further detail.

[0164] A cell that is capable to produce said acceptor intracellularly is preferably a cell that produces said acceptor de novo (preferably intracellularly) or that further modifies (preferably further elongates) a precursor acceptor (for example lactose) that is taken up by the cell from the cultivation medium. It is referred to the second aspect of the invention wherein this is elaborated in further detail.

[0165] A cell that produces said acceptor de novo is well-known to the skilled person and essentially such a cell is genetically engineered for the production of said acceptor, i.e. the cell comprises the required glycosyltransferase(s) (its is particularly referred to the one or more additional glycosyltransferases as disclosed earlier herein for further elaboration in this regard) and metabolic pathway(s) for the production of said acceptor (it is particularly referred to the second aspect of the invention wherein this is further elaborated).

[0166] Likewise, a cell that further modifies a precursor acceptor resulting in said acceptor is well-known to the skilled person and essentially is a cell that is genetically engineered for the production of said acceptor, i.e. the cell comprises the required glycosyltransferase(s) (its is particularly referred to the one or more additional glycosyltransferases as disclosed earlier herein for further elaboration in this regard) and metabolic pathway(s) for the production of said acceptor starting from said precursor acceptor (it is particularly referred to the second aspect of the invention wherein this is further elaborated).

[0167] A "precursor acceptor" is preferably to be understood as an acceptor as disclosed herein but that lacks one or more monosaccharides (which are then added by the cell to arrive at the acceptor as disclosed herein). "Elongate" preferably refers to the addition of one or more monosaccharides to the precursor acceptor (more specifically to the saccharide part of said precursor acceptor).

[0168] A cell that is able to take up said precursor acceptor from the cultivation medium is preferably a cell that is genetically engineered to import said precursor acceptor, wherein said cell comprises a nucleic acid encoding a transporter that is capable to import said precursor acceptor. Such transporter is for example a membrane protein belonging to the major facilitator superfamily (MFS), the ATP-binding cassette (ABC) transporter family or the PTS system involved in the uptake of e.g., mono-, di- and / or oligosaccharides. It is referred to the second aspect of the invention wherein this is elaborated in further detail.

[0169] The skilled person is familiar to non-cellular and cellular methods for the production of an acceptor or precursor acceptor as disclosed herein. For example:

[0170] - LN3: Zhu et al, 2021, J. Agric. Food Chem. 69(12) : 3702-3711,

[0171] LNnT: Hu et al, 2023, Carbohydrate polymers 316(8) : 121067,

[0172] - LNnFP-l: Dumon et al, 2001, Glyconj. J. 18(6) : p. 465-474,

[0173] LNnFP-V: Bai et al, 2019, Carbohydrate research 480 : p. 1-6,

[0174] LNFP-III: Sugita et al, J. Biotechnology 361 : p. 110-118, Bai et al, 2019, Carbohydrate research 480 : p. 1-6,

[0175] - LNnDFH: Dumon et al, 2001, Glyconj. J. 18(6) : p. 465-474,

[0176] - LST c: W02016 / 199071,

[0177] - LNT: Hu et al, 2022, J. Agric. Food Chem. 70(28): p. 8704-8712,

[0178] - LNFP-V: W02020 / 115671,

[0179] LNFP-II: Zeuner et al, 2018, N. Biotechnol. 41: p. 34-45,

[0180] LNFP-I: Derya et al, 2020, J. Biotechnol. 318: p. 31-38, Hu et al, 2022, Carbohydr. Polym. 297 : p. 120017,

[0181] - LNDFH-I: Huang et al, 2021, ACS Catal. 11(5): p. 2631-2643,

[0182] - LNDFH-II: Yu et al, 2017, chem. Comm. 53(80) : p. 11012-11015 ; Huang et al, 2021, ACS Catal. 11(5): p. 2631-2643,

[0183] - LST a: WO2023 / 166034,

[0184] DSLNT: Pei et al, 12 March 2024, Enzyme and Microbial Technology. In an embodiment of the first aspect of the invention, said compound comprises GlcNAc-beta-1,6- galactose-betal,4-Zi-Z2-R, wherein:

[0185] Zi is glucose or N-acetylglucosamine (GIcNAc); and

[0186] Z2 is absent or is a saccharide, preferably Z2 is absent or is selected from the list consisting of a monosaccharide, a disaccharide and an oligosaccharide; even more preferably Z2 is absent or is a disaccharide or is an oligosaccharide; most preferably Z2 is absent; and

[0187] R is absent or is selected from the list consisting of a peptide, a protein and a lipid, preferably wherein R is absent.

[0188] It is further referred to the Section "Acceptor" wherein Zi, Z2 and R are further elaborated in detail.

[0189] As will be apparent for the skilled person in the context of the invention, the beta-1, 6-N- acetylglucosaminyltransferase of the invention (it is in particular referred to the Section "Beta-1, 6-N- acetylglucosaminyltransferase") transfers a N-acetylglucosamine to the galactose bound at the nonreducing end of Zi of the acceptor, i.e. galactose-beta-l,4-Zi-Z -R (said galactose is underlined), so as to form a compound comprising GlcNAc-beta-l,6-galactose-betal,4-Zi-Z2-R, wherein Zi, Z2 and R are as defined earlier herein (it is further referred to the Section "Acceptor"). Said acceptor is further elaborated in detail in the Section "Acceptor".

[0190] In other words, a compound according to the invention comprises the structure of the acceptor (it is referred to the Section "Acceptor"), a N-acetylglucosamine (GIcNAc) that is bound to the acceptor in a beta-1, 6-linkage and wherein said beta-1, 6-linked GIcNAc is optionally further elongated with one or more additional monosaccharides. Said monosaccharide(s) is / are preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and sialic acid, even more preferably selected from the list consisting of galactose, fucose and sialic acid, most preferably selected from the list consisting of galactose and fucose.

[0191] As an example, the compound Neu5Ac-alpha2,6-galactose-beta-l,4-GlcNAc-beta-l,6-(galactose-beta-l,4- GlcNAc-betal,3-)galactose-(fucose-alpha-l,3-)beta-l,4-glucose-R is derived from the acceptor galactose- beta-l,4-GlcNAc-betal,3-galactose-(fucose-alpha-l,3-)beta-l,4-glucose-R by the addition of a beta-1, 6- GIcNAc (through the action of a beta-1, 6-N-acetylglucosaminyltransferase according to the invention) and the further elongation of said beta-1, 6-GlcNAc with a galactose and a Neu5Ac (through the action of a galactosyltransferase and a sialyltransferase, respectively).

[0192] In a preferred embodiment, said compound comprises GlcNAc-beta-l,6-(GlcNAc-beta-l,3-)galactose- beta-l,4-Zi-Z2-R, wherein Zi, Z2 and R are as defined earlier herein (it is further referred to the Section "Acceptor"); and optionally wherein said beta-1, 6-linked GIcNAc is further elongated with one or more additional monosaccharides, preferably selected from the list consisting of galactose, fucose, N- acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and sialic acid, even more preferably selected from the list consisting of galactose, fucose and sialic acid, most preferably selected from the list consisting of galactose and fucose; optionally wherein one or more additional monosaccharides are bound to the beta-1, 3-linked GIcNAC (i.e. GlcNAc-beta-l,6-(GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z;>-R), preferably wherein said additional monosaccharide(s) is / are selected from the list consisting of galactose, fucose, N- acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and sialic acid, even more preferably selected from the list consisting of galactose, fucose and sialic acid, most preferably selected from the list consisting of galactose and fucose; optionally wherein one or more additional monosaccharides are bound to Zi, preferably wherein said additional monosaccharide(s) is / are selected from the list consisting of galactose, fucose, N- acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and sialic acid, even more preferably selected from the list consisting of galactose, fucose and sialic acid, most preferably selected from the list consisting of galactose and fucose.

[0193] In a more preferred embodiment, said compound comprises GlcNAc-beta-l,6(galactose-beta-GlcNAc- beta-l,3-)galactose-beta-l,4-Zi-Z2-R, preferably comprises GlcNAc-beta-l,6(galactose-beta-l,4-GlcNAc- beta-l,3-)galactose-beta-l,4-Zi-Z2-R or GlcNAc-beta-l,6(galactose-beta-l,3-GlcNAc-beta-l,3-)galactose- beta-l,4-Zi-Z2-R, most preferably comprises GlcNAc-beta-l,6(galactose-beta-l,4-GlcNAc-beta-l,3- )galactose-beta-l,4-Zi-Z2-R; wherein Zi, Z2 and R are as defined earlier herein (it is further referred to the Section "Acceptor"); and optionally wherein said beta-1, 6-linked GIcNAc is further elongated with one or more additional monosaccharides, preferably selected from the list consisting of galactose, fucose, N- acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and sialic acid, even more preferably selected from the list consisting of galactose, fucose and sialic acid, most preferably selected from the list consisting of galactose and fucose; optionally wherein one or more additional monosaccharides are bound to the beta-linked galactose (i.e. GlcNAc-beta-l,6(galactose-beta-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z -R), preferably wherein said additional monosaccharide(s) is / are selected from the list consisting of galactose, fucose, N-acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and sialic acid, even more preferably selected from the list consisting of fucose, N-acetyglucosamine and sialic acid, most preferably selected from the list consisting of fucose and sialic acid; optionally wherein one or more additional monosaccharides are bound to the beta-1, 3-linked GIcNAC (i.e. GlcNAc-beta-l,6-(galactose-beta-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z;>-R, preferably wherein said additional monosaccharide(s) is / are selected from the list consisting of galactose, fucose, N-acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and sialic acid, even more preferably selected from the list consisting of galactose, fucose and sialic acid, most preferably selected from the list consisting of galactose and fucose; optionally wherein one or more additional monosaccharides are bound to Zi, preferably wherein said additional monosaccharide(s) is / are selected from the list consisting of galactose, fucose, N- acetylglucosamine, N-acetylgalactosamine and sialic acid, more preferably selected from the list consisting of galactose, fucose, N-acetylglucosamine and sialic acid, even more preferably selected from the list consisting of galactose, fucose and sialic acid, most preferably selected from the list consisting of galactose and fucose.

[0194] In the context of the present invention, it is particularly preferred that said compound according to the invention is a saccharide, preferably an oligosaccharide, more preferably a mammalian milk oligosaccharide (MMO), most preferably a human milk oligosaccharide (HMO).

[0195] The first aspect of the invention relates to a method for the production of a compound comprising GIcNAc- betal,6-galactose-betal,4-Zi-Z2-R as described herein. Also encompassed within the scope of the present invention is the production of a mixture of two or more compounds comprising GlcNAc-betal,6-galactose- betal,4-Zi-Z2-R as described herein. Such a mixture can for example be obtained by providing at least two different acceptors (it is referred to the Section "Acceptor" wherein said acceptor is further elaborated).

[0196] Within the scope of the present invention, it is preferred that said compound comprising GlcNAc-betal,6- galactose-betal,4-Zi-Z2-R as described herein has a purity of at least 60.0%, preferably at least 70.0%, more preferably at least 80.0%, even more preferably at least 85.0%, even more preferably at least 90.0%, most preferably at least 95.0%, as measured on the total amount of the compound, the acceptor, any intermediate compound and the precursor acceptor (if applicable as disclosed herein), preferably as measured on the total amount of the compound, the acceptor and the precursor acceptor (if applicable as disclosed herein).

[0197] As the skilled person will understand, "any intermediate compound" in the context of the present invention has the structure of (i) the final compound except that it lacks one or more monosaccharides and (ii) the acceptor from where it is derived except that it has one or more additional monosaccharides. If for example the final compound is sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-beta-l,6-(galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-glucose and the acceptor is LNnT, than the feasible intermediate compounds are galactose-beta-l,4-GlcNAc-beta-l,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-glucose and GlcNAc-beta-l,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0198] 1.4-glucose.

[0199] If said compound is a saccharide than the purity is preferably determined using UPLC or mass spectrometry, more preferably using UPLC. Such a method is described in the Section "Analytical analysis" in the Examples as disclosed further herein.

