Anti-globo h antibodies

Abstract

The present invention relates to antibodies binding to globo-series glycan comprising a terminal α-L-Fuc-(1→2)-β-D-Gal-(1– moiety as well as antibody drug conjugates, bispecific antibodies, particularly bispecific T-cell engaging antibodies, and T cell chimeric antigen receptors comprising said anti-Globo H antibodies. Thus, the present invention provides antibodies that can be used for targeting, treating and / or diagnosing several types of cancers associated with cells over-expressing said Globo H. The present invention also relates to recombinant nucleic acid sequences encoding said antibodies, and expression vectors and host cells comprising the same.

Description

[0001] Anti-Globo H antibodies Field of invention The present invention relates to antibodies and antigen-binding fragments thereof specifically binding to a globo-series glycan having a terminal α-L-Fuc-(1→2)-β-D-Gal-(1– moiety of the globo-series glycan, such as Globo H, as well as antibody drug conjugates, bispecific antibodies, particularly bispecific T-cell engaging antibodies, and T-cell chimeric antigen receptors comprising said anti-Globo H antibodies. Thus, the present invention provides antibodies that can be used for targeting, treating and / or diagnosing several types of cancers associated with cells over-expressing said Globo H. The present invention also relates to recombinant nucleic acid sequences encoding said antibodies, and expression vectors, and host cells comprising the same. Background of the invention Globo-series glycans comprise a group of neutral glycosphingolipids in which a ceramide is linked to a glycan with a root structure of GalNAcβ3Galα4Galβ4Glc. Typically, these glycans are retained on the plasma membrane and cluster into lipid rafts. The endogenous function of this glycan family is largely unknown. Their expression does, however, occur during early stages of development and is thought to mediate cell contact and adhesion. Importantly, changes in these glycans are observed throughout differentiation and during tumorigenesis. Two notable hexasaccharide members of this family are stage-specific embryonic antigen- 4 (SSEA-4) and Globo H (Fig. 1). These glycans share a common precursor, SSEA-3 (Galβ3GalNAcβ3Galα4Galβ4Glc), but vary in the terminal monosaccharide: β3-linked N- acetylneuraminic acid for SSEA-4 and α2-linkedL-fucose for Globo H. Globo H, also termed SSEA-3b, is a hexasaccharide with chemical formula Fucα1→2Galβ1→3GalNAcβ1→3Galα1→4Galβ1→4Glcβ1→O-Cer. Globo H expression has been found on several epithelial cancers such as endometrial colon, ovarian, gastric, pancreatic, lung, prostate, and breast cancers; in normal tissues it is moderately present in breast, colon, esophagus, small intestine, prostate, rectum, testis, and uterine cervix, but only on apical epithelial cells at lumen borders. Wang et al. (PNAS, 2008) found by glycan array that both normal donors and breast cancer patients expressed high levels of antibodies to SSEA-3, but breast cancer patients expressed much higher levels of antibodies to Globo H than normal donors. Because the sites where either SSEA-3 or Globo H could be found in normal tissues are in areas that are considered generally inaccessible to immune cells, both SSEA-3 and Globo H make attractive targets for a cancer vaccine or immunotherapy. However, most carbohydrate antigens are often tolerated by the immune system, and consequently, the immunogenicity induced by them is limited. Further, the production of antibody against a specific immunogen typically involves cooperative interactions between two types of lymphocytes, i.e., B-cells and helper T-cells. Globo H alone cannot activate helper T-cells, which also attributes to the poor immunogenicity of Globo H. Accordingly, immunization with Globo H alone often results in low titers of immunoglobulin M (IgM) and failure to class switch to immunoglobulin G (IgG), as well as ineffective antibody affinity maturation. Recently, it has been demonstrated that with addition of suitable adjuvants, antibodies against Globo H can be induced, including class switching from IgM to IgG. Thus, Globo H is a promising therapeutic target for cancer vaccination. This approach has been tested in clinical trials at various stages against different cancers, including breast cancer, ovarian cancer, prostate cancer, and lung cancer. While antibodies against Globo H have been shown to be promising in cancer diagnosis and therapy (WO 2015 / 143123 A2) better anti-Globo H antibodies are still needed. For the intended uses, antibodies are needed. The patent application WO 2015 / 143123 A2 discloses anti-Globo H antibodies and pharmaceutical compositions comprising these antibodies to prevent or treat Globo H positive cancers. However these antibodies have CDR sequences that can confer chemical instability, which makes them undesirable for further production scale-up and clinical study. The international patent application WO 2018 / 054353 A1 discloses therapeutic human antibodies binding Globo H and having CDR sequences engineered for increased stability against undesirable modifications and large aggregate formation that can occur under high expression manufacturing conditions. The international patent application WO 2018 / 218068 A1 discloses another therapeutic humanized monoclonal antibody binding Globo H. The European patent application EP 3799881 A1 discloses single domain antibodies (sdAbs or VHH) specifically binding a globo-series glycosphingolipid, such as Globo H or a fragment thereof. The patent US 11,000,601 B2 discloses a therapeutic humanized antibody used as an ADC. Thus, it is the objective of the present invention to provide antibodies specifically binding Globo H having a substantially improved affinity, low cross-reactivity, and which are compatible with therapeutic applications. This objective is solved by the teaching of the independent claims. Further advantageous features, aspects, and details of the invention are evident from the dependent claims, the description, the figures, and the examples of the present application. Brief description of the invention The application is directed to an antibody or antigen-binding fragment thereof binding a globo- series glycan. In particular said antibody or binding fragment thereof binds to a terminal α-L- Fuc-(1→2)-β-D-Gal-(1– moiety of the globo-series glycan, as comprised for example in Globo H. For example the antibody or antigen-binding fragment thereof comprises: (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.1, a HCDR2 as set forth in SEQ ID No.2, and a HCDR3 as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.4, a LCDR2 region as set forth in SEQ ID No.5, and a LCDR3 region as set forth in SEQ ID No.6. In one embodiment the antibody or antigen-binding fragment thereof comprises: (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.7, a HCDR2 as set forth in SEQ ID No.8, and a HCDR3 as set forth in SEQ ID No.9, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.10, a LCDR2 region as set forth in SEQ ID No.11, and a LCDR3 region as set forth in SEQ ID No. 12. In one embodiment the antibody or antigen-binding fragment thereof comprises: (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.53, a HCDR2 as set forth in SEQ ID No.60, and a HCDR3 as set forth in SEQ ID No.68, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.56, a LCDR2 region as set forth in SEQ ID No.57, and a LCDR3 region as set forth in SEQ ID No. 58. Surprisingly, by immunizing of chicken with a Globo H conjugate, isolation and sequencing of the antibodies formed, and subsequent expression of the antibodies, the inventors identified a new antibody specifically binding Globo H, which targets a completely new binding region in the antigen sequence overcoming many drawbacks of existing anti Globo H antibodies. The inventors created various variants showing the above-mentioned advantages. Accordingly, one embodiment refers to antibodies comprising (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.1, a HCDR2 as set forth in SEQ ID No.2, and a HCDR3 as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.4, a LCDR2 region as set forth in SEQ ID No.5, and a LCDR3 region as set forth in SEQ ID No.6. More specific embodiments refer to antibodies comprising (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.7, a HCDR2 as set forth in SEQ ID No.8, and a HCDR3 as set forth in SEQ ID No.9, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.10, a LCDR2 region as set forth in SEQ ID No.11, and a LCDR3 region as set forth in SEQ ID No. 12. In particular the antibodies exhibit improved properties over the known monoclonal antibody VK9 and OBI-888 (Figure 6). Particularly, the inventive antibody possesses a higher affinity (Figure 7) while maintaining specificity towards Globo H (see Figure 5), lower cross-reactivity, and a faster internalization in comparison to VK9 (see Figure 8). Thus, surprisingly the inventors found high affinity antibodies targeting Globo H while substantially not binding to / or binding with a much lesser extent to similar molecules such as Gb5, SSEA3, SSEA4 and SSEA5. In particular, the antibodies of the invention bind to Globo H with high affinity while having low cross-reactivity to the most critical (since most similar) molecules Gb5 and SSEA5. Thus, in some embodiments the antibody or antigen-binding fragment thereof has a 20-fold higher affinity to GloboH compared to SEEA-5 and / or a 10-fold higher affinity to GloboH compared to Gb5. The antibody binds to a terminal α-L-Fuc-(1→2)-β-D-Gal-(1– moiety of the globo-series glycan.In one embodiment the antibody binds to Fucα1→2Galβ1→3GalNAcβ1→3Galα1→4Galβ1→4Glcβ1→O-Cer. This structure is specific to Globo H and not comprised in similar molecules, such as Gb5 or SSEA5. In one preferred embodiment the antibody comprises (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.53, a HCDR2 as set forth in SEQ ID No.60, and a HCDR3 as set forth in SEQ ID No.68, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.56, a LCDR2 region as set forth in SEQ ID No.57, and a LCDR3 region as set forth in SEQ ID No. 58. The present invention is also directed to an antibody specifically binding Globo H as described herein, wherein the antibody is conjugated to a toxophore, a toxic component or a radiating component. In some embodiments, the antibody specifically binding Globo H is conjugated to a toxophore, a toxic component or radiating component is selected from: auristatin E, monomethyl auristatin E, monomethyl auristatin F, dolastatin, maytansine, ansamitocin, emtansine, soravtansine, duocarmycin A, duocarmycin BL duocarmycin B2, duocarmycin CI, duocarmycin C2, duocarmycin D, duocarmycin SA, duocarmycin MA, CC-1065, amiodarone, clarithromycin, ciclosporin, colchicine, diltiazem, erythromycin, felodipine, ketoconazole, lansoprazole, omeprazole, nifedipine, paroxetine, reserpine, saquinavir, sertraline, quinidine, tamoxifen, verapamil, duloxetine, elacridar CP 100356, zosuquidar, tariquidar, deruxtecan, exatecan, topotecan, belotecan, gimatecan, Dxd, lurtotecan, Irinotecan, Zirconium, Radium, Actinium, Thorium, and Lutetium. In some embodiments, the antibody specifically binding Globo H is conjugated to the toxic component monomethyl auristatin E (MMAE), deruxtecan, or exatecan. The present invention is also directed to an antibody specifically binding Globo H as described herein wherein the antibody is a T-cell-engaging bispecific antibody simultaneously specifically binding Globo H and CD3. The present invention is further directed to chimeric antigen receptor (CAR) specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, conjugated to a transmembrane region and an intracellular T-cell receptor signaling domain. The CAR as disclosed herein can be used to generate CAR T cells specifically recognizing Globo H. Said CAR T cells can thus be used in the therapy of a cancer, wherein the cancer cells of said cancer express on their surface Globo H. In some embodiments, the antibody specifically binding Globo H as described herein, is conjugated to an extracellular hinge region, at least one transmembrane domain, at least one costimulatory domain, and at least one intracellular activation domain, thereby forming a T-cell chimeric antigen receptor (CAR). The present invention also provides recombinant nucleic acid molecules encoding the antibodies of the invention, and vectors that comprise said recombinant nucleic acid molecules. Host cells comprising the recombinant nucleic acid molecules or vectors of the invention are also provided herein. Moreover, the invention also relates to pharmaceutical compositions comprising a therapeutically effective amount of the inventive antibody specifically binding Globo H, together with at least one pharmaceutically acceptable