73 results about "High mannose" patented technology

The invention features a method of producing a high mannose glucocerebrosidase (hmGCB) which includes: providing a cell which is capable of expressing glucocerebrosidase (GCB), and allowing production of GCB having a precursor oligosaccharide under conditions which prevent the removal of at least one mannose residue distal to the pentasaccharide core of the precursor oligosaccharide of GCB, to thereby produce an hmGCB preparation. Preferably, the condition which prevents the removal of at least one mannose residue distal to the pentasaccharide core is inhibition of a class 1 processing mannosidase and/or a class 2 processing mannosidase. The invention also features an hmGCB preparation and methods of using an hmGCB preparation.

This invention is to provide a process for producing a glycoprotein comprising a mammalian type sugar chain, characterized in that the process comprises introducing an α-1,2-mannosidase gene into a methylotrophic yeast having a mutation of a sugar chain biosynthesizing enzyme gene, so that the α-1,2-mannosidase gene is expressed under the control of a potent promoter in the yeast; culturing in a medium the methylotrophic yeast cells with a heterologous gene transferred thereinto; and obtaining the glycoprotein comprising a mammalian type sugar chain from the culture. Using the newly created methylotrophic yeast having a sugar chain mutation, a neutral sugar chain identical with a high mannose type sugar chain produced by mammalian cells such as human cells, or a glycoprotein comprising such a neutral sugar chain, can be produced in a large amount at a high purity. By introducing a mammalian type sugar chain biosynthesizing gene into the above-described mutant, a mammalian type sugar chain, such as a hybrid or complex, or a protein comprising a mammalian type sugar chain can be efficiently produced.

Cell lines having genetically modified glycosylation pathways that allow them to carry out a sequence of enzymatic reactions, which mimic the processing of glycoproteins in humans, have been developed. Recombinant proteins expressed in these engineered hosts yield glycoproteins more similar, if not substantially identical, to their human counterparts. The lower eukaryotes, which ordinarily produce high-mannose containing N-glycans, including unicellular and multicellular fungi are modified to produce N-glycans such as Man₅GlcNAc₂ or other structures along human glycosylation pathways. This is achieved using a combination of engineering and/or selection of strains which: do not express certain enzymes which create the undesirable complex structures characteristic of the fungal glycoproteins, which express exogenous enzymes selected either to have optimal activity under the conditions present in the fungi where activity is desired, or which are targeted to an organelle where optimal activity is achieved, and combinations thereof wherein the genetically engineered eukaryote expresses multiple exogenous enzymes required to produce “human-like” glycoproteins.

The present invention is directed to a composition comprising high mannuronic acid-containing alginate and a polycation having a polydispersity index of less than 1.5. The composition is particularly useful for making biocompatible microcapsules containing living cells for allo- or xeno-transplantation. Such microcapsules have enhanced durability and can maintain their structural and functional integrity over long periods of time compared to prior art alginate microcapsules.

Cell lines having genetically modified glycosylation pathways that allow them to carry out a sequence of enzymatic reactions, which mimic the processing of glycoproteins in humans, have been developed. Recombinant proteins expressed in these engineered hosts yield glycoproteins more similar, if not substantially identical, to their human counterparts. The lower eukaryotes, which ordinarily produce high-mannose containing N-glycans, including unicellular and multicellular fungi are modified to produce O-glycans or other structures along human glycosylation pathways. This is achieved using a combination of engineering and/or selection of strains which: do not express certain enzymes which create the undesirable complex structures characteristic of the fungal glycoproteins, which express exogenous enzymes selected either to have optimal activity under the conditions present in the fungi where activity is desired, or which are targeted to an organelle where optimal activity is achieved, and combinations thereof wherein the genetically engineered eukaryote expresses multiple exogenous enzymes required to produce “human-like” glycoproteins.

The present invention relates to a constructed to oligosaccharide cluster, optionally bonded to an immunogenic protein, that can be administered to a subject to induce an immune response for increasing production of 2G12 and/or used in assays as reactive sites for determining compounds that inactivate and/or bind the high-mannose oligosaccharide cluster. Compositions comprising these clusters, methods of using these clusters and compositions are disclosed.

The invention discloses a method for separating and identifying glycoprotein N-sugar chain structure, and belongs to the technical field of sugar chain detection. According to the method, concanavalin (ConA) is used to separate and enrich high-mannose type and non-high-mannose type N-sugar chains; matrix-assisted laser desorption-ionization time of flight mass spectrometry (MALDI-TOF-MS) is used to detect; a signal-to-noise ratio of 6 is used as a threshold value to carry out data screening; and a Glycoworkbench software is used to analyze. Structure shows that 23 N-sugar chains are identified from a reference group; 29 N-sugar chains are identified from two parts of the high-mannose type and non-high-mannose type; and the identified N-sugar chains are six more than that before ConA enrichment. The method has higher sensitivity and more abundant sugar chain information and has obvious advantage for identification of low kurtosis sugar chains.

The invention relates to a diagnostic marker for systemic lupus erythematosus, and in particular discloses application of a reagent for specific detection of high mannose type N-linked carbohydrate chain level in a serum antibody to preparation of a diagnostic tool for diagnosis and/or prognosis assessment of systemic lupus erythematosus. The increase of the high mannose type N-linked carbohydrate chain level in the serum antibody is closely related to the occurrence of systemic lupus erythematosus. Therefore, the diagnostic marker can be used for early diagnosis and/or prognostic assessment of systemic lupus erythematosus, and further can be used for guiding treatment of systemic lupus erythematosus.

Recombinant human alpha glucosidase (rhGAA) composition derived from CHO cells that contains a more optimized glycan composition consisting of a higher amount of rhGAA containing N-glycans carrying mannose-6-phosphate (M6P) or bis-M6P than conventional rhGAAs, along with low amount of non-phosphorylated high mannose glycans, and low amount of terminal galactose on complex oligosaccharides. Compositions containing the rhGAA, and methods of use are described.

The present invention describes a process to improve the activity as wine stabiliser of a mannoprotein, comprising treating a mannoprotein with a basic solution at a pH of at least 9. The mannoprotein obtainable by this process is more effective in stabilising wine against tartrate precipitation or protein haze formation when compared with the mannoprotein prior to the treatment with basic solution.

The invention discloses low-saccharification mutant interferon lambda1 as well as expression and purification methods thereof. The low-saccharification mutant interferon lambda1 is protein obtained after replacing Asn in the N46 bit in the IFN-lambda1 mature peptide sequence into Gln. The blockage on the high-mannose modification process of the N-glycosylation site of the IFN-lambda1 by the Pichia pastoris is realized so that the IFN-lambda1-Nm genes are correctly expressed in the Pichia pastoris in a high-efficiency secretory way, the uniformity of the expressed recombination IFN-lambda1-Nm protein is obviously improved, the expression level is higher than 65mg/L, the purity of the expressed recombination protein after two-step column chromatography is higher than 98 percent, and the low-saccharification modified recombination IFN-lambda1-Nm protein has the same biological activity as the original Pichia pastoris expressed wild IFN-lambda1 and simultaneously has better safety. The invention provides an effective method for efficient low-cost mass production of low-saccharification mutant interferon lambda1 with biological activity and good uniformity, higher practical application values are realized, and the application prospects are wide.