[0200] A compound comprising GlcNAc-beta-l,6-(GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, wherein Zi, Z2 and R are as defined earlier herein (it is further referred to the Section "Acceptor") is preferably selected from the list consisting of GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-

[0201] 1.4-GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-

[0202] GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4-

[0203] GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-

[0204] GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha-l,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-

[0205] (galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose- alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc- betal,3-)galactose-(fucose-alpha-l,3-)beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose- beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi- Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-(fucose-alphal,3-)-GlcNAc-betal,3-)galactose- beta-1, 4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-(fucose- alphal,3-)-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,6-(fucose-alphal,2-galactose-beta-l,4-(fucose-alphal,3-)-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4- (fucose-alphal,3-)-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4- (fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-1,4- GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose- alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose- beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4- (fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-(fucose-alphal,3- )GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose- alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose- beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-(fucose-alphal,3- )GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose- beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4- (fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4- Z1-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4- (fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose- beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose- beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi- Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4-

[0206] GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4- (galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-

[0207] (fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta- 1,4-ZI-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose- alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta- 1,4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi- Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose- beta-1, 4-(fucose-alphal,3-)-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose- alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-

[0208] 1.4-(fucose-alphal,3-)-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose- beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)- Z1-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(sialic acid- alpha2,3-galactose-betal,3-)-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc- betal,6-(fucose-alphal,4-(sialic acid-alpha2,3-galactose-betal,3-)-GlcNAc-betal,3-)galactose-beta-l,4- Z1-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(sialic acid-alpha2,3- galactose-betal,3-)-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(fucose-alphal,4-(sialic acid-alpha2,3-galactose-betal,3-)-GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0209] 1.4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-

[0210] )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R,

[0211] GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose- beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose- betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (sialic acid-alpha2,6-(sialic acid-alpha2,3-galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(sialic acid-alpha2,3-galactose-betal,3-)GlcNAc- betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,6-(sialic acid-alpha2,3-galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(sialic acid-alpha2,3-galactose-betal,3- )GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6- (galactose-beta-l,3-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3- )GlcNAc-beta-l,6-(fucose-alpha-l,4-(galactose-beta-l,3-)GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose-alpha-l,2-galactose-beta-l,3-GlcNAc- beta-1, 3-)galactose-beta-l,4-Zi-Z2-R and galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose- alpha-l,4-(fucose-alpha-l,2-galactose-beta-l,3-)GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R; more preferably selected from the list consisting of GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2- R, galactose-beta-l,4-GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta- 1,4-ZI-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-

[0212] GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha- 1,3-)ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4- (fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-(fucose-alpha-l,3-)beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- beta-1, 4-Z1-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi- Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-

[0213] )galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose- beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0214] 1.4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4- Z1-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0215] 1.4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0216] 1.4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2- R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose- alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi- Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3- )GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4- GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose- alpha-l,3-)GlcNAc-beta-l,6-(galactose-beta-l,3-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, Galactose- beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose-alpha-l,4-(galactose-beta-l,3-)GlcNAc-beta-l,3- )galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose-alpha-l,2- galactose-beta-l,3-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R and galactose-beta-l,4-(fucose-alpha- l,3-)GlcNAc-beta-l,6-(fucose-alpha-l,4-(fucose-alpha-l,2-galactose-beta-l,3-)GlcNAc-beta-l,3-

[0217] )galactose-beta-l,4-Zi-Z2-R; even more preferably selected from the list consisting of GlcNAc-betal,6- (GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6- (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4-

[0218] GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-

[0219] GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha-l,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-

[0220] (galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose- alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc- betal,3-)galactose-(fucose-alpha-l,3-)beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose- beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose- beta-1, 4-Z1-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta- 1.4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-

[0221] )galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose- alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-

[0222] 1.4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-

[0223] )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4- (galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0224] 1,4-ZI-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6- (galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose- beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose- betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6- (galactose-beta-l,3-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3- )GlcNAc-beta-l,6-(fucose-alpha-l,4-(galactose-beta-l,3-)GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose-alpha-l,2-galactose-beta-l,3-GlcNAc- beta-1, 3-)galactose-beta-l,4-Zi-Z2-R and galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose- alpha-l,4-(fucose-alpha-l,2-galactose-beta-l,3-)GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R; even more preferably selected from the list consisting of GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2- R, galactose-beta-l,4-GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta- 1,4-ZI-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-

[0225] GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose- beta-1, 4-Z1-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha- 1,3-)ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4- (fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-(fucose-alpha-l,3-)beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4- GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose- beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose- beta-1, 4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi- Zj-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4-

[0226] GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4- (galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-

[0227] (fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta- 1,4-ZI-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-

[0228] GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc- betal,3-galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose- betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3- galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R and sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R; even more preferably selected from the list consisting of GlcNAc-betal,6- (GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6- (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4-

[0229] GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-

[0230] GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha-l,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-

[0231] (galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose- alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc- betal,3-)galactose-(fucose-alpha-l,3-)beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose- beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0232] 1.4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4- Z1-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0233] 1.4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-

[0234] )galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-

[0235] )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose- beta-1, 4-Z1-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0236] 1.4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3- )GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4- GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R; even more preferably selected from the list consisting of GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta- 1,4-ZI-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-

[0237] GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-beta-l,4-GlcNAc-betal,3-)galactose- beta-1, 4-Z1-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha- 1,3-)ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4- (fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4- GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-(fucose-alpha-l,3-)beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(galactose-beta-l,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose- alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GIcNAc- betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4- GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R; most preferably selected from the list consisting of GlcNAc-betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc- betal,6-(GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose- beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc- betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-beta-l,4-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4- GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose- beta-1, 4-Z1-Z2-R; wherein Zi, Z2 and R are as defined earlier herein (it is further referred to the Section "Acceptor").

[0238] A compound comprising GlcNAc-beta-l,6(galactose-beta-l,4-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-

[0239] R, wherein Zi, Z2 and R are as defined earlier herein (it is further referred to the Section "Acceptor") is preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6- (galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose- betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-(fucose-alpha-l,3-)Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4- GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-(fucose- alpha-l,3-)betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-

[0240] )GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6- (galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4- (fucose-alphal,3-)-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4- GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-(fucose- alphal,3-)-Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose- betal,4-GlcNAc-betal,3-)galactose-betal,4-(fucose-alphal,3-)-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,4-(fucose-alphal,3-)-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4- GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-(fucose-alphal,3-)-GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose- betal,4-(fucose-alphal,3-)-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose- betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-(fucose-alphal,3-)-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3- )galactose-betal,4-(fucose-alphal,3-)Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4- (fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3- galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- betal,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(galactose- betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-(fucose- alphal,3-)Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-betal,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose- betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3- )galactose-betal,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-(fucose- alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc- betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(sialic acid- alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose- betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2- R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose- betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc- betal,6-(sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,6-galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi- Z2-R, galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-(fucose-alphal,3- )GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-(fucose-alphal,3- )GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,4- (fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid- alpha2,3-galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,4-(fucose-alphal,3- )GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6- (sialic acid-alpha2,3-galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R; more preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6- (galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose- betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-(fucose-alpha-l,3-)Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4- GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-(fucose- alpha-l,3-)betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-

[0241] )GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6- (galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- betal,4-(fucose-alphal,3-)Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-betal,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose- betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4- (fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4- (fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc- betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid- alpha2,3-galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6- galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3- galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose- betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R; even more preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose- betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid- alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-(fucose-alpha- 1.3-)Zi-Zz-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4- (fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4- GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-(fucose-alpha-l,3-)betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc- betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose- betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2- R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc- betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(sialic acid- alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid- alpha2,3-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc- betal,6-(sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid- alpha2,3-galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(sialic acid- alpha2,3-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R; even more preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4- Z1-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-(fucose-alpha-

[0242] 1.3-)ZI-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4- (fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4- GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-(fucose-alpha-l,3-)betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc- betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose- betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2- R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,4-GlcNAc- betal,3-)galactose-betal,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(sialic acid- alpha2,6-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R; even more preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4- Z1-Z2-R, sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-betal,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,4-GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-(fucose-alpha- 1,3-)ZI-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4- (fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-(fucose-alpha-l,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-betal,4- GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3-)galactose-(fucose-alpha-l,3-)betal,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose- betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-(fucose- alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-betal,4-GlcNAc- betal,6-(galactose-betal,4-(fucose-alphal,3-)GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R; most preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4-GlcNAc-betal,3- )galactose-betal,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-betal,4-GlcNAc-betal,6-(galactose-betal,4- GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-betal,4-GlcNAc-betal,6- (galactose-betal,4-GlcNAc-betal,3-)galactose-betal,4-Zi-Z2-R; wherein Zi, Z2 and R are as defined earlier herein (it is further referred to the Section "Acceptor").

[0243] A compound comprising GlcNAc-beta-l,6(galactose-beta-l,3-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-

[0244] R, wherein Zi, Z2 and R are as defined earlier herein (it is further referred to the Section "Acceptor") is preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,3-

[0245] GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-

[0246] (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose- alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(galactose- betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose- alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta- l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, GlcNAc-betal,6- (fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose- alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi- Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose- beta-1, 4-(fucose-alphal,3-)-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose- alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-

[0247] 1.4-(fucose-alphal,3-)-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose- beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)- Z1-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(sialic acid- alpha2,3-galactose-betal,3-)-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc- betal,6-(fucose-alphal,4-(sialic acid-alpha2,3-galactose-betal,3-)-GlcNAc-betal,3-)galactose-beta-l,4- Z1-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(sialic acid-alpha2,3- galactose-betal,3-)-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(fucose-alphal,4-(sialic acid-alpha2,3-galactose-betal,3-)-GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0248] 1.4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-

[0249] )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R,

[0250] GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose- beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose- betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (sialic acid-alpha2,6-(sialic acid-alpha2,3-galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(sialic acid-alpha2,3-galactose-betal,3-)GlcNAc- betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,6-(sialic acid-alpha2,3-galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(sialic acid-alpha2,3-galactose-betal,3- )GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6- (galactose-beta-l,3-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3- )GlcNAc-beta-l,6-(fucose-alpha-l,4-(galactose-beta-l,3-)GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose-alpha-l,2-galactose-beta-l,3-GlcNAc- beta-1, 3-)galactose-beta-l,4-Zi-Z2-R and galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose- alpha-l,4-(fucose-alpha-l,2-galactose-beta-l,3-)GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R; more preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,3-

[0251] GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-

[0252] (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose- alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(galactose- betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zl-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose- alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-

[0253] GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4- (fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose- alphal,4-(fucose-alphal,2-galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi- Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3- )GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6- (galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc- betal,3-galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(galactose-beta-l,3- GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6- (fucose-alpha-l,4-(galactose-beta-l,3-)GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-1,4- (fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose-alpha-l,2-galactose-beta-l,3-GlcNAc-beta-l,3-)galactose- beta-1, 4-Z1-Z2-R and galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose-alpha-l,4-(fucose- alpha-l,2-galactose-beta-l,3-)GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R; even more preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta- 1,4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4- Z1-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-

[0254] GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta- 1.4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-

[0255] )galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-

[0256] )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose- beta-1, 4-Z1-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-

[0257] 1.4-ZI-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4- GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc- betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid- alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3- )GlcNAc-beta-l,6-(galactose-beta-l,3-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R, Galactose-beta-1,4- (fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose-alpha-l,4-(galactose-beta-l,3-)GlcNAc-beta-l,3-)galactose- beta-1, 4-Z1-Z2-R, Galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc-beta-l,6-(fucose-alpha-l,2-galactose- beta-l,3-GlcNAc-beta-l,3-)galactose-beta-l,4-Zi-Z2-R and galactose-beta-l,4-(fucose-alpha-l,3-)GlcNAc- beta-l,6-(fucose-alpha-l,4-(fucose-alpha-l,2-galactose-beta-l,3-)GlcNAc-beta-l,3-)galactose-beta-l,4- Z1-Z2-R; even more preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-

[0258] GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4- GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-1,4- GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta- l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,4- (galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-

[0259] (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose- beta-1, 4-Z1-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose- betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2-galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(fucose- alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2- R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,3-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3- galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3- )GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6- (sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose- beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid- alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R and sialic acid-alpha2,6- galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose- beta-l,4-Zi-Z2-R; even more preferably selected from the list consisting of GlcNAc-betal,6-(galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose- beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GIcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-

[0260] Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4-

[0261] GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4- (galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-

[0262] (fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3- galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta- 1,4-ZI-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3- GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-

[0263] )GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-

[0264] (galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4- GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc-betal,3-galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-(galactose-betal,3-)GlcNAc- betal,3-galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose- betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc- betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(sialic acid-alpha2,6-galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-Zi-Z2-R; even more preferably selected from the list consisting of GIcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-l,4-GlcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose- beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose- alphal,3-)Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc- betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc- betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-(fucose-alphal,3-)Zi-Z2-R, GIcNAc- betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,4-(galactose-betal,3- )GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6- (fucose-alphal,4-(galactose-betal,3-)GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, GlcNAc-betal,6- (fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose-beta-1,4- GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid-alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2-galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R and sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(fucose-alphal,2- galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R; most preferably selected from the list consisting of GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, galactose- beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi-Z2-R, sialic acid- alpha2,3-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3-)galactose-beta-l,4-Zi- Z2-R and sialic acid-alpha2,6-galactose-beta-l,4-GlcNAc-betal,6-(galactose-betal,3-GlcNAc-betal,3- )galactose-beta-l,4-Zi-Z2-R; wherein Zi, Z2 and R are as defined earlier herein (it is further referred to the Section "Acceptor").

[0265] Cell for the production of a compound

[0266] In a second aspect, the invention provides a cell for the production of a compound comprising N- acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, wherein said cell comprises a beta-1, 6-N- acetylglucosaminyltransferase according to the first aspect of the invention (preferably as described in the Section "beta-1, 6-N-acetylglucosaminyltransferase" of the first aspect), and wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid, preferably wherein R is absent.

[0267] Said compound is preferably as disclosed in the Section "Compound" of the first aspect of the invention. In other words, in a second aspect, the invention provides a cell that is capable to produce, preferably produces, a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, wherein said cell comprises a beta-1, 6-N-acetylglucosaminyltransferase according to the first aspect of the invention (it is particularly referred to the Section "beta-1, 6-N-acetylglucosaminyltransferase" of the first aspect), and wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid, preferably wherein R is absent. Said compound is preferably as disclosed in the Section "Compound" of the first aspect of the invention.