vehicle, excipient and / or diluent. The invention also provides for the use of an antibody of the invention or of the pharmaceutical composition according to the invention in treatment and / or diagnosis of a cancer, wherein the cancer cells of said cancer express on their surface Globo. In other words, the invention provides the use of an antibody of the invention or of a pharmaceutical composition according to the invention in treatment and / or diagnosis of a cancer, wherein the cancer is characterised by cells expressing on their surface Globo H. The invention also provides for the use of an antibody of the invention or of the pharmaceutical composition according to the invention in treatment and / or diagnosis of a cancer, wherein the cancer cells of said cancer express on their surface Globo H, and wherein said cancer is selected from adenocarcinoma, choroidal melanoma, acute leukemia, acoustic neurinoma, ampullary carcinoma, anal carcinoma, astrocytoma, basal cell carcinoma, pancreatic cancer, desmoid tumor, bladder cancer, bronchial carcinoma, breast cancer, Burkitt's lymphoma, corpus cancer, CUP-syndrome (carcinoma of unknown primary), colorectal cancer, small intestine cancer, small intestinal tumors, ovarian cancer, endometrial carcinoma, ependymoma, epithelial cancer types, Ewing's tumors, gastrointestinal tumors, gastric cancer, gallbladder cancer, gall bladder carcinomas, uterine cancer, cervical cancer, cervix, glioblastomas, gynecologic tumors, ear, nose and throat tumors, hematologic neoplasias, hairy cell leukemia, urethral cancer, skin cancer, skin testis cancer, brain tumors (gliomas), brain metastases, testicle cancer, hypophysis tumor, carcinoids, Kaposi's sarcoma, laryngeal cancer, germ cell tumor, bone cancer, colorectal carcinoma, head and neck tumors (tumors of the ear, nose and throat area), colon carcinoma, craniopharyngiomas, oral cancer (cancer in the mouth area and on lips), cancer of the central nervous system, liver cancer, liver metastases, leukemia, eyelid tumor, lung cancer, lymph node cancer (Hodgkin's / Non- Hodgkin's), lymphomas, stomach cancer, malignant melanoma, malignant neoplasia, malignant tumors gastrointestinal tract, breast carcinoma, rectal cancer, medulloblastomas, melanoma, meningiomas, Hodgkin's disease, mycosis fungoides, nasal cancer, neurinoma, neuroblastoma, kidney cancer, renal cell carcinomas, non-Hodgkin's lymphomas, oligodendroglioma, esophageal carcinoma, osteolytic carcinomas and osteoplastic carcinomas, osteosarcomas, ovarial carcinoma, pancreatic carcinoma, penile cancer, plasmocytoma, prostate cancer, pharyngeal cancer, rectal carcinoma, retinoblastoma, vaginal cancer, thyroid carcinoma, Schneeberger disease, esophageal cancer, spinalioms, T-cell lymphoma (mycosis fungoides), thymoma, tube carcinoma, eye tumors, urethral cancer, urologic tumors, urothelial carcinoma, vulva cancer, wart appearance, soft tissue tumors, soft tissue sarcoma, Wilm's tumor, cervical carcinoma and tongue cancer. In some embodiments, the cancer is selected from brain cancer, liver cancer, bile duct cancer, kidney cancer, breast cancer, prostate cancer, lung cancer, small cell lung cancer, ovarian cancer, cervix cancer, esophagus cancer, stomach cancer, pancreatic cancer and colorectal cancer. The invention also provides a diagnostic kit comprising an antibody as described herein for screening for a cancer characterised by cells expressing on their surface Globo H. Detailed description of the invention Tumor associated antigens (TACAs) and types Cancer cells can be distinguished from normal cells for displaying aberrant levels and types of carbohydrate structures on their surfaces. These carbohydrate structures are known as tumor-associated carbohydrate antigens (TACAs). TACAs were considered as promising targets for the design of anticancer vaccines. Unfortunately, carbohydrates alone can only evoke poor immunogenicity because they are unable to induce T-cell-dependent immune responses, which is critical for cancer therapy. Glycosphingolipids (GSLs) represent a group of complex lipids composed of a glycan structure attached to a lipid tail that contains the sphingolipid ceramide. The basic structure for a glycosphingolipid is a monosaccharide, usually glucose or galactose, attached directly to a ceramide molecule and resulting in, respectively, glucosylceramide (glucocerebroside; GlcCer) or galactosylceramide (galactocerebroside; GalCer). GSLs are ubiquitous in cell membranes, where they are known to participate in cellular processes such as signaling, adhesion, and cell differentiation, among other functions. Certain glycosphingolipids highly expressed in tumor cells or tissues have been defined by specific monoclonal antibodies and thereby identified as tumor-associated carbohydrate antigens (TACAs) resulting from aberrant GSL synthesis in tumors. Tumor cells express aberrant glycosylation in GSLs, displaying either incomplete synthesis leading to an accumulation of precursors, or further addition of glycan residues to form new structures. While globotriosylceramide (Gb3Cer) and globoside (Gb4Cer) constitute the basis of P- blood group system, galactosyl globoside (Gb5Cer) and sialyl galactosyl globoside (sialyl Gb5Cer), also known as stage-specific embryonic antigen-3 (SSEA-3) and SSEA-4, respectively, are widely used as cell-surface markers to define human embryonic stem cells. Globo-series GSLs have also been observed in tumors as Globo H (fucosyl Gb5Cer) is overexpressed in many epithelial cancers, such as endometrial, colon, ovarian, gastric, pancreatic, lung, prostate, and breast cancers. The term “globo-series glycans” refers to a group of neutral glycosphingolipids in which a ceramide is linked to a glycan with a root structure of GalNAcβ3Galα4Galβ4Glc. Typically, these glycans are retained on the plasma membrane and cluster into lipid rafts. Exemplary globo-series glycans are stage-specific embryonic antigen-4 (SSEA-4) and Globo H. “Globo H” as used herein, refers to a hexasaccharide of formula, Fucα1→2Galβ1→3GalNAcβ1→3Galα1→4Galβ1→4Glcβ1→O-cer, having the structure: “Globo H-positive cancer” refers to a cancer comprising cancer cells expressing Globo H on their surface. "Globo H substructure” refers to any sequence of monosaccharide units (with minimum two) that appear in the same sequence of that from GloboH and which contain one or both of the first two units (i.e., Fucα1→2Gal). In this case, the kind of bond between the monosaccharides must be the same of that one in Globo H. "Globo H-related structure” refers to any sequence of monosaccharide units (with minimum two) that appear in the same sequence of that from GloboH and which contain one or both of the first two units (i.e., Fucα1→2Gal). In this case, the kind of bond between the monosaccharides can be different from that one present in Globo H. Besides, the monosacharrides can also be different, but not always, in case they differ only on the position of the OH groups connected to the carbon chain. “Antibodies” (Abs) and “immunoglobulins” (Igs) are glycoproteins having the same structural characteristics. While antibodies exhibit binding specificity to a specific antigen, immunoglobulins include both antibodies and other antibody-like molecules which generally lack antigen specificity. The terms “antibody” and “immunoglobulin” are used interchangeably in the broadest sense and include monoclonal antibodies (e.g., full length or intact monoclonal antibodies), polyclonal antibodies, human antibodies, multispecific (or heteroconjugate) antibodies (e.g. bispecific antibodies), monovalent antibodies, multivalent antibodies, antigen-binding antibody fragments (e.g., Fab′, F(ab′)2, Fab, Fv, rIgG, scFv fragments, sdAbs, VHH), antibody fusions, and synthetic antibodies (or antibody mimetics). An antibody can be chimeric, human, humanized, engineered, and / or affinity matured. As used herein, the term “antigen” is defined as any substance capable of eliciting an immune response. As used herein, the term “immunogenicity” refers to the ability of an immunogen, antigen, or vaccine to stimulate an immune response. As used herein, the term “epitope” is defined as the parts of an antigen molecule which contact the antigen binding site of an antibody or of a T cell receptor. As used herein, the term "specific binding" or “specifically binding” or "binds specifically" refers to the interaction between binding pairs (e.g., an antibody and an antigen). In various instances, specifically binding can be embodied by an affinity constant of about 10-6moles / liter, about 10-7moles / liter, or about 10-8moles / liter, or less. “Binding affinity” generally refers to the strength of the total sum of noncovalent interactions between a single binding site of a molecule (e.g., an antibody) and its binding partner (e.g., an antigen). Unless indicated otherwise, as used herein, “binding affinity” refers to intrinsic binding affinity which reflects a 1:1 interaction between members of a binding pair (e.g., antibody and antigen). The affinity of a molecule X for its partner Y can generally be represented by the dissociation constant (KD). Low-affinity antibodies generally bind antigen slowly and tend to dissociate readily, whereas high-affinity antibodies generally bind antigen faster and tend to remain bound longer. A variety of methods of measuring binding affinity are known in the art, any of which can be used for purposes of the present invention. For example, binding affinities and / or rate constants can be determined using techniques well known in the art or described herein, isothermal titration calorimetry (ITC), Biacore (SPR), biolayer interferometry orfluorescent polarization. Maximum mean fluorescent intensity (maxMFI) measured in flow cytometry (FC) can also be used to quantify the binding profile of antibodies. When comparing two antibodies binding to the same target, a higher maxMFI is indicative of a higher affinity and / or of a lower off rate. Specific illustrative embodiments are described in the following. The term “VK9” or “VK9 antibody” used herein relates to a commercially available monoclonal antibody binding to GloboH. The VK9 antibody was first described by Kudryashov et al.1998 (Glycoconj J.1998 Mar;15(3):243-9, PMID: 9579801). This antibody can be obtained e.g. from ThermoFischer Scientific with the catalog number 14-9700-82. The term “OBI-888” or “OBI-888 antibody” used herein relates to a commercially available humanized monoclonal antibody binding to GloboH. The OBI-888 antibody is described in the patent publications WO 2015 / 157629A2. Exemplarily, the OBI-888 antibody may comprise the CDRs of the variable heavy chain region of an antibody produced by hybridoma 2C2 (SEQ ID NOs: 5, 6 and 7); the CDRs of the variable light chain region of an antibody produced by hybridoma 2C2 (SEQ ID NOs: 8, 9 and 10) as defined in WO 2015 / 157629A2. The term “R783” refers to an antibody binding to GloboH described in the international patent application WO 2022 / 173840A1. Specifically, the R783 antibody comprises the heavy chain variable region set forth in SEQ ID: 19 and light chain variable region set forth in in SEQ ID NO: 20 of WO 2022 / 173840A1. “Functional antigen binding site” of an antibody is one which is capable of binding a target antigen. The antigen binding affinity of the antigen binding site is not necessarily as strong as the parent antibody from which the antigen binding site is derived, but the ability to bind antigen must be measurable using any one of a variety of methods known for evaluating antibody binding to an antigen. The term “vector” as used herein, is intended to refer to a nucleic acid molecule capable of transporting another nucleic acid to which it has been linked. One type of vector is a “plasmid”, which refers to a circular double stranded DNA loop into which additional DNA segments may be ligated. Another type of vector is a phage vector. Another type of vector is a viral vector, wherein additional DNA segments may be ligated into the viral genome. Certain vectors are capable of autonomous replication in a host cell into which they are introduced. Other vectors (e.g., non-episomal mammalian vectors) can be integrated into the genome of a host cell upon introduction into the host cell, and thereby are replicated along with the host genome. Moreover, certain vectors are capable of directing the expression of genes to which they are operatively linked. Such vectors are referred to herein as “recombinant expression vectors” (or simply, "expression vectors" or “recombinant vectors”). In general, expression vectors of utility in recombinant DNA techniques are often in the form of plasmids. In the present specification, “plasmid” and “vector” may be used interchangeably as the plasmid is the most commonly used form of vector. “Recombinant polynucleotide” or “recombinant nucleic acid molecule” as used interchangeably herein, refer to polymers of nucleotides of any length, and include DNA and RNA. The nucleotides can be deoxyribonucleotides, ribonucleotides, modified nucleotides or bases, and / or their analogs, or any substrate that can be incorporated into a polymer by DNA or RNA polymerase, or by a synthetic reaction. A polynucleotide may comprise modified nucleotides, such as methylated nucleotides and their analogs. If present, modification to the nucleotide structure may be imparted before or after assembly of the polymer. The sequence of nucleotides may be interrupted by non-nucleotide components. A polynucleotide may be further modified after synthesis, such as by conjugation with a label. Other types of modifications include, for example, “caps”, substitution of one or more of the naturally occurring nucleotides with an analog, internucleotide modifications such as, for example, those with uncharged linkages (e.g., methyl phosphonates, phosphotriesters, phosphoamidates, carbamates, etc.) and with charged linkages (e.g., phosphorothioates, phosphorodithioates, etc.), those containing pendant moieties, such as, for example, proteins (e.g., nucleases, toxins, antibodies, signal peptides, ply-L-lysine, etc.), those with intercalators (e.g., acridine, psoralen, etc.), those containing chelators (e.g., metals, radioactive metals, boron, oxidative metals, etc.), those containing alkylators, those with modified linkages (e.g., alpha anomeric nucleic acids, etc.), as well as unmodified forms of the polynucleotides(s). Further, any of the hydroxyl groups ordinarily present in the sugars may be replaced, for example, by phosphonate groups, phosphate groups, protected by standard protecting groups, or activated to prepare additional linkages to additional nucleotides, or may be conjugated to solid or semi-solid supports. The 5′ and 3′ terminal OH can be phosphorylated or substituted with amines or organic capping group moieties of from 1 to 20 carbon atoms. Other hydroxyls may also be derivatized to standard protecting groups. “Oligonucleotide” as used herein, generally refers to short, generally single-stranded, generally synthetic polynucleotides that are generally, but not necessarily, less than about 200 nucleotides in length. The terms “oligonucleotide” and “polynucleotide” are not mutually exclusive. The description above for polynucleotides is equally and fully applicable to oligonucleotides. “A globo-series glycan binding antibody” or “antibody that binds a globo-series glycan” or “antibody or fragment thereof biding a globo-series glycan” refers to a antibody that binds a globo-series glycan comprising a terminal α-L-Fuc-(1→2)-β-D-Gal-(1– moiety with sufficient affinity such that the antibody is useful as a diagnostic and / or therapeutic agent by binding the target glycan. A "Globo H binding antibody” or “antibody that binds Globo H” refers to a monoclonal antibody that binds Globo H with sufficient affinity such that the monoclonal antibody is useful as a diagnostic and / or therapeutic agent by binding GloboH. Typically, the antibody is a monoclonal antibody. “Full-length antibody”, “intact antibody”, or “whole antibody” are used herein interchangeably to refer to an antibody having a structure substantially similar to a native antibody structure. “Antibody fragment”, also termed “binding fragment” or “antigen-binding fragment” refers to a portion of a full-length antibody which is capable of binding the same antigen as the full- length antibody. Examples of antibody fragments include, but are not limited to, Fv, Fab, Fab', F(ab')2；diabodies；linear antibodies；single-chain antibody molecules (e.g.，scFv); single domain antibodies; multispecific antibodies formed from antibody fragments. Typically the antibody fragment comprises the 6 CDRs. The “variable region” or “variable domain” of an antibody refers to the amino-terminal domains of heavy or light chain of the antibody. The variable domains of the heavy chain and light chain (VH or heavy chain variable region VHand VL or light chain variable region VL, respectively) of a native antibody generally have similar structures. A single VH or VL domain may be sufficient to confer antigen-binding specificity. In particular, “variable region” or “variable domain” of a single domain antibody disclosed herein refers to the amino-terminal domains of the heavy chain, or light chain. The term “variable” refers to the fact that certain portions of the variable domains differ extensively in sequence among antibodies and are used in the binding and specificity of each particular antibody for its particular antigen. However, the variability is concentrated in three segments called complementarity-determining regions (CDRs) or hypervariable regions (HVR) both in the light-chain and the heavy-chain variable domains. The more highly conserved portions of variable domains are called framework regions (FR). The variable domains of native heavy and light chains each comprise four FR regions, largely adopting a beta-sheet configuration, connected by three CDRs, which form loops connecting, and in some cases forming part of, the beta-sheet structure. In a three-dimensional structure, the CDRs in each chain are held together in close proximity by the FR regions and, with the CDRs from the other chain, contribute to the formation of the antigen-binding site of antibodies (Kabat et al., Sequences of Proteins of Immunological Interest, Fifth Edition, National Institute of Health, Bethesda, Md. (1991)). The constant domains are usually not involved directly in binding of an antibody to an antigen, but exhibit various effector functions, such as participation of the antibody in antibody-dependent cellular toxicity. “Hypervariable region” or “HVR” as used herein, refers to each of the regions of an antibody variable domain which are hypervariable in sequence and / or form structurally defined loops. Generally, native antibodies comprise four chains with six HVRs； three in the heavy chain variable domains, VH (H1, H2, H3), and three in the light chain variable domains, VL (L1, L2, L3). Single domain antibodies only comprise three HVRs in the heavy chain variable domain, or in the light chain in rare cases. The HVRs generally comprise amino acid residues from the hypervariable loops and / or from the “complementarity determining regions” (CDRs). Unless otherwise indicated, HVR residues and other residues in the variable domain (e.g., FR residues) are numbered herein according to Kabat et al.， 1991. “Complementarity determining region” or “CDR” as used herein, refers to the regions within the hypervariable regions of the variable domain which have the highest sequence variability and / or are involved in antigen recognition. Generally, native antibodies comprise four chains with six CDRs；three in the heavy chain variable domains, VH (H1, H2, H3), also termed HCDR1, HCDR2, HCDR3, or VH-CDR1, VH-CDR2, VH-CDR3 and three in the light chain variable domains, VL (L1, L2, L3), also termed LCDR1, LCDR2, LCDR3, or VL- CDR1, VL-CDR2, VL-CDR3. The CDRs as set out in the SEQ ID Nos. refer to CDRs according to Kabat. The disclosure also encompasses the corresponding embodiments with CDRs according to IMGT nomenclature. “Native antibody” refers to a naturally occurring immunoglobulin molecule. For example, native IgG antibodies are heterotetrameric glycoproteins of about 150,000 Daltons, composed of two identical light chains and two identical heavy chains that are disulfide- bonded. From N- to C-terminus, each heavy chain has a variable region (VH), also called a variable heavy domain or a heavy chain variable domain, followed by three constant domains (CH1, CH2, and CH3). Similarly, from N- to C-terminus, each light chain has a variable region (VL), also called a variable light domain or a light chain variable domain, followed by a constant light (CL) domain. The light chain of an antibody may be assigned to one of two types, called kappa (κ) and lambda (λ), based on the amino acid sequence of its constant domain. “Monoclonal antibody” as used herein refers to an antibody obtained from a substantially homogeneous population of antibodies, i.e.， the individual antibodies comprising the population are identical and / or bind the same epitope, except for possible variant antibodies (e.g.， variant antibodies contain mutations that occur naturally or arise during production of a monoclonal antibody, and generally are present in minor amounts). In contrast to polyclonal antibody preparations, which typically include different antibodies directed against different determinants (epitopes), each monoclonal antibody of a monoclonal antibody preparation is directed against a single determinant on an antigen. Thus, the term “monoclonal” indicates the character of the antibody as being obtained from a substantially homogeneous population of antibodies, and is not to be construed as requiring production of the antibody by any particular method. “Engineered antibody” or “improved antibody” refers to a monoclonal antibody that has its amino acid sequence modified actively, non-naturally in order to improve desired biochemical characteristics. Such modifications may be made in the CDRs, FRs, or constant regions and, regardless of the location or nature of such amino acid change, may impact the affinity, specificity, stability, or other properties of the monoclonal antibody. “Chimeric antibody” refers to an antibody in which a portion of the heavy and / or light chain is derived from a particular source or species, while the remainder of the heavy and / or light chain is derived from a different source or species. “Humanized antibody” refers to a chimeric antibody comprising amino acid sequences from non-human HVRs and amino acid sequences from human FRs. In certain embodiments, a humanized antibody will comprise substantially a single domain antibody, in which all or substantially all of the CDRs correspond to those of a non-human antibody, and all or substantially all of the FRs correspond to those of a human antibody. A humanized antibody optionally may comprise at least a portion of an antibody constant region derived from a human antibody. A “humanized form” of an antibody, e.g., a non-human antibody, refers to an antibody that has undergone humanization. “Human antibody” refers to an antibody which possesses an amino acid sequence corresponding to that of an antibody produced by a human or a human cell or derived from a non-human source that utilizes human antibody repertoires or other human antibody- encoding sequences. This definition of a human antibody specifically excludes a humanized antibody comprising non-human antigen-binding residues. “Human consensus framework” is a framework which represents the most commonly occurring amino acid residues in a selection of human immunoglobulin VL or VH framework sequences. Generally, the selection of human immunoglobulin VL or VH sequences is from a subgroup of variable domain sequences. Generally, the subgroup of sequences is a subgroup as in Kabat et al.1991. “Multivalent antibody” as used herein, is an antibody comprising three or more antigen binding sites. The multivalent antibody is preferably engineered to have the three or more antigen binding sites and is generally not a native sequence IgM or IgA antibody. “Bispecific antibody” is an antibody having two different binding sites, each site with a different binding specificity. A bispecific antibody can be a full-length antibody or an antibody fragment, and the different binding sites may bind each to a different antigen or the different binding sites may bind to two different epitopes of the same antigen. “Multispecific antibody” is an antibody having at least two different binding sites, each site with a different binding specificity. A multispecific antibody can be a full-length antibody or an antibody fragment, and the different binding sites may bind each to a different antigen or the different binding sites may bind to two different epitopes of the same antigen. “Fc region” or "Fc antibody fragment" refers to a dimer complex comprising the C-terminal polypeptide sequences of an immunoglobulin heavy chain, wherein a C-terminal polypeptide sequence is that which is obtainable by papain digestion of an intact antibody. The Fc region may comprise native, or variant, or engineered Fc sequences. “Fab fragment" refers to an antibody fragment that contains a variable and constant domain of the light chain and a variable domain and the first constant domain (CH1) of the heavy chain. Papain digestion of antibodies produces two identical “Fab” fragments, each with a single antigen-binding site, and a residual “Fc” fragment, whose name reflects its ability to crystallize readily. Pepsin treatment yields an F(ab′)2 