[0268] In this context, it is preferred that said cell comprises a nucleic acid encoding said beta-1, 6-N- acetylglucosaminyltransferase as described herein (preferably as described in the Section "Beta-1, 6-N- acetylglucosaminyltransferase" of the first aspect). Said nucleic acid is integrated into the genome of the cell or is present within a plasmid. In the context of the present invention, more than one nucleic acid encoding a beta-1, 6-N-acetylglucosaminyltransferase as described herein can be present in the cell. Hence, a nucleic acid encoding a beta-1, 6-N-acetylglucosaminyltransferase mutant according to the invention is integrated into the genome of the cell and / or is present within a plasmid. Furthermore, in the context of the invention, a cell according to the invention preferably comprises two or more, preferably three or more, nucleic acids encoding the same beta-1, 6-N-acetylglucosaminyltransferase or wherein one or more (preferably all) nucleic acids encode a different beta-1, 6-N-acetylglucosaminyltransferase as described herein. A cell comprising two or more nucleic acids encoding a beta-1, 6-N- acetylglucosaminyltransferase (either the same beta-1, 6-N-acetylglucosaminyltransferase or one or more nucleic acids encode a different beta-1, 6-N-acetylglucosaminyltransferase) is particularly advantageous in a method according to the first aspect of the invention, as the presence of 2 or more nucleic acids increases the expression level of the beta-1, 6-N-acetylglucosaminyltransferase(s) and hence generally increases the yield of the produced compound(s) (it is referred to the Section "Compound" of the first aspect of the invention).

[0269] In this context, it is also preferred that said cell is an isolated cell. It is further preferred that said cell is a single cell. As understood by the skilled person, a single cell preferably refers to a cell culture derived from the same progenitor cell, i.e. all cells are genetically identical.

[0270] In a preferred embodiment, said cell is selected from a list consisting of a microorganism, a plant cell, an animal cell, an algal cell, an insect cell and a protozoan cell, preferably said cell is a microorganism, more preferably said cell is a bacterium, fungus or yeast, even more preferably said cell is a bacterium, even more preferably said cell is a bacterium belonging to the genus of Escherichia or Bacillus, even more preferably said cell is a bacterium belonging to the genus of Escherichia, even more preferably said cell is Escherichia coli, even more preferably said cell is an Escherichia coli K-12 strain, most preferably said cell is Escherichia coli MG1655.

[0271] Throughout the application and claims, unless specifically stated otherwise, a microorganism is preferably a bacterium, a yeast or a fungus, more preferably a bacterium or a yeast, most preferably a bacterium. Throughout the application and claims, unless specifically stated otherwise, a bacterium preferably belongs to the phylum of the Proteobacteria or the phylum of the Firmicutes or the phylum of the Cyanobacteria or the phylum Deinococcus-Thermus or the phylum of Actinobacteria. Said bacterium belonging to the phylum Proteobacteria belongs preferably to the family Enterobacteriaceae, preferably to the species Escherichia coli. Said bacterium preferably relates to any strain belonging to the species Escherichia coli such as but not limited to Escherichia coli B, Escherichia coli C, Escherichia coli W, Escherichia coli K12, Escherichia coli Nissle. More specifically, said bacterium relates to cultivated Escherichia coli strains - designated as E. coli K12 strains - which are well-adapted to the laboratory environment, and, unlike wild type strains, have lost their ability to thrive in the intestine. Well-known examples of the E. coli K12 strains are K12 Wild type, W3110, MG1655, M182, MC1000, MC1060, MC1061, MC4100, JM101, NZN111 and AA200. Hence, preferably the present invention specifically relates to an E. coli K12 strain, more preferably an E. coli MG1655 strain. Said bacterium belonging to the phylum Firmicutes belongs preferably to the Bacilli, preferably Lactobacilliales, with members such as Lactobacillus lactis, Leuconostoc mesenteroides, or Bacillales with members such as from the genus Bacillus, such as Bacillus subtilis or, B. amyloliquefaciens. Said bacterium belonging to the phylum Actinobacteria, preferably belonging to the family of the Corynebacteriaceae, with members Corynebacterium glutamicum or C. afermentans, or belonging to the family of the Streptomycetaceae with members Streptomyces griseus or S. fradiae. Said bacterium belonging to the phylum Proteobacteria, preferably belonging to the family of the Vibrionaceae, with member Vibrio natriegens.

[0272] Throughout the application and claims, unless specifically stated otherwise, a yeast cell preferably belongs to the phylum of the Ascomycota or the phylum of the Basidiomycota or the phylum of the Deuteromycota or the phylum of the Zygomycetes. Said yeast cell belongs preferably to the genus Saccharomyces (with members like e.g. Saccharomyces cerevisiae, S. bayanus, S. boulardii), Pichia (with members like e.g. Pichia pastoris, P. anomala, P. kluyveri), Komagataella, Hansunella, Kluyveromyces (with members like e.g. Kluyveromyces lactis, K. marxianus, K. thermotolerans), Yarrowia (like e.g. Yarrowia lipolytica), Eremothecium, Zygosaccharomyces, Starmerella l ike e.g. Starmerella bombicola) or Debaromyces. Said yeast cell is more preferably selected from Pichia pastoris, Yarrowia lipolitica, Saccharomyces cerevisiae, Kluyveromyces lactis, Hansenula polymorpha, Kluyveromyces marxianus, Pichia methanolica, Pichia stipites, Candida boidinii, Schizosaccharomyces pombe, Schwanniomyces occidentalis, Torulaspora delbrueckii, Zygosaccharomyces rouxii, and Zygosaccharomyces bailii.

[0273] Throughout the application and claims, unless specifically stated otherwise, a fungus preferably belongs to the genus Rhizopus, Dictyostelium, Penicillium, Mucor or Aspergillus.

[0274] Throughout the application and claims, unless specifically stated otherwise, a plant cell includes cells of flowering and non-flowering plants, as well as algal cells, for example Chlamydomonas, Chlorella, etc. Preferably, said plant cell is a tobacco, alfalfa, rice, cotton, rapeseed, tomato, corn, maize or soybean cell. Throughout the application and claims, unless specifically stated otherwise, an animal cell is preferably derived from non-human mammals (e.g. cattle, buffalo, pig, sheep, mouse, rat), birds (e.g. chicken, duck, ostrich, turkey, pheasant), fish (e.g. swordfish, salmon, tuna, sea bass, trout, catfish), invertebrates (e.g. lobster, crab, shrimp, clams, oyster, mussel, sea urchin), reptiles (e.g. snake, alligator, turtle), amphibians (e.g. frogs) or insects (e.g. fly, nematode) or is a genetically modified cell line derived from human cells excluding embryonic stem cells. Both human and non-human mammalian cells are preferably chosen from the list consisting of an epithelial cell like e.g. a mammary epithelial cell, an embryonic kidney cell (e.g. HEK293 or HEK 293T cell), a fibroblast cell, a COS cell, a Chinese hamster ovary (CHO) cell, a murine myeloma cell like e.g. an 1X120, SP2 / 0 or YB2 / 0 cell, an NIH-3T3 cell, a lactocyte derived from mammalian induced pluripotent stem cells (preferably human induced pluripotent stem cells), a lactocyte as part of mammary-like gland organoids, a post-parturition mammary epithelium cell, a polarized mammary cell (preferably a polarized mammary cell selected from the list consisting of live primary mammary epithelial cells, live mammary myoepithelial cells, live mammary progenitor cells, live immortalized mammary epithelial cells, live immortalized mammary myoepithelial cells, live immortalized mammary progenitor cells, a non-mammary adult stem cell or derivatives thereof as well-known to the person skilled in the art from e.g. WO2021 / 219634, WO 2022 / 054053, WO 2021 / 141762, WO 2021 / 142241, WO 2021 / 067641 and WO2021 / 242866.

[0275] Throughout the application and claims, unless specifically stated otherwise, an insect cell is preferably derived from Spodoptera frugiperda like e.g. Sf9 or Sf21 cells, Bombyx mori, Mamestra brassicae, Trichoplusia ni like e.g. BTI-TN-5B1-4 cells or Drosophila melanogaster like e.g. Drosophila S2 cells.

[0276] Throughout the application and claims, unless specifically stated otherwise, a protozoan cell is preferably a Leishmania tarentolae cell.

[0277] In another preferred embodiment, said cell according to the invention is a host cell. In the context of the present invention, a host cell is preferably a cell that is genetically engineered for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid, preferably wherein R is absent. It is referred to the Section "Compound" of the first aspect of the invention wherein said compound is disclosed in further detail. Preferably, the cell according to the invention is genetically modified with one or more expression modules, preferably for the expression of a transporter protein as described herein, a glycosyltransferase as described herein (e.g. a beta-1, 6-N-acetylglucosaminyltransferase according to the invention) and / or an enzyme involved in a metabolic pathway as described herein. The expression module(s) can be integrated in the genome of said cell or can be presented to said cell on a vector. Said vector is preferably a plasmid. Said expression modules are also known as transcriptional units and comprise polynucleotides for expression of recombinant genes including coding gene sequences and appropriate transcriptional and / or translational control signals that are operably linked to the coding genes. Said control signals comprise promoter sequences, untranslated regions, ribosome binding sites, terminator sequences. Said expression modules can contain elements for expression of one single recombinant gene but can also contain elements for expression of more recombinant genes or can be organized in an operon structure for integrated expression of two or more recombinant genes. Said polynucleotides may be produced by recombinant DNA technology using techniques well-known in the art. Methods which are well known to those skilled in the art to construct expression modules include, for example, in vitro recombinant DNA techniques, synthetic techniques, and in vivo genetic recombination. See, for example, the techniques described in Sambrook et al. (2001) Molecular Cloning: a laboratory manual, 3rd Edition, Cold Spring Harbor Laboratory Press, CSH, New York or to Current Protocols in Molecular Biology, John Wiley and Sons, N.Y. (1989 and yearly updates).

[0278] In this regard, it is a preferred embodiment that said cell according to the invention comprises at least one metabolic pathway involved in the synthesis of said compound. In the context of the present invention, said cell according to the invention comprises at least a N-acetylglucosaminylation pathway, comprising of (i) a beta-1, 6-N-acetylglucosaminyltransferase according to the invention and optionally at least one beta-1, 3-N-acetylglucosaminyltransferase (preferably as defined herein) and (ii) UDP-GIcNAc which is donor for said N-acetylglucosaminyltransferase(s).

[0279] Optionally, said cell according to the invention comprises at least one further metabolic pathway involved in the synthesis of said compound.

[0280] Said at least one metabolic pathway is preferably one or more selected from the list consisting of: a) fucosylation pathway comprising of (i) at least one fucosyltransferase (preferably as defined herein) and (ii) GDP-fucose which is donor for said fucosyltransferase(s); b) galactosylation pathway comprising of (i) at least one galactosyltransferase (preferably as defined herein) and (ii) UDP-galactose which is donor for said galactosyltransferase(s); and c) sialylation pathway comprising of (i) at least one sialyltransferase (preferably as defined herein) and (ii) CMP-sialic acid which is donor for said sialyltransferase(s).

[0281] Said at least one metabolic pathway is more preferably one or more selected from the list consisting of: a) fucosylation pathway comprising of (i) at least one fucosyltransferase (preferably as defined herein) and (ii) GDP-fucose which is donor for said fucosyltransferase(s); and b) galactosylation pathway comprising of (i) at least one galactosyltransferase (preferably as defined herein) and (ii) UDP-galactose which is donor for said galactosyltransferase(s).

[0282] Said at least one metabolic pathway is most preferably a galactosylation pathway comprising of (i) at least one galactosyltransferase (preferably as defined herein) and (ii) UDP-galactose which is donor for said galactosyltransferase(s). Said N-acetylglucosaminylation pathway optionally further comprises one or more enzymes and their respective genes selected from the list consisting of L-glutamine— D-fructose-6- phosphate aminotransferase, glucosamine-6-phosphate deaminase, phosphoglucosamine mutase, N- acetylglucosamine-6-phosphate deacetylase, glucosamine 6-phosphate N-acetyltransferase, N- acetylglucosamine-l-phosphate uridylyltransferase, glucosamine-l-phosphate acetyltransferase and glucosamine-l-phosphate acetyltransferase. Said fucosylation pathway optionally further comprises one or more enzymes and their respective genes selected from the list consisting of mannose-6-phosphate isomerase, phosphomannomutase, mannose-l-phosphate guanylyltransferase, GDP-mannose 4,6- dehydratase, GDP-L-fucose synthase and salvage pathway L-fucokinase / GDP-fucose pyrophosphorylase. Said galactosylation pathway optionally further comprises one or more enzymes and their respective genes selected from the list consisting of galactose-l-epimerase, galactokinase, glucokinase, galactose-1- phosphate uridylyltransferase, UDP-glucose 4-epimerase, glucose-l-phosphate uridylyltransferase and glucophosphomutase. Said sialylation pathway optionally further comprises one or more enzymes and their respective genes selected from the list consisting of L-glutamine— D-fructose-6-phosphate aminotransferase, glucosamine-6-phosphate deaminase, phosphoglucosamine mutase, N- acetylglucosamine-6-phosphate deacetylase, N-acetylglucosamine epimerase, UDP-N-acetylglucosamine 2-epimerase, N-acetylglucosamine-6P 2-epimerase, Glucosamine 6-phosphate N-acetyltransferase, N- AcetylGlucosamine-6-phosphate phosphatase, N-acetylmannosamine-6-phosphate phosphatase, N- acetylmannosamine kinase, phosphoacetylglucosamine mutase, N-acetylglucosamine-l-phosphate uridyltransferase, glucosamine-l-phosphate acetyltransferase, sialic acid synthase, N-acetylneuraminate lyase, N-acylneuraminate-9-phosphate synthase, N-acylneuraminate-9-phosphate phosphatase and CMP-sialic acid synthase. Throughout the application and claims, unless specifically stated otherwise, said "CMP-sialic acid" is preferably "CMP-Neu5Ac". Likewise, "sialic acid" is preferably replaced with "Neu5Ac" (N-acetylneuraminate and N-acetylneuraminic acid are interchangeably used for Neu5Ac).

[0283] In an additional and / or alternative preferred embodiment, at least one gene of said at least one metabolic pathway is genetically engineered. Preferably a glycosyltransferase of said at least one metabolic pathway is genetically engineered.

[0284] In this regard, it is another preferred embodiment, that said cell according to the invention further comprises one or more additional glycosyltransferases that are involved in the production of said compound. Preferably, said cell according to the invention is modified (preferably genetically modified) in the expression or activity of at least one, preferably at least two, of said glycosyltransferases including said beta-1, 6-N-acetylglucosaminyltransferase. Preferably, said one or more additional glycosyltransferases are selected from the list consisting of a beta-1, 3-N-acetylglucosaminyltransferase, a beta-1, 3-galactosyltransferase, a beta-1, 4-galactosyltransferase, a fucosyltransferase and a sialyltransferase, preferably selected from the list consisting of a beta-1, 3-N- acetylglucosaminyltransferase, a beta-1, 3-galactosyltransferase, a beta-1, 4-galactosyltransferase and a fucosyltransferase, most preferably selected from the list consisting of a beta-1, 3-N- acetylglucosaminyltransferase, a beta-1, 3-galactosyltransferase and a beta-1, 4-galactosyltransferase. As the skilled understands, a protein (such as a glycosyltransferase disclosed herein) is encoded by a nucleic acid (which can be integrated into the genome of the cell and / or is present within a plasmid as discussed earlier herein). Hence, throughout the application and claims, "a cell comprising e.g. a glycosyltransferase" can preferably be replaced with "a cell comprising a nucleic acid encoding a glycosyltransferase" (said nucleic acid is preferably as described earlier herein in the context of beta-1, 6- N-acetylglycosyltransferase). Said fucosyltransferase is preferably an alpha-1, 2-fucosyltransferase or an alpha-1, 3-fucosyltransferase. Said alpha-1, 2-fucosyltransferase is preferably FutC (preferably from Helicobacter pylori). Said alpha-1, 3-fucosyltransferase is preferably FucT (preferably from Helicobacter pylori). Said sialyltransferase is preferably an alpha-2, 3-sialyltransferase or an alpha-2, 6-sialyltransferase, more preferably an alpha-2, 6-sialyltransferase. Said alpha-2, 3-sialyltransferase is preferably ST3 (preferable from Pasteurella multocida). Said alpha-2, 6-sialyltransferase is preferably ST6 (preferable from Photobacterium damselae). Said beta-1, 4-galactosyltransferase is preferably selected from GalT7, gatD and LgtB, more preferably LgtB. Said GalT7 is preferably from Pasteurella multocida, more preferably Uniprot ID F47LW1 (sequence version 01). Said gatD is preferably from Pasteurella multocida, more preferably Uniprot ID DOEAD4 (sequence version 01). Said LgtB is preferably from Neisseria meningitidis, more preferably Uniprot ID Q51116 (sequence version 02). Said beta-1, 3-galactosyltransferase is preferably WbgO, more preferably WbgO from E. coli O55:H7, even more preferably Uniprot ID D3QY14 (sequence version 01). Said beta-1, 3-N-acetylglucosaminyltransferase is preferably LgtA, more preferably LgtA from Neisseria meningitidis, even more preferably Uniprot ID Q9JXQ6 (sequence version 01).

[0285] In this regard, it is another preferred embodiment that a metabolic pathway for the production of UDP- GIcNAc is present in said cell according to the invention, preferably said cell further comprises a metabolic pathway for the production of GDP-fucose, a metabolic pathway for the production of UDP-galactose and / or a metabolic pathway for the production of CMP-sialic acid, more preferably said cell further comprises a metabolic pathway for the production of UDP-galactose and optionally a metabolic pathway for the production of GDP-fucose and optionally a metabolic pathway for the production of CMP-sialic acid. Preferably, a metabolic pathway for the production of UDP-GIcNAc comprises one or more enzymes and their respective genes selected from (i) the list consisting of glucosamine 6-phosphate N- acetyltransferase, phosphatase (preferably a HAD-like phosphatase), L-glutamine— D-fructose-6- phosphate aminotransferase and UDP-glucose 4-epimerase, more preferably a glucosamine 6-phosphate N-acetyltransferase and a phosphatase (preferably a HAD-like phosphatase). For an enhanced production of UDP-GIcNAc, a cell according to the invention preferably comprises any one or more modification(s) selected from the list consisting of knock-out of an N-acetylglucosamine-6-phosphate deacetylase, overexpression of an L-glutamine— D-fructose-6-phosphate aminotransferase, over-expression of a phosphoglucosamine mutase and over-expression of an N-acetylglucosamine-l-phosphate uridyltransferase / glucosamine-l-phosphate acetyltransferase. Preferably, a metabolic pathway for the production of GDP-fucose comprises one or more enzymes and their respective genes selected from a bifunctional fucose kinase / fucose-l-phosphate guanylyltransferase or the combination of a fucose kinase a fucose-l-phosphate guanylyltransferase. For an enhanced production of GDP-fucose, a cell according to the invention preferably comprises any one or more modification(s) selected from the list consisting of a knock-out of an N-acetylglucosamine-6-phosphate deacetylase, over-expression of an L-glutamine— D- fructose-6-phosphate aminotransferase, over-expression of a phosphoglucosamine mutase and overexpression of an N-acetylglucosamine-l-phosphate uridyltransferase / glucosamine-l-phosphate acetyltransferase. Preferably, a metabolic pathway for the production of UDP-galactose comprises UDP- glucose-4-epimerase. For an enhanced production of UDP-galactose, a cell according to the invention preferably comprises any one or more modification(s) selected from the list consisting of a knock-out of an bifunctional 5'-nucleotidase / UDP-sugar hydrolase encoding gene, knock-out of a galactose-1- phosphate uridylyltransferase encoding gene and over-expression of an UDP-glucose-4-epimerase encoding gene, preferably over-expression of an UDP-glucose-4-epimerase encoding gene. Preferably, a metabolic pathway for the production of CMP-sialic acid comprises CMP-sialic acid synthetase (e.g. N- acylneuraminate cytidylyltransferase, for example from Homo sapiens, Neisseria meningitidis or Pasteurella multocida). For an enhanced production of CMP-sialic acid, a cell according to the invention preferably comprises any one or more modification(s) selected from the list consisting of knock-out of an N-acetylglucosamine-6-phosphate deacetylase, knock-out of a glucosamine-6-phosphate deaminase, over-expression of a CMP-sialic acid synthetase, and over-expression of an N-acetyl-D-glucosamine-2- epimerase encoding gene.

[0286] In this regard, it is another preferred embodiment, that said cell according to the invention further comprises a membrane transporter protein that is capable to transport said compound according to the invention across the outer membrane of the cell wall (i.e. from inside the cell to outside the cell). Such a transporter protein is preferably selected from the list consisting of a porter, P-P-bond-hydrolysis-driven transporter, p-barrel porin, auxiliary transport protein and phosphotransfer-driven group translocator, more preferably a porter. Said porter is preferably selected from the list consisting of MFS transporter, sugar efflux transporter and siderophore exporter, more preferably MFS transporter. Said MFS transporter as disclosed throughout the application and claims is preferably a MdfA transporter, for example E. coli MdfA (UniProt ID P0AEY8, sequence version 01), Cronobacter muytjensii MdfA (UniProt ID A0A2T7ANQ9, sequence version 01), Citrobacter youngae MdfA (UniProt ID D4BC23, sequence version 01) and Yokenella regensburgei MdfA (UniProt ID G9Z5F4, sequence version 01). Said sugar efflux transporter as disclosed throughout the application and claims is preferably a SetA transporter, for example E. coli setA (UniProt ID P31675, sequence version 03) and Citrobacter koseri SetA (UniProt ID A0A078LM16, sequence version 01). Said siderophore exporter as disclosed throughout the application and claims is preferably E. coli entS (UniProt ID P24077, sequence version 02), the K. ascorbata entS (UniProt ID A0A378GQ13, sequence version 01) and the E. coli iceT (UniProt ID A0A024L207, sequence version 01).

[0287] In this regard, it is preferred that said cell is genetically engineered to import lactose in the cell, by the introduction and / or overexpression of a lactose permease, like e.g., encoded by the LacY gene or the LAC12 gene.

[0288] In the context of the second aspect of the invention wherein a cell comprises a beta-1, 6-N- acetylglucosaminyltransferase according to the first aspect of the invention (preferably as described in the Section "beta-1, 6-N-acetylglucosaminyltransferase" of the first aspect), it is particularly beneficial that said cell according to the invention is adapted (preferably genetically engineered) for the production of a functional disulfide bond containing protein. Hence, it is preferred that the expression of one or more proteins involved in a reductive pathway is lowered or diminished compared to an unmodified cell (i.e. unmodified progenitor cell).

[0289] The term "reductive pathway" as used herein is a biochemical pathway that results in the cytoplasmic environment of the cell to be reducing as understood by the skilled person, wherein said reducing environment can negatively influence proper protein folding and / or can block disulfide bond formation. The term "reducing cytoplasm" preferably means that e.g. the NADP+:NADPH ratio in said cytoplasmic environment is low and / or that the reduced glutathione (i.e. GSH) levels are high (e.g. 10 mM). Reducing environments may affect the oxidation state of a molecule, thereby altering its solubility.

[0290] Examples of said reductive pathway include the reductive acetyl-CoA-pathway, the reductive pyrimidine catabolic pathway, the reductive citric acid cycle, the thiol-redox pathway and the reductive glycine pathway.

[0291] Said one or more proteins involved in a reductive pathway are preferably selected from the list consisting of formate dehydrogenase, formate-tetrahydrofolate ligase, methenyltetrahydrofolate cyclohydrolase, glycine dehydrogenase / decarboxylating, glycine cleavage system protein, glutamate dehydrogenase, glycine reductase complex, CO2 reductase, folate synthetase, folate cyclohydrolase, folate dehydrogenase, folate reductase, methyltransferase, pyruvate synthase, phosphotransacetylase, acetate kinase, ATPase, acetyl-CoA carbonylase / synthase, methylenetetrahydrofolate reductase, methylenetetrahydrofolate dehydrogenase, methyltetrahydrofolate:corrinoid / iron-sulfur protein methyltransferase, methenyltetrahydrofolate cyclohydrolase, pyruvate: ferredoxin oxidoreductase, serine hydroxymethyltransferase, dihydropyrimidine dehydrogenase, dihydropyrimidinase, p- ureidopropionase, ribulose-l,5-bisphosphate carboxylase, ATP citrate lyase, citrate synthase, aconitase, isocitrate dehydrogenase, 2-ketoglutarate dehydrogenase, 2-ketoglutarate ferredoxin oxidoreductase, succinyl-CoA synthetase, succinyl-CoA-acetoacetate-CoA-transferase, fumarate reductase, succinate dehydrogenase, fumarase, malate dehydrogenase, isocitrate lyase, malate synthase, phosphoenol pyruvate carboxykinase, hhosphoenol pyruvate carboxylase, malic enzyme, pyruvate carboxylase / oxaloacetate decarboxylase, pyruvate dehydrogenase, pyruvate ferredoxin oxidoreductase, KatG catalase, alkylhydroperoxide reductase, DNA-binding ferritin-like protein, glutaredoxin, ferric homeostasis regulator, manganese transporter, OxyS, OxyR, glutathione reductase, thioredoxin reductase, thioredoxin-disulphide reductase and glutamine synthetase.

[0292] More preferably said one or more proteins involved in a reductive pathway is / are selected from the list consisting of a glutathione reductase and a thioredoxin reductase.

[0293] A lowered or diminished expression of a protein can be obtained by insertion, deletion and / or modification of one or more nucleotide(s) in one or more polynucleotide sequence(s) selected from the list consisting of promoter sequence, ribosome binding site, untranslated region, coding sequence and transcription terminator sequence of a gene encoding said protein.

[0294] Cells adapted for the production of a functional disulfide bond containing protein, i.e. cell that are permissive to the formation of disulfide bonds, are well-known to the skilled person. Exemplary Escherichia coli strains that are commercially available include Origami™ strains (e.g. Origami™, Origami™ B, Origami™ 2) and SHuffle® strains (Lobstain et al, 2012, Microbial Cell Factories 11: 56).

[0295] In another preferred embodiment, said cell according to the invention produces a precursor acceptor for the synthesis of said compound and / or wherein said cell takes up a precursor acceptor from the cultivation medium for the synthesis of said compound. Said precursor acceptor is further elaborated in the Section "Acceptor" of the first aspect of the invention. Preferably, said cell is genetically engineered to import said precursor acceptor, wherein said cell comprises a nucleic acid encoding a transporter that is capable to import said precursor acceptor. Such transporter is for example a membrane protein belonging to the major facilitator superfamily (MFS), the ATP-binding cassette (ABC) transporter family or the PTS system involved in the uptake of e.g., mono-, di- and / or oligosaccharides. Said ABC transporter as disclosed throughout the application and claims is preferably oppF from E. coli (UniProt ID P77737, sequence version 01), ImrA from Lactococcus lactis subsp. lactis bv. diacetylactis (UniProt ID A0A1V0NEL4, sequence version 01) or Blon_2475 from Bifidobacterium longum subsp. infantis (UniProt ID B7GPD4, sequence version 01).