fragment that has two antigen- combining sites and is still capable of cross-linking antigen. Fab′ fragments differ from Fab fragments by the addition of a few residues at the carboxy terminus of the heavy chain CH1 domain including one or more cysteines from the antibody hinge region. F(ab′)2 antibody fragments originally were produced as pairs of Fab′ fragments which have hinge cysteines between them. Other chemical couplings of antibody fragments also are known in the art. “Fv fragment” refers to an antibody fragment which contains a complete antigen recognition and binding site. This region consists of a dimer of one heavy and one light chain variable domain in tight association, which can be covalent in nature, for example in scFv. It is in this configuration that the three HVRs of each variable domain interact to define an antigen binding site on the surface of the VH-VL dimer. Collectively, the six HVRs or a subset thereof confer antigen binding specificity to the antibody. However, even a single variable domain (or half of an Fv comprising only three HVRs specific for an antigen) has the ability to recognize and bind antigen, although usually at a lower affinity than the entire binding site. “Single-chain Fv” or “scFv” refers to antibody fragments comprising the VH and VL domains of an antibody, wherein these domains are present in a single polypeptide chain. Generally, an Fv polypeptide further comprises a polypeptide linker between the VH and VL domains which enables the scFv to form the desired antigen binding structure. “Naked antibody” refers to an antibody that is not conjugated to a heterologous moiety (e.g., a cytotoxic moiety) or radiolabel. An “isolated” antibody is one which has been identified and separated and / or recovered from a component of its natural environment. Contaminant components of its natural environment are materials which would interfere with research, diagnostic or therapeutic uses for the antibody, and may include enzymes, hormones, and other proteinaceous or non-proteinaceous solutes. Ordinarily, isolated antibody will be prepared by at least one purification step. Sequence similarity related disclosure The term “substantially similar,” “substantially the same”, “equivalent”, or “substantially equivalent”,” as used herein, refer to a sufficiently high degree of similarity between two numeric values (for example, one associated with a test antibody and the other associated with a reference antibody), such that one of skill in the art would consider the difference between the two values to be of little or no biological and / or statistical significance within the context of the biological characteristic measured by said values (e.g. Kd values). The difference between said two values is, for example, less than about 50%, less than about 40%, less than about 30%, less than about 20%, and / or less than about 10% as a function of the value for the reference / comparator molecule. “Substantially different” as used herein, refers to a sufficiently high degree of difference between two numeric values (generally one associated with a molecule and the other associated with a reference molecule) such that one of skill in the art would consider the difference between the two values to be of statistical significance within the context of the biological characteristic measured by said values (e.g. Kd values). The difference between said two values is, for example, greater than about 10%, greater than about 20%, greater than about 30%, greater than about 40%, and / or greater than about 50% as a function of the value for the reference / comparator molecule. All variants tested (see Table 6) and considered to be functional are represented by the antibody comprising (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.7, a HCDR2 as set forth in SEQ ID No.8, and a HCDR3 as set forth in SEQ ID No.9, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.10, a LCDR2 region as set forth in SEQ ID No.11, and a LCDR3 region as set forth in SEQ ID No. 12. From the tested functional variants, the inventors could conclude that further variants have the same properties. These variants are represented by the antibody comprising (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.1, a HCDR2 as set forth in SEQ ID No.2, and a HCDR3 as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.4, a LCDR2 region as set forth in SEQ ID No.5, and a LCDR3 region as set forth in SEQ ID No.6. Hence the above antibody definition covers all functional variants disclosed herein, in particular those disclosed in embodiments 5 and 6 of the embodiment list herein. Accordingly, whenever it is referred herein to an antibody or antigen-binding fragment thereof comprising (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.1, a HCDR2 as set forth in SEQ ID No.2, and a HCDR3 as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.4, a LCDR2 region as set forth in SEQ ID No.5, and a LCDR3 region as set forth in SEQ ID No.6, it is also referred to the specific variants covered by this formula. For example, if an embodiment refers to antibody or antigen-binding fragment thereof comprising (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.1, a HCDR2 as set forth in SEQ ID No.2, and a HCDR3 as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.4, a LCDR2 region as set forth in SEQ ID No.5, and a LCDR3 region as set forth in SEQ ID No.6, it refers also to an antibody or antigen-binding fragment thereof comprising (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.7, a HCDR2 as set forth in SEQ ID No.8, and a HCDR3 as set forth in SEQ ID No.9, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.10, a LCDR2 region as set forth in SEQ ID No.11, and a LCDR3 region as set forth in SEQ ID No. 12, or to an antibody or antigen-binding fragment thereof comprising (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.53, a HCDR2 as set forth in SEQ ID No.60, and a HCDR3 as set forth in SEQ ID No.68, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.56, a LCDR2 region as set forth in SEQ ID No.57, and a LCDR3 region as set forth in SEQ ID No. 58. Cross-reactivity In one embodiment the antibody of the invention does not substantially bind to Gb5 and / or SSEA5. Hence, it does not exhibit cross-reactivity. In one embodiment the antibody of the invention does not substantially bind to SSEA-5. In particular, the antibody has at least 5-fold, at least 10-fold, preferably at least 20-fold higher affinity to GloboH compared to SEEA-5. Hence, it does not exhibit cross-reactivity to SEEA-5. In one embodiment the antibody of the invention does not substantially bind to Gb5. In particular, the antibody has at least 5-fold, preferably at least 10-fold higher affinity to GloboH compared to Gb5. Hence, it does not exhibit cross-reactivity to Gb5. In one embodiment the antibody binds to Globo H with higher affinity than the VK9 antibody, In one embodiment the antibody binds to Globo H with at least 5-fold, preferably at least 10- fold more preferably at least 15-fold higher affinity to Globo H than VK9. In one embodiment the antibody binds to Globo H with higher affinity than the OBI-888. In one embodiment the antibody binds to Globo H with at least 5-fold, preferably at least 10- fold more preferably at least 15-fold higher affinity to Globo H than OBI-888. In one embodiment the antibody binds to Globo H with higher affinity than the antibody R783. In one embodiment the antibody binds to Globo H with at least 5-fold, preferably at least 10- fold more preferably at least 15-fold higher affinity to Globo H than R783. The invention also relates to recombinant nucleic acid molecules capable of encoding said polypeptides, and to vectors and host cells comprising said recombinant nucleic acid molecules. In one embodiment, the antibody is capable of binding to said Globo H with an affinity of better than 10-6M, i.e. a Kd lower than 10-6M. In one embodiment, the antibody is capable of binding to said Globo H with an affinity of better than 10-6M, i.e. a Kd lower than 10-6M, measured by SPR, with immobilized glycan target, and the tested mAb in solution. Affinity calculation performed to eliminate avidity effects, meaning that a monovalent binding affinity is calculated. Targets may also be fragments of said principal target. Thus, a target is also a fragment of said target, capable of eliciting an immune response. A target is also a fragment of said target, capable of binding to a single domain antibody raised against the full length target. Binding of the antibody to Globo H occurs preferably with high affinity: typically, the dissociation constant of the binding between the antibody Globo H is lower than 10−6M, even more preferably, the dissociation constant is lower than 10−7M, most preferably, the dissociation constant is lower than 10−8M. As used herein, a “variant sequence” of the present invention may comprise additions, deletions, or substitutions of one or more amino acids, which do not substantially alter the functional characteristics of the antibodies of the invention compared with the unmodified parent antibody, also referred to as reference antibody. The number of amino acid deletions or substitutions in the variant sequence in comparison with the parent sequence is preferably up to 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, or 40 amino acids. Where variant sequence indicates sequence identity, it means a variant sequence which presents a high sequence identity, such as more than 70%, 75%, 80%, 85%, 90%, 95% or 98% sequence identity with the parent sequence and is preferably characterised by similar properties of the parent sequence, namely affinity, said identity calculated as described below. The percentage of "sequence identity" is determined by comparing two optimally aligned nucleic acid or polypeptide sequences over a "comparison window" on the full length of the reference sequence. A "comparison window" as used herein, refers to the optimal alignment between the reference and variant sequence after that the two sequences are optimally aligned, wherein the variant nucleic acid or polypeptide sequence in the comparison window may comprise additions or deletions (i.e., gaps) of 20 percent or less, usually 5 to 15 percent, or 10 to 12 percent, as compared to the reference sequences (which does not comprise additions or deletions) for optimal alignment. Identity percentage is calculated by determining the number of positions at which the identical nucleic acid bases or amino acid residues occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the reference sequence (i.e., the full length in amino acid or nucleotide) and multiplying the results by 100 to yield the percentage of sequence identity. Two nucleic acid or polypeptide sequences are said to be "identical" if the sequence of nucleotides or amino acids in the two sequences is the same when optimally aligned as described above. Alternatively, a variant sequence may also be any amino acid sequence resulting from allowed substitutions at any number of positions of the parent sequence according to the formula below: Ser substituted by Ser, Thr, Gly, and Asn; Arg substituted by one of Arg, His, Gin, Lys, and Glu; Leu substituted by one of Leu, Ile, Phe, Tyr, Met, and Val; Pro substituted by one of Pro, Gly, Ala, and Thr; Thr substituted by one of Thr, Pro, Ser, Ala, Gly, His, and Gin; Ala substituted by one of Ala, Gly, Thr, and Pro; Val substituted by one of Val, Met, Tyr, Phe, Ile, and Leu; Gly substituted by one of Gly, Ala, Thr, Pro, and Ser; Ile substituted by one of Ile, Met, Tyr, Phe, Val, and Leu; Phe substituted by one of Phe, Trp, Met, Tyr, lie, Val, and Leu; Tyr substituted by one of Tyr, Trp, Met, Phe, Ile, Val, and Leu; His substituted by one of His, Glu, Lys, Gin, Thr, and Arg; Gln substituted by one of Gin, Glu, Lys, Asn, His, Thr, and Arg; Asn substituted by one of Asn, Glu, Asp, Gin, and Ser; Lys substituted by one of Lys, Glu, Gln, His, and Arg; Asp substituted by one of Asp, Glu, and Asn; Glu substituted by one of Glu, Asp, Lys, Asn, Gln, His, and Arg; Met substituted by one of Met, Phe, Ile, Val, Leu, and Tyr. "Humanized " According to an aspect of the invention, an antibody specifically binding Globo H may be a humanized variant sequence of the sequences from immunized chicken. The humanisation of the antibody is aimed to further reduce the possibility of unwanted immunological reaction in a human individual upon administration. More specifically, the invention relates to modified antibodies, which are modified for administration to humans, and the use of such "humanized" antibodies in the treatment of diseases in humans. Humanising an antibody according to the present invention comprises a step of replacing one or more of the chicken amino acids by their human counterpart as found in the human consensus sequence, without that antibody losing its typical character, i.e, the humanisation does not significantly affects the antigen binding capacity of the resulting antibody. Such methods are known by the skilled person in the art. Thus, in some embodiments the antibody or binding-fragment thereof comprises a humanized framework region selected from:- A heavy chain variable region VH comprisingHFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 21, HFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 22, HFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 23, HFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 24, and A light chain variable region VLcomprising LFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 25, LFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 26, LFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 27, LFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 28,- A heavy chain variable region VH comprisingHFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 21, HFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 22, HFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 23, HFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 24, and A light chain variable region VLcomprising LFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 25, LFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 34, LFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 27, LFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 28,- A heavy chain variable region VH comprisingHFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 21, HFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 14, HFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 39, HFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 24, and A light chain variable region VLcomprising LFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 25, LFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 26, LFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 27, LFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 28,- A heavy chain variable region VH comprisingHFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 45, HFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 46, HFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 47, HFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 24, and A light chain variable region VLcomprising LFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 25, LFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 26, LFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 27, LFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 28. More specifically, in some embodiments the antibody or binding-fragment thereof comprises a humanized framework region selected from:- A heavy chain variable region VH comprising HFR1, HFR2, HFR3 and HFR4 of SEQ IDNO: 21, SEQ ID NO: 22, SEQ ID NO: 23 and SEQ ID NO: 24, respectively and A light chain variable region VLcomprising LFR1, LFR2, LFR3 and HFR4 of SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, and SEQ ID NO: 28, respectively.- A heavy chain variable region VH comprising HFR1, HFR2, HFR3 and HFR4 of SEQ IDNO: 21, SEQ ID NO: 22, SEQ ID NO: 23, and SEQ ID NO: 24, respectively and A light chain variable region VLcomprising LFR1, LFR2, LFR3 and HFR4 of SEQ ID NO: 25, SEQ ID NO: 34, SEQ ID NO: 27, and SEQ ID NO: 28, respectively.- A heavy chain variable region VH comprising HFR1, HFR2, HFR3 and HFR4 of SEQ IDNO: 21, SEQ ID NO: 14, SEQ ID NO: 39, and SEQ ID NO: 24, respectively and A light chain variable region VLcomprising LFR1, LFR2, LFR3 and HFR4 of SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, and SEQ ID NO: 28, respectively.- A heavy chain variable region VH comprising HFR1, HFR2, HFR3 and HFR4 of SEQ IDNO: 45, SEQ ID NO: 46, SEQ ID NO: 47, and SEQ ID NO: 24, respectively and A light chain variable region VLcomprising LFR1, LFR2, LFR3 and HFR4 of SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, and SEQ ID NO: 28, respectively. In one embodiment, the invention provides an antibody or antigen-binding fragment thereof binding to Globo H that competes for binding with an antibody or fragment thereof as described herein. Nucleic acid sequences In another embodiment, a recombinant nucleic acid sequence encoding any of the above antigen-binding proteins or variant thereof is also part of the present invention. The invention provides recombinant nucleic acid molecules encoding the antibodies or antigen-binding fragments thereof. Exemplary nucleic acid sequences are set out in SEQ ID Nos.179-182: SEQ ID NO description179 Ab1_VHCS180 Ab1_VL181 cAb9498-VH (Ab1CSh7)182 Ab1CSh7.34_VLThus, the invention provides recombinant nucleic acid molecules comprising the nucleic acid sequences encoding the antibodies or antigen-binding fragments thereof as disclosed herein (e.g. as set forth in one or more of SEQ ID NO 179-182) or a variant thereof. Moreover, the invention provides host cells comprising one or more recombinant nucleic acid molecules encoding the antibodies or antigen-binding fragments thereof as disclosed herein (e.g. as set forth in one or more of SEQ ID NO 179-182), or variants thereof. In particular, the invention provides cells comprising one or more recombinant nucleic acid molecules encoding the antibodies or antigen-binding fragments thereof as disclosed herein (e.g. as set forth in SEQ ID NOs: 179-182), or a variant thereof. In another aspect, the invention provides recombinant nucleic acid molecules and variants thereof encoding a polypeptide specifically binding to Globo H as disclosed herein. In some exemplary embodiments, such variant recombinant nucleic acid molecules share at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to any of SEQ ID NO 179–182 wherein the percentage of sequence identity is determined as described above. These amounts are not meant to be limiting, and increments between the recited percentages are specifically envisioned as part of the disclosure. Polynucleotides or nucleic acid molecules complementary to any such sequences are also encompassed by the present disclosure. The nucleic acid molecules may be single-stranded (coding or antisense) or double- stranded, and may be DNA (genomic, cDNA or synthetic) or RNA molecules. RNA molecules include HnRNA molecules, which contain introns and correspond to a DNA molecule in a one- to-one manner, and mRNA molecules, which do not contain introns. Additional coding or non- coding sequences may, but need not, be present within a polynucleotide of the present disclosure, and a polynucleotide may, but need not, be linked to other molecules and / or support materials. The nucleic acid molecules may comprise a native sequence (i.e., an endogenous sequence that encodes an antibody or a portion thereof) or may comprise a variant of such a sequence. Nucleic acid variants contain one or more substitutions, additions, deletions and / or insertions such that the immunoreactivity of the encoded monoclonal antibody specifically binding to Globo H is not substantially different, relative to a native immunoreactive monoclonal antibody of reference. The effect on the immunoreactivity of the encoded polypeptide may generally be assessed as described herein. In some embodiments, nucleic acid variants exhibit at least about 70% identity, in some embodiments, at least about 80% identity, in some embodiments, at least about 85% identity, in some embodiments, at least about 90% identity, and in some embodiments, at least about 95% identity to a nucleic acid sequence that encodes a native single domain antibody of reference or a portion thereof, wherein the percentage of sequence identity is determined as described above. These amounts are not meant to be limiting, and increments between the recited percentages are specifically envisioned as part of the disclosure. The recombinant nucleic acid molecules of this disclosure can be obtained using chemical synthesis, recombinant methods, or polymerase chain reaction (PCR). Methods of chemical polynucleotide synthesis are well known in the art and need not be described in detail herein. One of skill in the art can use the sequences provided herein and a commercial DNA synthesizer to produce a desired DNA sequence. For preparing polynucleotides using recombinant methods, a polynucleotide comprising a desired sequence can be inserted into a suitable vector, and the vector in turn can be introduced into a suitable host cell for replication and amplification, as further discussed herein. Polynucleotides may be inserted into host cells by any means known in the art. Cells are transformed by introducing an exogenous polynucleotide by direct uptake, endocytosis, transfection, F-mating or electroporation. Once introduced, the exogenous polynucleotide can be maintained within the cell as a non-integrated vector (such as a plasmid) or integrated into the host cell genome. The polynucleotide so amplified can be isolated from the host cell by methods well known within the art. Suitable cloning vectors and expression vectors can include a variety of components, such as promoter, enhancer, and other transcriptional regulatory sequences. The vector may also be constructed to allow for subsequent cloning of an antibody variable domain into different vectors. Suitable cloning vectors may be constructed according to standard techniques, or may be selected from a large number of cloning vectors available in the art. While the cloning vector selected may vary according to the host cell intended to be used, useful cloning vectors will generally have the ability to self-replicate, may possess a single target for a particular restriction endonuclease, and / or may carry genes for a marker that can be used in selecting clones containing the vector. Suitable examples include plasmids and bacterial viruses, e.g., pUC18, pUC19, Bluescript (e.g., pBS SK+) and its derivatives, mp18, mp19, pBR322, pMB9, ColE1, pCR1, RP4, phage DNAs, and shuttle vectors such as pSA3 and pAT28. These and many other cloning vectors are available from commercial vendors such as Merck, BioRad, Strategene, and Invitrogen. Further, the present invention also envisages expression vectors comprising nucleic acid sequences encoding any of the single domain antibodies here disclosed or variants thereof, as well as host cells comprising such expression vectors. It is implied that an expression vector must be replicable in the host cells either as episomes or as an integral part of the chromosomal DNA. Vector components may generally include, but are not limited to, one or more of the following: a signal sequence; an origin of replication; one or more marker genes; suitable transcriptional controlling elements (such as promoters, enhancers and terminator). For expression (i.e., translation), one or more translational controlling elements are also usually required, such as ribosome binding sites, translation initiation sites, and stop codons. The vectors containing the recombinant nucleic acid molecules of interest and / or the recombinant nucleic acid molecules themselves, can be introduced into the host cell by any of a number of appropriate means, including electroporation, transfection employing calcium chloride, rubidium chloride, calcium phosphate, DEAE-dextran, or other substances; microprojectile bombardment; lipofection; and infection (e.g., where the vector is an infectious agent such as vaccinia virus). The choice of the particular procedure will often depend on features of the host cell. Suitable expression systems include constitutive and inducible expression systems in bacteria or yeasts, virus expression systems, such as baculovirus, semliki forest virus and lentiviruses, or transient transfection in insect or mammalian cells. Particularly preferred are pET expression vectors (Novagen) for the cloning and expression of recombinant proteins in E. coli. In the pET system, target genes are cloned in pET plasmids under control of strong bacteriophage T7 transcription and optionally translation signals; expression is induced by providing a source of T7 RNA polymerase in the host cell. T7 RNA polymerase is so selective and active that, when fully induced, almost all of the cell's resources are converted to target gene expression; the desired product can comprise more than 50% of the total cell protein a few hours after induction. The pET-22b(+) vector carries an N-terminal pelB signal sequence for potential periplasmic localization, plus optional C-terminal His^Tag®sequence. Suitable host cells include E. coli, Lactococcus lactis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Pichia pastoris, and the like. Suitable animal host cells include HEK 293, COS, S2, CHO, NSO, DT40 and the like. Particularly preferred are ArcticExpress®E. Coli cells. The cloning, expression and / or purification of the