[0296] In another preferred embodiment, said cell according to the invention, said cell is able to take up an acceptor as disclosed herein (it is referred to the Section "Acceptor" of the first aspect of the invention) from the cultivation medium, preferably said cell is genetically engineered to import said acceptor, wherein said cell comprises a nucleic acid encoding a transporter that is capable to import said acceptor. Such transporter is for example a membrane protein belonging to the major facilitator superfamily (MFS), the ATP-binding cassette (ABC) transporter family or the PTS system involved in the uptake of e.g., mono- , di- and / or oligosaccharides.

[0297] In an optional embodiment, said cell according to the invention comprises a pathway for production of phosphoenolypyruvate (PEP), more preferably that said cell is genetically modified for enhanced synthesis and / or supply of PEP compared to a non-modified progenitor cell.

[0298] In a preferred embodiment and as a means for enhanced production and / or supply of PEP, one or more PEP-dependent, sugar-transporting phosphotransferase system(s) is / are disrupted such as but not limited to: 1) the N-acetyl-D-glucosamine Npi-phosphotransferase (EC 2.7.1.193), which is for instance encoded by the nagE gene (or the cluster nagABCD) in E. coli or Bacillus species, 2) ManXYZ which encodes the Enzyme II Man complex (mannose PTS permease, protein-Npi- phosphohistidine-D-mannose phosphotransferase) that imports exogenous hexoses (mannose, glucose, glucosamine, fructose, 2- deoxyglucose, mannosamine, N-acetylglucosamine, etc.) and releases the phosphate esters into the cell cytoplasm, 3) the glucose-specific PTS transporter (for instance encoded by PtsG / Crr) which takes up glucose and forms glucose-6-phosphate in the cytoplasm, 4) the sucrose-specific PTS transporter which takes up sucrose and forms sucrose-6-phosphate in the cytoplasm, 5) the fructose-specific PTS transporter (for instance encoded by the genes fruA and fruB and the kinase fruK which takes up fructose and forms in a first step fructose-l-phosphate and in a second step fructosel,6 bisphosphate, 6) the lactose PTS transporter (for instance encoded by lacE in Lactococcus easel) which takes up lactose and forms lactose- 6-phosphate, 7) the galactitol-specific PTS enzyme which takes up galactitol and / or sorbitol and forms galactitol-l-phosphate or sorbitol-6-phosphate respectively, 8) the mannitol-specific PTS enzyme which takes up mannitol and / or sorbitol and forms mannitol-l-phosphate or sorbitol-6-phosphate respectively, and 9) the trehalose-specific PTS enzyme which takes up trehalose and forms trehalose-6-phosphate.

[0299] In another and / or additional preferred embodiment and as a means for enhanced production and / or supply of PEP, the full PTS system is disrupted by disrupting the PtsIH / Crr gene cluster.

[0300] In another and / or additional preferred embodiment, the cell is further modified to compensate for the deletion of a PTS system of a carbon source by the introduction and / or overexpression of the corresponding permease. These are e.g. permeases or ABC transporters that comprise but are not limited to transporters that specifically import lactose such as e.g. the transporter encoded by the LacY gene from E. coli, sucrose such as e.g. the transporter encoded by the cscB gene from E. coli, glucose such as e.g. the transporter encoded by the galP gene from E. coli, fructose such as e.g. the transporter encoded by the frul gene from Streptococcus mutans, or the Sorbitol / mannitol ABC transporter such as the transporter encoded by the cluster SmoEFGK of Rhodobacter sphaeroides, the trehalose / sucrose / maltose transporter such as the transporter encoded by the gene cluster ThuEFGK of Sinorhizobium meliloti and the N- acetylglucosamine / galactose / glucose transporter such as the transporter encoded by NagP otShewanella oneidensis. Examples of combinations of PTS deletions with overexpression of alternative transporters are: 1) the deletion of the glucose PTS system, e.g. ptsG gene, combined with the introduction and / or overexpression of a glucose permease (e.g. galP of glcP), 2) the deletion of the fructose PTS system, e.g. one or more of the fruB, fruA, fruK genes, combined with the introduction and / or overexpression of fructose permease, e.g. frul, 3) the deletion of the lactose PTS system, combined with the introduction and / or overexpression of lactose permease, e.g. LacY, and / or 4) the deletion of the sucrose PTS system, combined with the introduction and / or overexpression of a sucrose permease, e.g. cscB.

[0301] In a further preferred embodiment, the cell is modified to compensate for the deletion of a PTS system of a carbon source by the introduction of carbohydrate kinases, such as glucokinase (EC 2.7.1.1, EC 2.7.1.2, EC 2.7.1.63), galactokinase (EC 2.7.1.6), and / or fructokinase (EC 2.7.1.3, EC 2.7.1.4).

[0302] In another and / or additional preferred embodiment and as a means for enhanced production and / or supply of PEP, the cell is modified by the introduction of or modification in any one or more of the list comprising phosphoenolpyruvate synthase activity (EC: 2.7.9.2 encoded for instance in E. coli by ppsA), phosphoenolpyruvate carboxykinase activity (EC 4.1.1.32 or EC 4.1.1.49 encoded for instance in Corynebacterium glutamicum by PCK or in E. coli by pckA, resp.), phosphoenolpyruvate carboxylase activity (EC 4.1.1.31 encoded for instance in E. coli by ppc), oxaloacetate decarboxylase activity (EC 4.1.1.112 encoded for instance in E. coli by eda), pyruvate kinase activity (EC 2.7.1.40 encoded for instance in E. coli by pykA and pykF), pyruvate carboxylase activity (EC 6.4.1.1 encoded for instance in B. subtilis by pyc) and malate dehydrogenase activity (EC 1.1.1.38 or EC 1.1.1.40 encoded for instance in E. coli by maeA or maeB, resp.).

[0303] In another and / or additional preferred embodiment and as a means for enhanced production and / or supply of PEP, the cell is modified by a reduced activity of phosphoenolpyruvate carboxylase activity, and / or pyruvate kinase activity, preferably a deletion of the genes encoding for phosphoenolpyruvate carboxylase, the pyruvate carboxylase activity and / or pyruvate kinase.

[0304] In an optional embodiment, said cell according to the invention is genetically modified for reduced production of acetate compared to a non-modified progenitor cell. Said modification can be any one or more chosen from the group comprising overexpression of an acetyl-coenzyme A synthetase, a full or partial knock-out or rendered less functional pyruvate dehydrogenase and a full or partial knock-out or rendered less functional lactate dehydrogenase.

[0305] Preferably, the cell is modified in the expression or activity of at least one acetyl-coenzyme A synthetase like e.g. acs from E. coli, S. cerevisiae, H. sapiens, M. musculus. In a preferred embodiment, said acetyl- coenzyme A synthetase is an endogenous protein of the cell with a modified expression or activity, preferably said endogenous acetyl-coenzyme A synthetase is overexpressed; alternatively, said acetyl- coenzyme A synthetase is a heterologous protein that is heterogeneously introduced and expressed in said cell, preferably overexpressed. Said endogenous acetyl-coenzyme A synthetase can have a modified expression in the cell which also expresses a heterologous acetyl-coenzyme A synthetase.

[0306] In an optional embodiment, said cell is genetically modified in the expression or activity of at least one pyruvate dehydrogenase like e.g. from E. coli, S. cerevisiae, H. sapiens and R. norvegicus. In a preferred embodiment, the cell has been modified to have at least one partially or fully knocked out or mutated pyruvate dehydrogenase encoding gene by means generally known by the person skilled in the art resulting in at least one protein with less functional or being disabled for pyruvate dehydrogenase activity. In a more preferred embodiment, the cell has a full knock-out in the poxB encoding gene resulting in a cell lacking pyruvate dehydrogenase activity.

[0307] In an optional embodiment, said cell is genetically modified in the expression or activity of at least one lactate dehydrogenase like e.g. from E. coli, S. cerevisiae, H. sapiens and R. norvegicus. In a preferred embodiment, the cell has been modified to have at least one partially or fully knocked out or mutated lactate dehydrogenase encoding gene by means generally known by the person skilled in the art resulting in at least one protein with less functional or being disabled for lactate dehydrogenase activity. In a more preferred embodiment, the cell has a full knock-out in the IdhA encoding gene resulting in a cell lacking lactate dehydrogenase activity.

[0308] In an optional embodiment said cell comprises a lower or reduced expression and / or abolished, impaired, reduced or delayed activity of any one or more of the proteins comprising beta-galactosidase, galactoside O-acetyltransferase, N-acetylglucosamine-6-phosphate deacetylase, glucosamine-6-phosphate deaminase, N-acetylglucosamine repressor, ribonucleotide monophosphatase, EIICBA-Nag, UDP- glucose:undecaprenyl-phosphate glucose-l-phosphate transferase, L-fuculokinase, L-fucose isomerase, N-acetylneuraminate lyase, N-acetylmannosamine kinase, N-acetylmannosarnine-6-phosphate 2- epimerase, EIIAB-Man, EIIC-Man, EIID-Man, ushA, galactose-l-phosphate uridylyltransferase, glucose-l- phosphate adenylyltransferase, glucose-l-phosphatase, ATP-dependent 6-phosphofructokinase isozyme 1, ATP-dependent 6-phosphofructokinase isozyme 2, glucose-6-phosphate isomerase, aerobic respiration control protein, transcriptional repressor IcIR, Ion protease, glucose-specific translocating phosphotransferase enzyme IIBC component ptsG, glucose-specific translocating phosphotransferase (PTS) enzyme IIBC component malX, enzyme I IAGlc, beta-glucoside specific PTS enzyme II, fructose-specific PTS multiphosphoryl transfer protein FruA and FruB, ethanol dehydrogenase aldehyde dehydrogenase, pyruvate-formate lyase, acetate kinase, phosphoacyltransferase, phosphate acetyltransferase, pyruvate decarboxylase.

[0309] Specific embodiments

[0310] The present invention preferably relates to the following specific embodiments:

[0311] 1. A method for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose- beta-l,4-Zi-Zz-R, the method comprising the steps of: providing (i) an acceptor comprising galactose-beta-l,4-Zi-Zz-R, (ii) UDP-N-acetylglucosamine (UDP-GIcNAc) and (iii) a beta-1, 6-N-acetylglucosaminyltransferase; and bringing said (i), (ii) and (iii) into contact with each other under conditions such that said beta- 1,6-N-acetylglucosaminyltransferase transfers a N-acetylglucosamine (GIcNAc) from UDP- GIcNAc to said acceptor in an beta-1, 6-glycosidic linkage as to produce a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0312] 2. A method according to embodiment 1, the method comprising the steps of: providing (i) said acceptor comprising galactose-beta-l,4-Zi-Z2-R, (ii) UDP-N- acetylglucosamine (UDP-GIcNAc), (iii) said beta-1, 6-N-acetylglucosaminyltransferase, and (iv) one or more additional glycosyltransferase(s) and their corresponding nucleotide sugar; and bringing: o said (i), (ii), (iii) and (iv) into contact with each other, or o said (i), (ii) an (iii) into contact with each other and subsequently with (iv), or o said (i) and (iv) into contact with each other and subsequently with (ii) and (iii), under conditions such that said beta-1, 6-N-acetylglucosaminyltransferase transfers a N- acetylglucosamine (GIcNAc) from UDP-GIcNAc to said acceptor in an beta-1,6- glycosidic linkage as to produce a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta- 1,4-Z1-Z2-R; wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0313] 3. A method according to embodiment 1 or 2, wherein at least said beta-1, 6-N- acetylglucosaminyltransferase is provided by a cell.

[0314] 4. A method according to embodiment 1 or 2, wherein at least said beta-1, 6-N- acetylglucosaminyltransferase is provided as part of a cell extract.

[0315] 5. A method according to embodiment 3, the method comprising the steps of: providing said cell in a suitable cultivation medium, wherein said cell expresses said beta-1, 6- N-acetylglucosaminyltransferase and optionally expresses one or more additional glycosyltransferase(s); providing said UDP-GIcNAc intracellularly, wherein said UDP-GIcNAc is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; providing said acceptor intracellularly, wherein said acceptor is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; optionally providing each corresponding nucleotide sugar of said one or more additional glycosyltransferase(s) intracellularly, wherein said nucleotide sugar is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; cultivating said cell in the suitable cultivation medium under conditions such that a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R is produced, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and optionally separating the produced compound from the cultivation broth.

[0316] 6. A method according to embodiment 5, wherein said method is a method for the fermentative production of said compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R.

[0317] 7. A method according to embodiment 3, 5 or 6, wherein said cell is genetically engineered for the production of said compound.

[0318] 8. A method according to any one of embodiments 3 to 7, wherein said cell is a microorganism.

[0319] 9. A method according to any one of embodiments 3 to 8, wherein said cell is a bacterium.

[0320] 10. A method according to any one of embodiments 1 to 9, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises a domain R(X)io-

[0321] 2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE; wherein X is any amino acid; Xi is any amino acid except for F and P; X2is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, Xg is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y and Xg is any amino acid except for A; and wherein: (i) the first amino acid of SEQ ID NO 01 (i.e. R) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R199 of a reference beta-1, 6- N-acetylglucosaminyltransferase represented by SEQ ID NO 03;

[0322] (ii) XsXgXyXg of SEQ ID NO 01 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with G234-T235-A236-Y237 of a reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and

[0323] (iii) the last two amino acids of SEQ ID NO 01 (i.e. DE) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with D268-E269 of a reference beta- 1,6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03.