antigen- binding proteins can be done according to techniques known by the person skilled in the art, including the Baculovirus-infected Insect Cell system. Another aspect of the present invention is directed to an antibody drug conjugate comprising the antibody described herein. Thus, the present invention is also directed to an antibody specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, wherein the antibody is conjugated to conjugated to a toxophore or toxic component. Said conjugate is particularly useful in the therapeutic treatment of tumors, as the experimental data indicate (see for instance Figure 21). Thus, in a preferred embodiment, the antibody specifically binding Globo H comprises (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No. 6, wherein the antibody is conjugated to a toxophore, a toxic component or radiating component is selected from: auristatin E, monomethyl auristatin E, monomethyl auristatin F, dolastatin, maytansine, ansamitocin, emtansine, soravtansine, duocarmycin A, duocarmycin BL duocarmycin B2, duocarmycin CI, duocarmycin C2, duocarmycin D, duocarmycin SA, duocarmycin MA, CC-1065, amiodarone, clarithromycin, ciclosporin, colchicine, diltiazem, erythromycin, felodipine, ketoconazole, lansoprazole, omeprazole, nifedipine, paroxetine, reserpine, saquinavir, sertraline, quinidine, tamoxifen, verapamil, duloxetine, elacridar CP 100356, zosuquidar, tariquidar, deruxtecan, exatecan, topotecan, belotecan, gimatecan, Dxd, lurtotecan, Irinotecan, Zirconium, Radium, Actinium, Thorium, and Lutetium. Preferably, the toxophore or toxic component is selected from monomethyl auristatin E (MMAE), deruxtecan, or exatecan. In one embodiment the toxophore is MMAE. In a further embodiment, the antibody is conjugated to the toxophore, the toxic component or the radiating component via a Lys-Val-Cit-PABC or Lys-GGFG, or Cys-Val-Cit-PABC, or Cys- GGFG linker. In a further embodiment, the antibody is directly conjugated to the toxophore, the toxic component or the radiating component. In another embodiment, the molar ratio between the toxophore, the toxic component or the radiating component and the antibody (DAR) is between 2 and 12, more preferably, between 2 and 40 and most preferably between 4 and 8. In a preferred embodiment, the molar ratio between the toxophore, the toxic component or the radiating component and the antibody is about 4. In a preferred embodiment, the molar ratio between the toxophore, the toxic component or the radiating component and the antibody is about 8. As used herein, the term "multispecific" refers to the ability to bind to at least two different epitopes, e.g. on different antigens or on the same antigen. While a conventional monospecific IgG-type antibodies usually have two identical epitope binding sites (paratopes) and can, thus, only bind to identical epitopes (but not to different epitopes). A multispecific antibody, in contrast, has at least two different types of paratopes (antigen-binding sites) and can, thus, bind to at least two different epitopes. As used herein, "paratope" refers to an antigen-binding site (or epitope-binding site) of the antibody. Moreover, a single "specificity" may refer to one, two, three or more identical paratopes in a single antibody (the actual number of paratopes in one single antibody molecule is referred to as "valency"). For example, a single native IgG antibody is monospecific and bivalent, since it has two identical paratopes. Accordingly, a multispecific antibody comprises at least two (different) paratopes. Thus, the term "multispecific antibodies" refers to antibodies having more than one paratope and the ability to bind to two or more different epitopes. The term "multispecific antibodies" comprises in particular bispecific antibodies, but typically also protein, e.g. antibody scaffolds, which bind in particular to three or more different epitopes, i.e., antibodies with three or more different paratopes. In particular, the multispecific antibody, or the multispecific antigen binding fragment, of the invention may comprise two or more paratopes, wherein one or more paratopes may be identical so that all paratopes of the antibody belong to at least two different types of paratopes and, hence, the antibody has at least two specificities. Monoclonal antibody based CAR-T cell therapy The term "chimeric antigen receptor", or "CAR" as used herein, refers to an artificially constructed hybrid protein or polypeptide comprising the antigen binding domain of the antibody according to the invention linked to a T-cell transmembrane domain, which is in turn linked to a T cell intracellular signaling or activation domain; the linking between the antibody and the transmembrane domain may occur through a hinge region. Domains or other functional or structural sequence of a CAR, e.g., a transmembrane domain or intracellular activation or signaling domain, is referred to as an element or module of said CAR. CARs are able to redirect T-cell specificity and reactivity toward a selected target in a non- MHC-restricted manner, exploiting the antigen-binding properties of antibodies. The antigen recognition module, also referred to as ectodomain, of CAR T cells is usually a scFv, linked to a hinge region, a transmembrane region, a costimulatory domain, and a cytoplasmic activation domain, such as the CD3-zeta or FcRγ intracellular signaling domain. However, scFvs do not always fold efficiently and can be prone to aggregation. In contrast, the variable regions of heavy-chain−only antibodies (VHHs or sdAbs) are small, stable, single-domain antibody fragments with affinities comparable to traditional scFvs. A major difficulty in developing CAR T cells for cancer treatment is the lack of targetable antigens (Xie et al., 2018). Most antigens proposed as CAR T cell targets to treat cancers are exclusive to a specific cancer type, and limited information on cancer-specific antigens for the vast majority of cancers renders unsuitable CAR T cell therapy. Thus, an aspect of particular advantage of the present invention is to provide CARs specifically targeting Globo H that are expressed in a variety of cancers, and that can be used to engineer anti-glycan CAR T cells, which can then be used to treat several different cancers. Therefore, an embodiment of the present invention is CAR specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, conjugated to a transmembrane region and an intracellular T-cell receptor signaling domain. In one embodiment of the present invention, the CAR specifically binding Globo H comprises (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No. 1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No. 6, conjugated to at least one extracellular hinge region, at least one transmembrane domain, at least one costimulatory domain, and at least one intracellular activation domain. Said conjugate is a T cell chimeric antigen receptor, wherein the light and heavy chain variable regions, the at least one extracellular hinge region, the at least one transmembrane domain, the at least one costimulatory domain, and the at least one intracellular activation domain are comprised in that chimeric antigen receptor in an N-terminal to C-terminal direction. More in particular, an embodiment of the present invention is a CAR specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, conjugated to at least one extracellular CD8-alpha hinge region, at least one CD8-alpha or CD28 transmembrane domain, at least one CD28, 4-IBB, ICOS costimulatory domain, and at least one CD3-zeta intracellular activation domain. A more preferred embodiment of the invention is a CAR specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No. 3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6 conjugated to at least one extracellular hinge region, at least one transmembrane domain, at least one costimulatory domain, and at least one intracellular activation domain for use in treatment of cancer, wherein the cancer cells of said cancer express on their surface Globo H. A more preferred embodiment of the invention is a CAR specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No. 3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6 conjugated to at least one extracellular hinge region, at least one transmembrane domain, at least one costimulatory domain, and at least one intracellular activation domain, thereby forming a chimeric antigen receptor, for use in treatment of cancer, wherein the cancer cells of said cancer express on their surface Globo H, and wherein the cancer is selected from adenocarcinoma, choroidal melanoma, acute leukemia, acoustic neurinoma, ampullary carcinoma, anal carcinoma, astrocytoma, basal cell carcinoma, pancreatic cancer, desmoid tumor, bladder cancer, bronchial carcinoma, breast cancer, Burkitt's lymphoma, corpus cancer, CUP-syndrome (carcinoma of unknown primary), colorectal cancer, small intestine cancer, small intestinal tumors, ovarian cancer, endometrial carcinoma, ependymoma, epithelial cancer types, Ewing's tumors, gastrointestinal tumors, gastric cancer, gallbladder cancer, gall bladder carcinomas, uterine cancer, cervical cancer, cervix, glioblastomas, gynecologic tumors, ear, nose and throat tumors, hematologic neoplasias, hairy cell leukemia, urethral cancer, skin cancer, skin testis cancer, brain tumors (gliomas), brain metastases, testicle cancer, hypophysis tumor, carcinoids, Kaposi's sarcoma, laryngeal cancer, germ cell tumor, bone cancer, colorectal carcinoma, head and neck tumors (tumors of the ear, nose and throat area), colon carcinoma, craniopharyngiomas, oral cancer (cancer in the mouth area and on lips), cancer of the central nervous system, liver cancer, liver metastases, leukemia, eyelid tumor, lung cancer, lymph node cancer (Hodgkin's / Non- Hodgkin's), lymphomas, stomach cancer, malignant melanoma, malignant neoplasia, malignant tumors gastrointestinal tract, breast carcinoma, rectal cancer, medulloblastomas, melanoma, meningiomas, Hodgkin's disease, mycosis fungoides, nasal cancer, neurinoma, neuroblastoma, kidney cancer, renal cell carcinomas, non-Hodgkin's lymphomas, oligodendroglioma, esophageal carcinoma, osteolytic carcinomas and osteoplastic carcinomas, osteosarcomas, ovarial carcinoma, pancreatic carcinoma, penile cancer, plasmocytoma, prostate cancer, pharyngeal cancer, rectal carcinoma, retinoblastoma, vaginal cancer, thyroid carcinoma, Schneeberger disease, esophageal cancer, spinalioms, T-cell lymphoma (mycosis fungoides), thymoma, tube carcinoma, eye tumors, urethral cancer, urologic tumors, urothelial carcinoma, vulva cancer, wart appearance, soft tissue tumors, soft tissue sarcoma, Wilm's tumor, cervical carcinoma and tongue cancer. A more preferred embodiment of the invention is a CAR specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No. 3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6 conjugated to at least one extracellular hinge region, at least one transmembrane domain, at least one costimulatory domain, and at least one intracellular activation domain, for use in treatment of cancer, wherein the cancer cells of said cancer express on their surface Globo H, and wherein the cancer is selected from brain cancer, liver cancer, bile duct cancer, kidney cancer, breast cancer, prostate cancer, lung cancer, small cell lung cancer, ovarian cancer, cervix cancer, esophagus cancer, stomach cancer, pancreatic cancer and colorectal cancer. The hinge region of the chimeric antigen receptor is usually derived from the human CD8- alpha chain (exemplary sequence SEQ ID NO: 4 in WO2016019300 A1, or a fragment thereof as described in US 20160303166 A1). The transmembrane domain of the chimeric antigen receptor crosses the plasma membrane and links the extracellular domain and intracellular signal domain. Examples of the transmembrane domain include but are not limited to human CD28 (exemplary sequence: residues 153-179 of SEQ ID NO:4 in US 20160303166 A1), CD8-alpha (exemplary sequence SEQ ID NO: 12 in WO2016019300 A1). The intracellular activation domain transmits the signals necessary for exertion of the effector function of the CAR T cell. More specifically, when the extracellular domain binds with the target Globo H series glycan, an intracellular activation domain transmits the signals necessary for activation of the cells. The intracellular activation domain is usually human CD3-zeta (exemplary sequences SEQ ID NO: 18 or 20 in WO2016019300 A1). "Costimulatory domain" (CSD) as used herein refers to the portion of the CAR which enhances the proliferation, survival and / or development of memory cells. The CARs of the invention may comprise one or more co-stimulatory domains. Each costimulatory domain can comprise the costimulatory domain of, for example, CD28 (exemplary sequence SEQ ID NO: 44 in WO2016019300 A1), 4-1BB (CD137, exemplary sequence SEQ ID NO: 14 in WO2016019300 A1), and ICOS (exemplary sequence SEQ ID NO:263 in WO2016014553 A1). Methods for constructing chimeric antigen receptors have been described in the prior art, such as in US 20160303166 A1, WO2016014553 A1, Xie et al. PNAS 2018. Moreover, the present invention also describes a method for generating a genetically engineered chimeric antigen receptor T-cell (CAR T-cell), comprising: a) generating a chimeric antigen receptor (CAR) construct, having at least one antibody specifically binding Globo H, at least one extracellular hinge region, at least one transmembrane domain, at least one costimulatory domain, and at least one intracellular activation domain of a chimeric antigen receptor, wherein the antibody is linked to the extracellular hinge region, b) transfecting T cells removed from blood of a subject, c) expressing the CAR construct to produce a functional CAR in the T cells to produce a CAR T cell specifically recognizing Globo H. Genetically engineered T cells which may comprise and express the CARs of the invention include, but are not limited to, T-lymphocytes (T-cells), naive T cells (TN), memory T cells (for example, central memory T cells (TCM), effector memory cells (TEM)), natural killer cells, hematopoietic stem cells and / or pluripotent embryonic / induced stem cells capable of giving rise to therapeutically relevant progeny. In an embodiment, the genetically engineered cells are autologous cells. By way of example, individual T-cells of the invention may be CD4+ / CD8-, CD4- / CD8+, CD4- / CD8- or CD4+ / CD8+. The T-cells may be a mixed population of CD4+ / CD8- and CD4- / CD8+cells or a population of a single clone. CD4+T-cells of the invention may produce IL-2, IFNy, TNFa and other T-cell effector cytokines when co-cultured in vitro with cells expressing the target antigens (i.e., cancer cells expressing a Globo H series glycan). CD8+T-cells of the invention may lyse antigen-specific target cells when co- cultured in vitro with the target cells (i.e., cancer cells expressing a Globo H series glycan). Finally, the present invention also describes a method for treating a subject having a cancer, wherein the cancer cells of said cancer express on their surface Globo H, comprising administering to the subject having said cancer a chimeric antigen receptor T-cell (CAR T cell) specifically recognizing Globo H, wherein said CAR T cell expresses a functional CAR polypeptide comprising an antibody specifically binding Globo H as disclosed herein, at least one extracellular hinge region, at least one transmembrane domain, at least one costimulatory domain, and at least one intracellular activation domain, in an effective amount to treat the subject having said cancer. “Pharmaceutical composition” refers to a preparation in a form that allows the biological activity of the active ingredient(s) to be effective, and which contain no additional components which are toxic to the subjects to which the formulation is administered. As used herein, the terms "pharmaceutically acceptable", "physiologically tolerable" and grammatical variations thereof, are used interchangeably and represent that the materials are capable of administration to or upon a mammal without the production of undesirable physiological effects such as weight loss, nausea, dizziness, gastric upset, and the like. The pharmaceutical composition is designed to facilitate the administering of the inventive polypeptides comprising the single domain antibodies in an effective manner. “Pharmaceutically acceptable vehicle” refers to an ingredient in a pharmaceutical formulation, other than an active ingredient, which is nontoxic to the subject to whom it is administered. A pharmaceutically acceptable vehicle includes, but is not limited to, a buffer, stabilizer, or preservative. Examples of suitable vehicles or excipients include, without limitation, lactose, dextrose, sucrose, glucose, powdered sugar, sorbitol, mannitol, xylitol, starches, acacia gum, xanthan gum, guar gum, tara gum, mesquite gum, fenugreek gum, locust bean gum, ghatti gum, tragacanth gum, inositol, molasses, maltodextrin, extract of Irish moss, panwar gum, mucilage of isapol husks, Veegum, larch arabogalactan, calcium silicate, calcium phosphate, dicalcium phosphate, calcium sulfate, kaolin, sodium chloride, sodium phosphate, polyethylene glycol, alginates, gelatine, microcrystalline cellulose, polyvinylpyrrolidone, cellulose, water, saline, syrup, methylcellulose, ethylcellulose, hydroxypropylnethylcellulose, carboxymethylcellulose, polyacrylic acids such as Carbopols, such as Carbopol941, Carbopol980, Carbopol981, and gum bases such as PharmagumTM(SPI Pharma Group; New Castle, Del.), and similar. Typically, the compositions of the present invention comprise from about 10% to about 90% by weight, the excipient or combinations thereof. Preferably, the pharmaceutical composition contains from about 0.001% to about 90%, preferably from about 0.01% to about 75%, more preferably from about 0.1% to 50%, and still more preferably from about 0.1% to 10% by weight of the polypeptide of the present invention, with the remainder consisting of suitable pharmaceutical vehicles, excipients, and / or diluents. The pharmaceutical composition can be formulated into powders, granules, tablets, capsules, suspensions, emulsions, syrups, oral dosage form, external preparation, suppository or in the form of sterile injectable solutions, such as aerosolized in a usual manner, respectively. When formulated, it can be prepared using a diluent or excipient such as generally used fillers, extenders, binders, wetting agents, disintegrating agents, surface active agents. In the pharmaceutical composition, the solid preparation for oral administration may be a tablet, pill, powder, granule, or capsule. The solid preparation may further comprise an excipient. Excipients may be, for example, starch, calcium carbonate, sucrose, lactose, or gelatine. In addition, the solid preparation may further comprise a lubricant, such as magnesium stearate, or talc. In the pharmaceutical composition, liquid preparations for oral administration may be best suspensions, solutions, emulsions, or syrups. The liquid formulation may comprise water, or liquid paraffin. The liquid formulation may, for excipients, for example, include wetting agents, sweeteners, aromatics or preservatives. For the purposes of parenteral administration, compositions containing the polypeptides of the invention are preferably dissolved in distilled water and the pH preferably adjusted to about 6 to 8. Useful preparations of the compositions of the invention for parenteral administration also include sterile aqueous and non-aqueous solvents, suspensions and emulsions. Examples of useful non-aqueous solvents include propylene glycol, polyethylene glycol, vegetable oil, fish oil, and injectable organic esters. An embodiment of the present invention is a pharmaceutical composition comprising an antibody specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.1, and a VHCDR3 region as set forth in SEQ ID No.1, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.3, a VLCDR2 region as set forth in SEQ ID No.4, and a VLCDR3 region as set forth in SEQ ID No.5 together with at least one pharmaceutically acceptable vehicle, excipient and / or diluent. Another embodiment of the present invention is a pharmaceutical composition comprising an antibody specifically binding Globo H as disclosed herein, for example an antibody comprising (1) a heavy chain variable region VHcomprising an amino acid sequence of at least 95% sequence identity to a sequence as set forth in SEQ ID No.104 or a humanized variant thereof, and (2) a light chain variable region VLcomprising an amino acid sequence of at least 95% sequence identity to a sequence as set forth in SEQ ID No.146 or a humanized variant thereof, together with at least one pharmaceutically acceptable vehicle, excipient and / or diluent. Another particular embodiment of the present invention is a pharmaceutical composition comprising an antibody specifically binding Globo H as disclosed herein, for example an antibody comprising (1) a heavy chain variable region VHcomprising an amino acid sequence as set forth in SEQ ID No.104, and (2) a light chain variable region VLcomprising an amino acid sequence as set forth in SEQ ID No.146, together with at least one pharmaceutically acceptable vehicle, excipient and / or diluent. Another embodiment of the present invention is directed to antibody binding a globo-series glycan comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, or the pharmaceutical composition comprising said antibody, for use in treatment and / or diagnosis of cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan. Another embodiment of the present invention relates to an antibody specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No. 6, or the pharmaceutical composition comprising said antibody, for use in treatment and / or diagnosis of cancer, wherein the cancer cells of said cancer express on their surface Globo H, and wherein the cancer is selected from adenocarcinoma, choroidal melanoma, acute leukemia, acoustic neurinoma, ampullary carcinoma, anal carcinoma, astrocytoma, basal cell carcinoma, pancreatic cancer, desmoid tumor, bladder cancer, bronchial carcinoma, breast cancer, Burkitt's lymphoma, corpus cancer, CUP-syndrome (carcinoma of unknown primary), colorectal cancer, small intestine cancer, small intestinal tumors, ovarian cancer, endometrial carcinoma, ependymoma, epithelial cancer types, Ewing's tumors, gastrointestinal tumors, gastric cancer, gallbladder cancer, gall bladder carcinomas, uterine cancer, cervical cancer, cervix, glioblastomas, gynecologic tumors, ear, nose and throat tumors, hematologic neoplasias, hairy cell leukemia, urethral cancer, skin cancer, skin testis cancer, brain tumors (gliomas), brain metastases, testicle cancer, hypophysis tumor, carcinoids, Kaposi's sarcoma, laryngeal cancer, germ cell tumor, bone cancer, colorectal carcinoma, head and neck tumors (tumors of the ear, nose and throat area), colon carcinoma, craniopharyngiomas, oral cancer (cancer in the mouth area and on lips), cancer of the central nervous system, liver cancer, liver metastases, leukemia, eyelid tumor, lung cancer, lymph node cancer (Hodgkin's / Non- Hodgkin's), lymphomas, stomach cancer, malignant melanoma, malignant neoplasia, malignant tumors gastrointestinal tract, breast carcinoma, rectal cancer, medulloblastomas, melanoma, meningiomas, Hodgkin's disease, mycosis fungoides, nasal cancer, neurinoma, neuroblastoma, kidney cancer, renal cell carcinomas, non-Hodgkin's lymphomas, oligodendroglioma, esophageal carcinoma, osteolytic carcinomas and osteoplastic carcinomas, osteosarcomas, ovarial carcinoma, pancreatic carcinoma, penile cancer, plasmocytoma, prostate cancer, pharyngeal cancer, rectal carcinoma, retinoblastoma, vaginal cancer, thyroid carcinoma, Schneeberger disease, esophageal cancer, spinalioms, T-cell lymphoma (mycosis fungoides), thymoma, tube carcinoma, eye tumors, urethral cancer, urologic tumors, urothelial carcinoma, vulva cancer, wart appearance, soft tissue tumors, soft tissue sarcoma, Wilm's tumor, cervical carcinoma and tongue cancer. Another embodiment of the present invention relates to an antibody specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No. 6, or the pharmaceutical composition comprising said antibody, for use in treatment and / or diagnosis of cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan, and wherein the cancer is selected from brain cancer, liver cancer, bile duct cancer, kidney cancer, breast cancer, prostate cancer, lung cancer, small cell lung cancer, ovarian cancer, cervix cancer, esophagus cancer, stomach cancer, pancreatic cancer and colorectal cancer. Another aspect is directed to an antibody specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, or the pharmaceutical composition comprising said antibody, for use in treatment and / or diagnosis of cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan and wherein the antibody is conjugated to a toxophore, a toxic component or a radiating component. Preferably, the toxophore, the toxic component or the radiating component is selected from: auristatin E, monomethyl auristatin E, monomethyl auristatin F, dolastatin, maytansine, ansamitocin, emtansine, soravtansine, duocarmycin A, duocarmycin BL duocarmycin B2, duocarmycin CI, duocarmycin C2, duocarmycin D, duocarmycin SA, duocarmycin MA, CC- 1065, amiodarone, clarithromycin, ciclosporin, colchicine, diltiazem, erythromycin, felodipine, ketoconazole, lansoprazole, omeprazole, nifedipine, paroxetine, reserpine, saquinavir, sertraline, quinidine, tamoxifen, verapamil, duloxetine, elacridar CP 