[0324] 11. A method according to any one of embodiments 1 to 10, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises the IPR domain IPR003406 as defined by InterPro 102.0.

[0325] 12. A method according to any one of embodiments 1 to 11, wherein said beta-1, 6-N- acetylglucosaminyltransferase is not naturally present in a human and is not naturally present in a mouse.

[0326] 13. A method according to any one of embodiments 1 to 12, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237, wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237, and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively.

[0327] 14. A method according to any one of embodiments 1 to 13, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237, wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively; or d) that is a functional fragment of a polypeptide that has at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237 , and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively.

[0328] 15. A method according to any one of embodiments 1 to 12, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 238 to 472; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, and wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively.

[0329] 16. A method according to any one of embodiments 1 to 15, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises a domain represented by SEQ ID NO 02.

[0330] 17. A method according to embodiment 2 or 5, wherein said one or more additional glycosyltransferases are involved in the production of said compound.

[0331] 18. A method according to any one of embodiments 1 to 17, wherein said acceptor comprises GIcNAc- beta-l,3-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0332] 19. A method according to any one of embodiments 1 to 18, wherein said acceptor comprises galactose- beta-GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0333] 20. A method according to any one of embodiments 1 to 19, wherein Z2 is absent or is a lacto-N- neotetraose (LNnT)-containing oligosaccharide or is a lacto-N-tetraose (LNT)-containing oligosaccharide.

[0334] 21. A method according to any one of embodiments 1 to 20, wherein said acceptor is a mammalian milk oligosaccharide.

[0335] 22. A method according to any one of embodiments 1 to 21, wherein said compound is a saccharide, preferably an oligosaccharide.

[0336] 23. A method according to any one of embodiments 1 to 22, wherein said compound is a mammalian milk oligosaccharide.

[0337] 24. A cell for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta- 1,4-Zi-Zj-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and wherein said cell comprises a beta-1, 6-N-acetylglucosaminyltransferase comprising a domain R(X)IO-2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE; wherein X is any amino acid; Xi is any amino acid except for F and P; X2is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, Xg is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y and Xg is any amino acid except for A; and wherein:

[0338] (i) the first amino acid of SEQ ID NO 01 (i.e. R) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R199 of a reference beta-1, 6- N-acetylglucosaminyltransferase represented by SEQ ID NO 03;

[0339] (ii) X5X6X7Xg of SEQ ID NO 01 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with G234-T235-A236-Y237 of a reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and

[0340] (iii) the last two amino acids of SEQ ID NO 01 (i.e. DE) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with D268-E269 of a reference beta- 1,6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03. A cell according to embodiment 24, wherein said cell is genetically engineered for the production of said compound. A cell according to embodiment 24 or 25, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises the IPR domain IPR003406 as defined by InterPro 102.0. A cell according to any one of embodiments 24 to 26, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237, wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237, and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively. A cell according to any one of embodiments 24 to 27, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237 , wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237 , respectively; or d) that is a functional fragment of a polypeptide that has at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237 , and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237 , respectively.

[0341] 29. A cell according to any one of embodiments 24 to 26, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 238 to 472; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, and wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively.

[0342] 30. A cell according to any one of embodiments 24 to 29, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises a domain represented by SEQ ID NO 02.

[0343] 31. A cell according to any one of embodiments 24 to 30, wherein said cell is a microorganism.

[0344] 32. A cell according to any one of embodiments 24 to 31, wherein said cell is a bacterium.

[0345] 33. A cell according to any one of embodiments 24 to 32, wherein said cell is adapted for the production of a functional disulfide bond containing protein.

[0346] 34. A cell according to embodiment 33, wherein the expression of a glutathione reductase and / or a thioredoxin reductase is lowered or diminished compared to an unmodified cell.

[0347] 35. A cell according to any one of embodiments 24 to 34, wherein said cell further comprises one or more additional glycosyltransferases that are involved in the production of said compound.

[0348] 36. A cell according to embodiment 35, wherein said one or more additional glycosyltransferases are selected from the list consisting of a beta-1, 3-N-acetylglucosaminyltransferase, a beta-1, 3- galactosyltransferase, a beta-1, 4-galactosyltransferase, a fucosyltransferase and a sialyltransferase.

[0349] The present invention more preferably relates to the following specific embodiments: A method for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose- beta-l,4-Zi-Zz-R, the method comprising the steps of: providing (i) an acceptor comprising galactose-beta-l,4-Zi-Z2-R, (ii) UDP-N-acetylglucosamine (UDP-GIcNAc) and (iii) a beta-1, 6-N-acetylglucosaminyltransferase; and bringing said (i), (ii) and (iii) into contact with each other under conditions such that said beta- 1,6-N-acetylglucosaminyltransferase transfers a N-acetylglucosamine (GIcNAc) from UDP- GIcNAc to said acceptor in an beta-1, 6-glycosidic linkage as to produce a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises a domain R(X)io- 2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE; wherein X is any amino acid; Xi is any amino acid except for F and P; X2 is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, Xg is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y and Xg is any amino acid except for A; and wherein:

[0350] (i) the first amino acid of SEQ ID NO 01 (i.e. R) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R199 of a reference beta-1, 6- N-acetylglucosaminyltransferase represented by SEQ ID NO 03;

[0351] (ii) X5XgX7Xg of SEQ ID NO 01 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with G234-T235-A236-Y237 of a reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and

[0352] (iii) the last two amino acids of SEQ ID NO 01 (i.e. DE) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with D268-E269 of a reference beta- 1,6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03. A method according to embodiment 1, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises the IPR domain IPR003406 as defined by InterPro 102.0. A method according to embodiment 1 or 2, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237, wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237 , and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237 , respectively.

[0353] 4. A method according to any one of embodiments 1 to 3, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237, wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively; or d) that is a functional fragment of a polypeptide that has at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237, and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively.

[0354] 5. A method according to embodiment 1 or 2, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 238 to 472; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, and wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively.

[0355] 6. A method according to any one of embodiments 1 to 5, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises a domain represented by SEQ ID NO 02.

[0356] 7. A method according to any one of embodiment 1 to 6, the method comprising the steps of: providing (i) said acceptor comprising galactose-beta-l,4-Zi-Zz-R, (ii) UDP-N- acetylglucosamine (UDP-GIcNAc), (iii) said beta-1, 6-N-acetylglucosaminyltransferase, and (iv) one or more additional glycosyltransferase(s) and their corresponding nucleotide sugar; and bringing: o said (i), (ii), (iii) and (iv) into contact with each other, or o said (i), (ii) an (iii) into contact with each other and subsequently with (iv), or o said (i) and (iv) into contact with each other and subsequently with (ii) and (iii), under conditions such that said beta-1, 6-N-acetylglucosaminyltransferase transfers a N- acetylglucosamine (GIcNAc) from UDP-GIcNAc to said acceptor in an beta-1,6- glycosidic linkage as to produce a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta- 1,4-ZI-Z2-R; wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0357] 8. A method according to any one of embodiments 1 to 7, wherein at least said beta-1, 6-N- acetylglucosaminyltransferase is provided as part of a cell extract.

[0358] 9. A method according to any one of embodiments 1 to 7, wherein at least said beta-1, 6-N- acetylglucosaminyltransferase is provided by a cell.

[0359] 10. A method according to embodiment 9, wherein said cell is a microorganism.

[0360] 11. A method according to embodiment 9 or 10, wherein said cell is a bacterium.

[0361] 12. A method according to any one of embodiments 9 to 11, wherein said cell is genetically engineered for the production of said compound.

[0362] 13. A method according to any one of embodiments 9 to 12, the method comprising the steps of: providing said cell in a suitable cultivation medium, wherein said cell expresses said beta-1, 6- N-acetylglucosaminyltransferase and optionally expresses one or more additional glycosyltransferase(s); providing said UDP-GIcNAc intracellularly, wherein said UDP-GIcNAc is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; providing said acceptor intracellularly, wherein said acceptor is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; optionally providing each corresponding nucleotide sugar of said one or more additional glycosyltransferase(s) intracellularly, wherein said nucleotide sugar is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; cultivating said cell in the suitable cultivation medium under conditions such that a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R is produced, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and optionally separating the produced compound from the cultivation broth.

[0363] 14. A method according to embodiment 7 or 13, wherein said one or more additional glycosyltransferases are involved in the production of said compound.

[0364] 15. A method according to any one of embodiments 1 to 14, wherein said acceptor comprises GIcNAc- beta-l,3-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0365] 16. A method according to any one of embodiments 1 to 15, wherein said acceptor comprises galactose- beta-GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0366] 17. A method according to any one of embodiments 1 to 16, wherein Z2 is absent or is a lacto-N- neotetraose (LNnT)-containing oligosaccharide or is a lacto-N-tetraose (LNT)-containing oligosaccharide.

[0367] 18. A method according to any one of embodiments 1 to 17, wherein said acceptor is a mammalian milk oligosaccharide.

[0368] 19. A method according to any one of embodiments 1 to 18, wherein said compound is a saccharide, preferably an oligosaccharide.

[0369] 20. A method according to any one of embodiments 1 to 19, wherein said compound is a mammalian milk oligosaccharide.

[0370] 21. A cell for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta- 1,4-ZI-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and wherein said cell comprises a beta-1, 6-N-acetylglucosaminyltransferase comprising a domain R(X)IO-2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE; wherein X is any amino acid; Xi is any amino acid except for F and P; X2 is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, Xg is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y and Xg is any amino acid except for A; and wherein:

[0371] (i) the first amino acid of SEQ ID NO 01 (i.e. R) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R199 of a reference beta-1, 6- N-acetylglucosaminyltransferase represented by SEQ ID NO 03;

[0372] (ii) X5XgX7Xg of SEQ ID NO 01 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with G234-T235-A236-Y237 of a reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and

[0373] (iii) the last two amino acids of SEQ ID NO 01 (i.e. DE) should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with D268-E269 of a reference beta- 1,6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03.

[0374] 22. A cell according to embodiment 21, wherein said cell is genetically engineered for the production of said compound.

[0375] 23. A cell according to embodiment 21 or 22, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises the IPR domain IPR003406 as defined by InterPro 102.0. 24. A cell according to any one of embodiments 21 to 23, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237, wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237, and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively.

[0376] 25. A cell according to any one of embodiments 21 to 24, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 03 to 237; or b) having at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 237, wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively; or d) that is a functional fragment of a polypeptide that has at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 237, and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 237, respectively.

[0377] 26. A cell according to any one of embodiments 21 to 23, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence: a) selected from the list consisting of SEQ ID NO 238 to 472; or b) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472; or c) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively; or d) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, and wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively. 27. A cell according to any one of embodiments 21 to 26, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises a domain represented by SEQ. ID NO 02.

[0378] 28. A cell according to any one of embodiments 21 to 27, wherein said cell is a microorganism.

[0379] 29. A cell according to any one of embodiments 21 to 28, wherein said cell is a bacterium.

[0380] 30. A cell according to any one of embodiments 21 to 29, wherein said cell is adapted for the production of a functional disulfide bond containing protein.

[0381] 31. A cell according to embodiment 30, wherein the expression of a glutathione reductase and / or a thioredoxin reductase is lowered or diminished compared to an unmodified cell.

[0382] 32. A cell according to any one of embodiments 21 to 31, wherein said cell further comprises one or more additional glycosyltransferases that are involved in the production of said compound.

[0383] 33. A cell according to embodiment 32, wherein said one or more additional glycosyltransferases are selected from the list consisting of a beta-1, 3-N-acetylglucosaminyltransferase, a beta-1, 3- galactosyltransferase, a beta-1, 4-galactosyltransferase, a fucosyltransferase and a sialyltransferase.

[0384] The present invention even more preferably relates to the following specific embodiments:

[0385] 1. A method for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose- beta-l,4-Zi-Zz-R, the method comprising the steps of: providing (i) an acceptor comprising galactose-beta-l,4-Zi-Zz-R, (ii) UDP-N-acetylglucosamine (UDP-GIcNAc) and (iii) a beta-1, 6-N-acetylglucosaminyltransferase; and bringing said (i), (ii) and (iii) into contact with each other under conditions such that said beta- 1,6-N-acetylglucosaminyltransferase transfers a N-acetylglucosamine from UDP-GIcNAc to said acceptor in an beta-1, 6-glycosidic linkage as to produce a compound comprising N- acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine, wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0386] 2. A method according to embodiment 1, the method comprising the steps of: providing (i) said acceptor comprising galactose-beta-l,4-Zi-Z2-R, (ii) UDP-N- acetylglucosamine, (iii) said beta-1, 6-N-acetylglucosaminyltransferase, and (iv) one or more additional glycosyltransferase(s) and their corresponding nucleotide sugar; and bringing: o said (i), (ii), (iii) and (iv) into contact with each other, or o said (i), (ii) an (iii) into contact with each other and subsequently with (iv), or o said (i) and (iv) into contact with each other and subsequently with (ii) and (iii), under conditions such that said beta-1, 6-N-acetylglucosaminyltransferase transfers a N- acetylglucosamine from UDP-GIcNAc to said acceptor in an beta-1,6- glycosidic linkage as to produce a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R; wherein Zi is glucose or N-acetylglucosamine, wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0387] 3. A method according to embodiment 1 or 2, wherein at least said beta-1, 6-N- acetylglucosaminyltransferase is provided by a cell.

[0388] 4. A method according to embodiment 1 or 2, wherein at least said beta-1, 6-N- acetylglucosaminyltransferase is provided as part of a cell extract.

[0389] 5. A method according to embodiment 3, the method comprising the steps of: providing said cell in a suitable cultivation medium, wherein said cell expresses said beta-1, 6- N-acetylglucosaminyltransferase and optionally expresses one or more additional glycosyltransferase(s); providing said UDP-GIcNAc intracellularly, wherein said UDP-GIcNAc is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; providing said acceptor intracellularly, wherein said acceptor is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; optionally providing each corresponding nucleotide sugar of said one or more additional glycosyltransferase(s) intracellularly, wherein said nucleotide sugar is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; cultivating said cell in the suitable cultivation medium under conditions such that a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R is produced, wherein Zi is glucose or N-acetylglucosamine, wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and optionally separating the produced compound from the cultivation broth.

[0390] 6. A method according to embodiment 5, wherein said method is a method for the fermentative production of said compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R.

[0391] 7. A method according to embodiment 3, 5 or 6, wherein said cell is genetically engineered for the production of said compound.

[0392] 8. A method according to any one of embodiments 3 to 7, wherein said cell is a microorganism.

[0393] 9. A method according to any one of embodiments 3 to 8, wherein said cell is a bacterium.

[0394] 10. A method according to any one of embodiments 1 to 9, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises the IPR domain IPR003406 as defined by InterPro 102.0.

[0395] 11. A method according to any one of embodiments 1 to 10, wherein said beta-1, 6-N- acetylglucosaminyltransferase is not naturally present in a human and is not naturally present in a mouse.

[0396] 12. A method according to any one of embodiments 1 to 11, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:

[0397] (i) selected from the list consisting of SEQ ID NO 03 to 17; or

[0398] (ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 17; or

[0399] (iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 17, wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 17, respectively; or

[0400] (iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 17, and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 17, respectively. A method according to any one of embodiments 1 to 12, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:

[0401] (i) selected from the list consisting of SEQ ID NO 03 to 17; or

[0402] (ii) having at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 17; or

[0403] (iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 17, wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 17, respectively; or

[0404] (iv) that is a functional fragment of a polypeptide that has at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 17, and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 17, respectively. A method according to any one of embodiments 1 to 11, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises a domain R(X)io-

[0405] 2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE, i.e. SEQ ID NO 01; wherein X is any amino acid; Xi is any amino acid except for F and P; X2is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, Xg is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y and Xg is any amino acid except for A; and wherein:

[0406] (i) the first amino acid of SEQ ID NO 01, i.e. R, should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R199 of a reference beta-1, 6- N-acetylglucosaminyltransferase represented by SEQ ID NO 03;

[0407] (ii) X5XgX7Xg of SEQ ID NO 01 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with G234-T235-A236-Y237 of a reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and (iii) the last two amino acids of SEQ ID NO 01, i.e. DE, should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with D268-E269 of a reference beta- 1,6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03. A method according to any one of embodiments 1 to 11 or 14, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:

[0408] (i) selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17; or

[0409] (ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17; or

[0410] (iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17, wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17, respectively; or

[0411] (iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17, and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17, respectively. A method according to any one of embodiments 1 to 11, 14 or 15, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:

[0412] (i) selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17; or

[0413] (ii) having at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17; or

[0414] (iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17, wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17, respectively; or

[0415] (iv) that is a functional fragment of a polypeptide that has at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, preferably SEQ ID NO 03 to 09 and 12 to 17, and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , preferably SEQ ID NO 03 to 09 and 12 to 17, respectively.

[0416] 17. A method according to any one of embodiments 1 to 11, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:

[0417] (i) selected from the list consisting of SEQ ID NO 238 to 472; or

[0418] (ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472; or

[0419] (iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively; or

[0420] (iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, and wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively.

[0421] 18. A method according to any one of embodiments 1 to 11 or 14, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:

[0422] (i) selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472; or

[0423] (ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472; or

[0424] (iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472, respectively; or

[0425] (iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472, and wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472, respectively.

[0426] 19. A method according to any one of embodiments 1 to 18, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises a domain represented by SEQ ID NO 02.

[0427] 20. A method according to embodiment 2 or 5, wherein said one or more additional glycosyltransferases are involved in the production of said compound.

[0428] 21. A method according to any one of embodiments 1 to 20, wherein said acceptor comprises GIcNAc- beta-l,3-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid. 22. A method according to any one of embodiments 1 to 21, wherein said acceptor comprises galactose- beta-GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

[0429] 23. A method according to any one of embodiments 1 to 22, wherein Z2 is absent or is a lacto-N- neotetraose (LNnT)-containing oligosaccharide or is a lacto-N-tetraose (LNT)-containing oligosaccharide.

[0430] 24. A method according to any one of embodiments 1 to 23, wherein said acceptor is a mammalian milk oligosaccharide.

[0431] 25. A method according to any one of embodiments 1 to 24, wherein said compound is a saccharide, preferably an oligosaccharide.

[0432] 26. A method according to any one of embodiments 1 to 25, wherein said compound is a mammalian milk oligosaccharide.

[0433] 27. A cell for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta- 1,4-ZI-Z2-R, wherein Zi is glucose or N-acetylglucosamine , wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and wherein said cell comprises a beta-1, 6-N-acetylglucosaminyltransferase comprising a domain R(X)io- 2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE, i.e. SEQ ID NO 01; wherein X is any amino acid; Xi is any amino acid except for F and P; X2 is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, X6is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y and X9is any amino acid except for A; and wherein:

[0434] (i) the first amino acid of SEQ ID NO 01, i.e. R, should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R199 of a reference beta-1, 6- N-acetylglucosaminyltransferase represented by SEQ ID NO 03;

[0435] (ii) XsXgXyXg of SEQ ID NO 01 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with G234-T235-A236-Y237 of a reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and

[0436] (iii) the last two amino acids of SEQ ID NO 01, i.e. DE, should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with D268-E269 of a reference beta- 1,6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03.

[0437] 28. A cell according to embodiment 27, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises the IPR domain IPR003406 as defined by InterPro 102.0.

[0438] 29. A cell for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta- 1,4-ZI-Z2-R, wherein Zi is glucose or N-acetylglucosamine , wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and wherein said cell comprises a beta-1, 6-N-acetylglucosaminyltransferase comprising an amino acid sequence:

[0439] (i) selected from the list consisting of SEQ ID NO 03 to 17; or

[0440] (ii) having at least 80.0%, preferably at least 90.0%, sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 17; or

[0441] (iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 17, wherein the length of said functional fragment is at least 80.0%, preferably at least 90.0%, of the length of any one selected from the list consisting of SEQ ID NO 03 to 17, respectively; or

[0442] (iv) that is a functional fragment of a polypeptide that has at least 80.0%, preferably at least 90.0%, sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 17, and wherein the length of said functional fragment is at least 80.0%, preferably at least 90.0%, of the length of any one selected from the list consisting of SEQ ID NO 03 to 17, respectively preferably wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises the IPR domain IPR003406 as defined by InterPro 102.0. A cell according to embodiment 27 or 28, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises an amino acid sequence:

[0443] (i) selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or

[0444] (ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or

[0445] (iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, respectively; or

[0446] (iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, respectively. A cell according to embodiment 27, 28 or 30, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises an amino acid sequence:

[0447] (i) selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or

[0448] (ii) having at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or

[0449] (iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, respectively; or (iv) that is a functional fragment of a polypeptide that has at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , respectively. 2. A cell according to embodiment 27 or 28, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises an amino acid sequence:

[0450] (i) selected from the list consisting of SEQ ID NO 238 to 472, preferably SEQ ID NO 238 to 244 and 247 to 472; or

[0451] (ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, preferably SEQ ID NO 238 to 244 and 247 to 472; or

[0452] (iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, preferably SEQ ID NO 238 to 244 and 247 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, preferably SEQ ID NO 238 to 244 and 247 to 472, respectively; or

[0453] (iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, preferably SEQ ID NO 238 to 244 and 247 to 472, and wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, preferably SEQ ID NO 238 to 244 and 247 to 472, respectively.

[0454] 33. A cell according to any one of embodiments 27 to 32, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises a domain represented by SEQ ID NO 02.

[0455] 34. A cell according to any one of embodiments 27 to 33, wherein said cell is genetically engineered for the production of said compound.

[0456] 35. A cell according to any one of embodiments 27 to 34, wherein said cell is a microorganism.

[0457] 36. A cell according to any one of embodiments 27 to 35, wherein said cell is a bacterium.

[0458] 37. A cell according to any one of embodiments 27 to 36, wherein said cell is adapted for the production of a functional disulfide bond containing protein.

[0459] 38. A cell according to embodiment 37, wherein the expression of a glutathione reductase and / or a thioredoxin reductase is lowered or diminished compared to an unmodified cell.

[0460] 39. A cell according to any one of embodiments 27 to 38, wherein said cell further comprises one or more additional glycosyltransferases that are involved in the production of said compound.

[0461] 40. A cell according to embodiment 39, wherein said one or more additional glycosyltransferases are selected from the list consisting of a beta-1, 3-N-acetylglucosaminyltransferase, a beta-1, 3- galactosyltransferase, a beta-1, 4-galactosyltransferase, a fucosyltransferase and a sialyltransferase. Definitions

[0462] The words used in this specification to describe the invention and its various embodiments are to be understood not only in the sense of their commonly defined meanings, but to include by special definition in this specification structure, material or acts beyond the scope of the commonly defined meanings. Thus, if an element can be understood in the context of this specification as including more than one meaning, then its use in a claim must be understood as being generic to all possible meanings supported by the specification and by the word itself.

[0463] The various aspects and embodiments of the invention disclosed herein are to be understood not only in the order and context specifically described in this specification, but to include any order and any combination thereof. Each embodiment as identified herein may be combined together unless otherwise indicated. All publications, patents and patent applications cited in this specification are herein incorporated by reference in their entirety to the same extent as if each individual publication, patent or patent application was specifically and individually indicated to be incorporated by reference in its entirety. Unless specifically stated otherwise, all words used in the singular number shall be deemed to include the plural and vice versa. Unless defined otherwise, all technical and scientific terms used herein generally have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Generally, the nomenclature used herein and the laboratory procedures in cell culture, molecular genetics, organic chemistry and nucleic acid chemistry and hybridization described herein are those well-known and commonly employed in the art. Standard techniques are used for nucleic acid and peptide synthesis. Generally, enzymatic reactions and purification steps are performed according to the manufacturer's specifications.

[0464] In the drawings and specification, there have been disclosed embodiments of the invention, and although specific terms are employed, the terms are used in a descriptive sense only and not for purposes of limitation, the scope of the invention being set forth in the following claims. It must be understood that the illustrated embodiments have been set forth only for the purposes of example and that it should not be taken as limiting the invention. It will be apparent to those skilled in the art that alterations, other embodiments, improvements, details and uses can be made consistent with the letter and spirit of the invention herein and within the scope of this invention, which is limited only by the claims, construed in accordance with the patent law, including the doctrine of equivalents. In the claims which follow, reference characters used to designate claim steps are provided for convenience of description only, and are not intended to imply any particular order for performing the steps (unless specifically stated otherwise).

[0465] In this document and in its claims, the verbs "to comprise", "to have" and "to contain", and their conjugations are used in their non-limiting sense to mean that items following the word are included, but items not specifically mentioned are not excluded. The verb "to consist essentially of" means that e.g. a mixture as defined herein may comprise additional component(s) than the ones specifically identified, said additional component(s) not altering the unique characteristic of the invention. Throughout the document and claims, unless specifically stated otherwise, the verbs "to comprise", "to have" and "to contain", and their conjugations, may be preferably replaced by "to consist" (and its conjugations) or "to consist essentially of" (and its conjugations). In addition, reference to an element by the indefinite article "a" or "an" does not exclude the possibility that more than one of the element is present, unless the context clearly requires that there be one and only one of the elements. The indefinite article "a" or "an" thus usually means "at least one". Preferably, "a" and "an" are replaced with "one". The word "about" or "approximately" or "around" when used in association with a numerical value, parameter or numerical range such as amounts, volumes, volume ratios, volume percentages, weight ratios, weight percentages, or application rates of ingredients of a composition; means an amount, a volume, a volume ratio, a volume percentage, a weight ratio, a weight percentage, or an application rate that is recognized by those of ordinary skill in the art to provide a desired effect equivalent to that obtained from the specified amount, volume, volume ratios, volume percentages, weight ratio, weight percentage, or application rate; and is encompassed herein and should be construed in light of the number of reported significant digits and applying ordinary rounding techniques. Preferably, the word "about" or "approximately" or "around" when used in association with a numerical value (e.g. about 10) preferably means that the value may be the given value (of 10) more or less 15%, preferably 10%, more preferably 5%, even more preferably 1%, of the value.

[0466] Throughout the description and claims, unless specifically stated otherwise, the expression "from x to y", wherein x and y represent numerical values, refers to a range of numerical values wherein both x and y are included and wherein x represents the lowest value and y represents the highest value. Hence, both x and y are also included in the range in addition to any value in-between.

[0467] Throughout the application and claims, unless explicitly stated otherwise, the expressions "capable of...<verb>" and "capable to...<verb>" are preferably replaced with the active voice of said verb and vice versa. For example, the expression "capable of expressing" is preferably replaced with "expresses" and vice versa, i.e. "expresses" is preferably replaced with "capable of expressing".

[0468] Throughout the application and claims, the expression "one or more" is interchangeably used with "at least one".

[0469] The term "isolated" means altered "by the hand of man" from its natural state, i.e., if it occurs in nature, it has been changed or removed from its original environment, or both. For example, a polynucleotide or a polypeptide naturally present in a living organism is not "isolated," but the same polynucleotide or polypeptide separated from the coexisting materials of its natural state is "isolated", as the term is employed herein.

[0470] The terms "culture medium" and "cultivation medium" as used herein are used interchangeably and refer to the medium wherein the cell is cultivated. The term "cultivation broth" refers to the culture medium (with all of its components) wherein the cell is cultivated, the cell itself, and a compound comprising N- acetylglucosamine-beta-l,6-[N-acetylglucosamine-betal,3-]-galactose-beta-l,4-glucose-R according to the invention that is produced by the cell, i.e. inside (intracellularly) as well as outside (extracellularly) of the cell.

[0471] The term "modified expression" of a gene relates to a change in expression compared to the wild type expression of said gene. Said modified expression is either a lower or higher expression compared to the wild type, wherein the term "higher expression" is also defined as "overexpression" of said gene in the case of an endogenous gene or "expression" in the case of a heterologous gene that is not present in the wild type strain. Lower expression is obtained by means of common well-known technologies for a skilled person (such as the usage of siRNA, CrispR, CrispRi, recombineering, homologous recombination, ssDNA mutagenesis, RNAi, miRNA, asRNA, mutating genes, knocking-out genes, transposon mutagenesis,...) which are used to change the genes in such a way that they are less-able (i.e. statistically significantly 'less-able' compared to a functional wild-type gene) or completely unable (such as knocked-out genes) to produce functional final products. Overexpression or expression is obtained by means of common well- known technologies for a skilled person, wherein said gene is part of an "expression cassette" which relates to any sequence in which a promoter sequence, untranslated region sequence (containing either a ribosome binding sequence or Kozak sequence), a coding sequence (for instance a membrane protein gene sequence) and optionally a transcription terminator is present, and leading to the expression of a functional active protein. Said expression is either constitutive or conditional or regulated or tuneable. "Expression" of a transporter protein is defined as "overexpression" of the gene encoding said transporter protein in the case said gene is an endogenous gene or "expression" in the case the gene encoding said transporter protein is a heterologous gene that is not present in the wild type strain.

[0472] As used herein, the term "cell productivity index (CPI)" refers to the mass of the product (i.e. saccharide or saccharides according to the invention) produced by the cells divided by the mass of said cells in the culture.

[0473] A "genetic pathway" or "biosynthetic pathway" as used herein preferably refers to a set of at least two different coding sequences, where the coding sequences encode enzymes that catalyze different parts of a synthetic pathway to form a desired product (e.g., a compound comprising N-acetylglucosamine-beta- l,6-(N-acetylglucosamine-betal,3-)-galactose-beta-l,4-glucose-R, wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid). In a genetic pathway, a first encoded enzyme uses a substrate to make a first product which in turn is used as a substrate for a second encoded enzyme to make a second product. In some embodiments, the genetic pathway includes 3 or more members (e.g., 3, 4, 5, 6, 7, 8, 9, etc.), wherein the product of one encoded enzyme is the substrate for the next enzyme in the synthetic pat...

Claims

Claims1. A method for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose- beta-l,4-Zi-Zz-R, the method comprising the steps of: providing (i) an acceptor comprising galactose-beta-l,4-Zi-Z2-R, (ii) UDP-N-acetylglucosamine (UDP-GIcNAc) and (iii) a beta-1, 6-N-acetylglucosaminyltransferase; and bringing said (i), (ii) and (iii) into contact with each other under conditions such that said beta- 1,6-N-acetylglucosaminyltransferase transfers a N-acetylglucosamine from UDP-GIcNAc to said acceptor in an beta-1, 6-glycosidic linkage as to produce a compound comprising N- acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine, wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises a domain R(X)io- 2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE, i.e. SEQ ID NO 01; wherein X is any amino acid; Xi is any amino acid except for F and P; X2 is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, Xg is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y and Xg is any amino acid except for A; and wherein:(i) the first amino acid of SEQ ID NO 01, i.e. R, should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R199 of a reference beta-1, 6- N-acetylglucosaminyltransferase represented by SEQ ID NO 03;(ii) X5XgX7Xg of SEQ ID NO 01 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with G234-T235-A236-Y237 of a reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and(iii) the last two amino acids of SEQ ID NO 01, i.e. DE, should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with D268-E269 of a reference beta-1, 6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03.

2. A method according to claim 1, the method comprising the steps of: providing (i) said acceptor comprising galactose-beta-l,4-Zi-Z2-R, (ii) UDP-N- acetylglucosamine, (iii) said beta-1, 6-N-acetylglucosaminyltransferase, and (iv) one or more additional glycosyltransferase(s) and their corresponding nucleotide sugar; and bringing: o said (i), (ii), (iii) and (iv) into contact with each other, or o said (i), (ii) an (iii) into contact with each other and subsequently with (iv), or o said (i) and (iv) into contact with each other and subsequently with (ii) and (iii), under conditions such that said beta-1, 6-N-acetylglucosaminyltransferase transfers a N- acetylglucosamine from UDP-GIcNAc to said acceptor in an beta-1,6- glycosidic linkage as to produce a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R;wherein Zi is glucose or N-acetylglucosamine, wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

3. A method according to claim 1 or 2, wherein at least said beta-1, 6-N-acetylglucosaminyltransferase is provided by a cell.

4. A method according to claim 1 or 2, wherein at least said beta-1, 6-N-acetylglucosaminyltransferase is provided as part of a cell extract.

5. A method according to claim 3, the method comprising the steps of: providing said cell in a suitable cultivation medium, wherein said cell expresses said beta-1, 6- N-acetylglucosaminyltransferase and optionally expresses one or more additional glycosyltransferase(s); providing said UDP-GIcNAc intracellularly, wherein said UDP-GIcNAc is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; providing said acceptor intracellularly, wherein said acceptor is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; optionally providing each corresponding nucleotide sugar of said one or more additional glycosyltransferase(s) intracellularly, wherein said nucleotide sugar is produced intracellularly by said cell and / or is taken up by the cell from the cultivation medium; cultivating said cell in the suitable cultivation medium under conditions such that a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R is produced, wherein Zi is glucose or N-acetylglucosamine, wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and optionally separating the produced compound from the cultivation broth.

6. A method according to claim 5, wherein said method is a method for the fermentative production of said compound comprising N-acetylglucosamine-beta-l,6-galactose-beta-l,4-Zi-Z2-R.

7. A method according to claim 3, 5 or 6, wherein said cell is genetically engineered for the production of said compound.

8. A method according to any one of claims 3 to 7, wherein said cell is a microorganism.

9. A method according to any one of claims 3 to 8, wherein said cell is a bacterium.

10. A method according to any one of claims 1 to 9, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises the IPR domain IPR003406 as defined by InterPro 102.0.

11. A method according to any one of claims 1 to 10, wherein said beta-1, 6-N- acetylglucosaminyltransferase is not naturally present in a human and is not naturally present in a mouse.

12. A method according to any one of claims 1 to 11, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:(i) selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or(ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or(iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , respectively; or(iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , respectively.

13. A method according to any one of claims 1 to 12, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:(i) selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or(ii) having at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or(iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, respectively; or(iv) that is a functional fragment of a polypeptide that has at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, respectively.

14. A method according to any one of claims 1 to 12, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:(i) selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17; or(ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17; or(iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17, wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of 03 to 09 and 12 to 17, respectively; or(iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17, and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17,respectively.

15. A method according to any one of claims 1 to 12, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:(i) selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17; or(ii) having at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17; or(iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17, wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17, respectively; or(iv) that is a functional fragment of a polypeptide that has at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17, and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 17, respectively.

16. A method according to any one of claims 1 to 11, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises an amino acid sequence:(i) selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472; or(ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472; or(iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472, respectively; or(iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472, and wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 244 and 247 to 472, respectively.

17. A method according to any one of claims 1 to 16, wherein said beta-1, 6-N- acetylglucosaminyltransferase comprises a domain represented by SEQ ID NO 02.

18. A method according to claim 2 or 5, wherein said one or more additional glycosyltransferases are involved in the production of said compound.

19. A method according to any one of claims 1 to 18, wherein said acceptor comprises GlcNAc-beta-1,3- galactose-beta-l,4-Zi-Zz-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide,a protein and a lipid.

20. A method according to any one of claims 1 to 19, wherein said acceptor comprises galactose-beta- GlcNAc-beta-l,3-galactose-beta-l,4-Zi-Z2-R, wherein Zi is glucose or N-acetylglucosamine (GIcNAc), wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid.

21. A method according to any one of claims 1 to 20, wherein Z2 is absent or is a lacto-N-neotetraose (LNnT)-containing oligosaccharide or is a lacto-N-tetraose (LNT)-containing oligosaccharide.

22. A method according to any one of claims 1 to 21, wherein said acceptor is a mammalian milk oligosaccharide.

23. A method according to any one of claims 1 to 22, wherein said compound is a saccharide, preferably an oligosaccharide.

24. A method according to any one of claims 1 to 23, wherein said compound is a mammalian milk oligosaccharide.

25. A cell for the production of a compound comprising N-acetylglucosamine-beta-l,6-galactose-beta- 1,4-ZI-Z2-R, wherein Zi is glucose or N-acetylglucosamine , wherein Z2 is absent or is a saccharide, and wherein R is absent or is selected from the list consisting of a peptide, a protein and a lipid; and wherein said cell comprises a beta-1, 6-N-acetylglucosaminyltransferase comprising a domain R(X)io- 2OXIXXXXXXX2XXX3XXXXX4XXXXXX5X6X7X8XXX9(X)2O-6ODE, i.e. SEQ ID NO 01; wherein X is any amino acid; Xi is any amino acid except for F and P; X2 is any amino acid except for A; X3 is any amino acid except for M and E; X4is any amino acid except for D; X5is G or S, X6is S, T, A or N; X7is N, A, L or T; Xg is W, F or Y and X9is any amino acid except for A; and wherein:(i) the first amino acid of SEQ ID NO 01, i.e. R, should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with R199 of a reference beta-1, 6- N-acetylglucosaminyltransferase represented by SEQ ID NO 03;(ii) XsXgXyXg of SEQ ID NO 01 should align with the beta-1, 6-N-acetylglucosaminyltransferase in the same way as it aligns with G234-T235-A236-Y237 of a reference beta-1, 6-N- acetylglucosaminyltransferase represented by SEQ ID NO 03; and(iii) the last two amino acids of SEQ ID NO 01, i.e. DE, should align with the beta-1, 6-N- acetylglucosaminyltransferase in the same way as it aligns with D268-E269 of a reference beta- 1,6-N-acetylglucosaminyltransferase represented by SEQ ID NO 03.

26. A cell according to claim 25, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises the IPR domain IPR003406 as defined by InterPro 102.0.

27. A cell according to claim 25 or 26, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises an amino acid sequence:(i) selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or(ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or(iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , respectively; or(iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , and wherein the length of said functional fragment is at least 80.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237 , respectively.

28. A cell according to any one of claims 25 to 27, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises an amino acid sequence:(i) selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or(ii) having at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237; or(iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, respectively; or(iv) that is a functional fragment of a polypeptide that has at least 90.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, and wherein the length of said functional fragment is at least 90.0% of the length of any one selected from the list consisting of SEQ ID NO 03 to 09 and 12 to 237, respectively.

29. A cell according to claim 25 or 26, wherein said beta-1, 6-N-acetylglucosaminyltransferase comprises an amino acid sequence:(i) selected from the list consisting of SEQ ID NO 238 to 472; or(ii) having at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472; or(iii) that is a functional fragment of any one selected from the list consisting of SEQ ID NO 238 to 472, wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively; or(iv) that is a functional fragment of a polypeptide that has at least 80.0% sequence identity to the full-length amino acid sequence of any one selected from the list consisting of SEQ ID NO 238 to 472, and wherein the length of said functional fragment is at least 70.0% of the length of any one selected from the list consisting of SEQ ID NO 238 to 472, respectively.

30. A cell according to any one of claims 25 to 29, wherein said beta-1, 6-N-acetylglucosaminyltransferasecomprises a domain represented by SEQ. ID NO 02.

31. A cell according to any one of claims 25 to 30, wherein said cell is genetically engineered for the production of said compound.

32. A cell according to any one of claims 25 to 31, wherein said cell is a microorganism.

33. A cell according to any one of claims 25 to 32, wherein said cell is a bacterium.

34. A cell according to any one of claims 25 to 33, wherein said cell is adapted for the production of a functional disulfide bond containing protein.

35. A cell according to claim 34, wherein the expression of a glutathione reductase and / or a thioredoxin reductase is lowered or diminished compared to an unmodified cell.

36. A cell according to any one of claims 25 to 35, wherein said cell further comprises one or more additional glycosyltransferases that are involved in the production of said compound.

37. A cell according to claim 36, wherein said one or more additional glycosyltransferases are selected from the list consisting of a beta-1, 3-N-acetylglucosaminyltransferase, a beta-1, 3- galactosyltransferase, a beta-1, 4-galactosyltransferase, a fucosyltransferase and a sialyltransferase.

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