100356, zosuquidar, tariquidar, deruxtecan, exatecan, topotecan, belotecan, gimatecan, Dxd, lurtotecan, Irinotecan, Zirconium, Radium, Actinium, Thorium, and Lutetium. Most preferably, the toxophore or toxic component is monomethyl auristatin E, deruxtecan, or exatecan. Another aspect is directed to an antibody specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No. 1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, or the pharmaceutical composition comprising said antibody, for use in treatment and / or diagnosis of cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan and wherein the antibody is a T-cell-engaging bispecific antibody simultaneously specifically binding Globo H and CD3. Another aspect is directed to an antibody specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No. 1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, or the pharmaceutical composition comprising said antibody, for use in treatment and / or diagnosis of cancer, wherein the cancer cells of said cancer express on their surface Globo H, wherein the cancer is selected from adenocarcinoma, choroidal melanoma, acute leukemia, acoustic neurinoma, ampullary carcinoma, anal carcinoma, astrocytoma, basal cell carcinoma, pancreatic cancer, desmoid tumor, bladder cancer, bronchial carcinoma, breast cancer, Burkitt's lymphoma, corpus cancer, CUP-syndrome (carcinoma of unknown primary), colorectal cancer, small intestine cancer, small intestinal tumors, ovarian cancer, endometrial carcinoma, ependymoma, epithelial cancer types, Ewing's tumors, gastrointestinal tumors, gastric cancer, gallbladder cancer, gall bladder carcinomas, uterine cancer, cervical cancer, cervix, glioblastomas, gynecologic tumors, ear, nose and throat tumors, hematologic neoplasias, hairy cell leukemia, urethral cancer, skin cancer, skin testis cancer, brain tumors (gliomas), brain metastases, testicle cancer, hypophysis tumor, carcinoids, Kaposi's sarcoma, laryngeal cancer, germ cell tumor, bone cancer, colorectal carcinoma, head and neck tumors (tumors of the ear, nose and throat area), colon carcinoma, craniopharyngiomas, oral cancer (cancer in the mouth area and on lips), cancer of the central nervous system, liver cancer, liver metastases, leukemia, eyelid tumor, lung cancer, lymph node cancer (Hodgkin's / Non-Hodgkin's), lymphomas, stomach cancer, malignant melanoma, malignant neoplasia, malignant tumors gastrointestinal tract, breast carcinoma, rectal cancer, medulloblastomas, melanoma, meningiomas, Hodgkin's disease, mycosis fungoides, nasal cancer, neurinoma, neuroblastoma, kidney cancer, renal cell carcinomas, non-Hodgkin's lymphomas, oligodendroglioma, esophageal carcinoma, osteolytic carcinomas and osteoplastic carcinomas, osteosarcomas, ovarial carcinoma, pancreatic carcinoma, penile cancer, plasmocytoma, prostate cancer, pharyngeal cancer, rectal carcinoma, retinoblastoma, vaginal cancer, thyroid carcinoma, Schneeberger disease, esophageal cancer, spinalioms, T- cell lymphoma (mycosis fungoides), thymoma, tube carcinoma, eye tumors, urethral cancer, urologic tumors, urothelial carcinoma, vulva cancer, wart appearance, soft tissue tumors, soft tissue sarcoma, Wilm's tumor, cervical carcinoma and tongue cancer, and wherein the antibody is a T-cell-engaging bispecific antibody simultaneously specifically binding Globo H and CD3. A further embodiment of the present invention is directed to a CAR specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, conjugated to a transmembrane region and an intracellular T-cell receptor signaling domain, for use in treatment of cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan. A further embodiment of the present invention is directed to a CAR specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.4, and a VLCDR3 region as set forth in SEQ ID No.5, conjugated to at least one CAR extracellular hinge region, at least one CAR transmembrane domain, at least one CAR costimulatory domain, and at least one CAR intracellular activation domain, for use in treatment of cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan. Another further embodiment of the present invention is directed to a CAR specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, conjugated to at least one extracellular CD8- alpha hinge region, at least one CD8-alpha or CD28 transmembrane domain, at least one CD28, 4-IBB, ICOS costimulatory domain, and at least one CD3-zeta intracellular activation domain, for use in treatment of cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan A further embodiment of the present invention is directed to a polypeptide specifically binding a globo-series glycan comprising at least one single domain antibody, wherein said single domain antibody is a variable domain of a heavy chain antibody naturally devoid of a light chain and naturally devoid of the constant region 1, or a variant of said variable domain, and wherein said single domain antibody binds at least one globo-series glycan selected from Globo H, Gb3, Gb4, and Gb5, and further comprising at least one CAR extracellular hinge region, at least one CAR transmembrane domain, at least one CAR costimulatory domain, and at least one CAR intracellular activation domain, wherein the single domain antibody is linked to the CAR extracellular hinge region, for use in treatment of cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan selected from Globo H, Gb3, Gb4, and Gb5, and wherein said cancer is selected from brain cancer, liver cancer, bile duct cancer, kidney cancer, breast cancer, prostate cancer, lung cancer, small cell lung cancer, ovarian cancer, cervix cancer, esophagus cancer, stomach cancer, pancreatic cancer and colorectal cancer. Another further embodiment of the present invention is directed to a CAR specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, conjugated to at least one extracellular CD8- alpha hinge region, at least one CD8-alpha or CD28 transmembrane domain, at least one CD28, 4-IBB, ICOS costimulatory domain, and at least one CD3-zeta intracellular activation domain, for use in treatment of cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan, and wherein said cancer is selected from brain cancer, liver cancer, bile duct cancer, kidney cancer, breast cancer, prostate cancer, lung cancer, small cell lung cancer, ovarian cancer, cervix cancer, esophagus cancer, stomach cancer, pancreatic cancer and colorectal cancer. Also described herein is a method for the treatment of a cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan, comprising administering to a patient suffering from said cancer a therapeutically effective amount of an antibody as disclosed herein or a therapeutically effective amount of a pharmaceutical composition comprising said antibody. In particular, it is described a method for the treatment of a cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan, comprising administering to a patient suffering from said cancer a therapeutically effective amount of an antibody specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6, or a therapeutically effective amount of the pharmaceutical composition comprising said antibody. Also described herein is a method for the treatment of a cancer, wherein the cancer cells of said cancers express on their surface at least one globo-series glycan, comprising administering to a patient suffering from said cancer a therapeutically effective amount of an antibody as disclosed herein or a therapeutically effective amount of a pharmaceutical composition comprising said antibody, wherein said cancer is selected from the group comprising brain cancer, liver cancer, bile duct cancer, kidney cancer, breast cancer, prostate cancer, lung cancer, small cell lung cancer, ovarian cancer, cervix cancer, esophagus cancer, stomach cancer, pancreatic cancer and colorectal cancer. A further embodiment describes a method of diagnosing a cancer characterized by cancer cells expressing on their surface Globo H, comprising the steps of: a) contacting a sample with an antibody specifically binding Globo H as disclosed herein b) detecting binding of said antibody to said sample c) comparing the binding detected in step b) with a standard, wherein a difference in binding relative to said sample is diagnostic of a cancer characterized by cancer cells expressing on their surface at least one globo-series glycan. “Disorder” is any condition that would benefit from treatment with a substance / molecule or method described herein. “Cell proliferative disorder” and “proliferative disorder” refer to disorders that are associated with some degree of abnormal cell proliferation, such as cancer. “Cancer” and “cancerous” refer to, or describe a physiological condition in mammals that is typically characterized by a cell proliferative disorder. Cancer generally can include, but is not limited to, carcinoma, lymphoma (e.g.，Hodgkin's and non-Hodgkin's lymphoma), blastoma, sarcoma, and leukemia. More specific examples of cancer can include, squamous cell cancer, small-cell lung cancer, non-small cell lung cancer, adenocarcinoma of the lung, squamous carcinoma of the lung, cancer of the peritoneum, hepatocellular cancer, gastrointestinal cancer, pancreatic cancer, glioma, cervical cancer, ovarian cancer, liver cancer, bladder cancer, hepatoma, breast cancer, colon cancer, colorectal cancer, endometrial or uterine carcinoma, salivary gland carcinoma, kidney cancer, liver cancer, prostate cancer, vulval cancer, thyroid cancer, hepatic carcinoma, leukemia and other lymphoproliferative disorders, and various types of head and neck cancer. “Tumor” refers to all neoplastic cell growth and proliferation, whether malignant or benign, and all pre-cancerous and cancerous cells and tissues. The terms “cancer”, “cancerous”, “cell proliferative disorder”, “proliferative disorder”, and “tumour” are not mutually exclusive as referred to herein. “Metastasis” refers to the spread of cancer and / or tumour from its primary site to other places in the body of an individual. “Treatment, ” “treat” or “treating” refers to clinical intervention in an attempt to alter the natural course of a disorder in the individual being treated, and can be performed either for prophylaxis or during the course of clinical pathology. Desired results of treatment can include, but are not limited to, preventing occurrence or recurrence of the disorder, alleviation of symptoms, diminishment of any direct or indirect pathological consequences of the disorder, preventing metastasis, decreasing the rate of progression, amelioration or palliation of a disease state, and remission or improved prognosis. For example, treatment can include administration of a therapeutically effective amount of pharmaceutical formulation comprising an anti-Globo H antibody to a subject to delay development or slow progression of a cancer, wherein the cancer cells of said cancer express on their surface at least one globo-series glycan selected from Globo H, Gb3, Gb4, and Gb5. “Pharmaceutical formulation” refers to a preparation in a form that allows the biological activity of the active ingredient(s) to be effective, and which contain no additional components which are toxic to the subjects to which the formulation is administered. “Pharmaceutically acceptable carrier” refers to an ingredient in a pharmaceutical formulation, other than an active ingredient, which is nontoxic to the subject to whom it is administered. A pharmaceutically acceptable carrier includes, but is not limited to, a buffer, excipient, stabilizer, or preservative. “Therapeutically effective amount” refers to the amount of an active ingredient or agent (e.g.，a pharmaceutical formulation) to achieve a desired therapeutic or prophylactic result, e.g., to treat or prevent a disease or disorder in a subject. In the case of a cancer, the therapeutically effective amount of the therapeutic agent is an amount that reduces the number of cancer cells；reduces the primary tumour size； inhibits (i.e., slows to some extent and preferably stop) cancer cell infiltration into peripheral organs; inhibits (i.e., slows to some extent and preferably stop) tumour metastasis; inhibits, to some extent, tumour growth; and / or relieves to some extent one or more of the symptoms associated with the cancer. To the extent the drug may prevent growth and / or kill existing cancer cells, it may be cytostatic and / or cytotoxic. For cancer therapy, efficacy in vivo can, for example, be measured by assessing the duration of survival, time to disease progression (TTP), the response rates (RR), tumor growth inhinition (TGI), duration of response, and / or quality of life. “Individual” or “subject” refers to a mammal, including but not limited to, domesticated animals (e.g.，cows, sheep, cats, dogs, and horses), primates (e.g.，humans and non- human primates such as monkeys), rabbits, and rodents (e.g.，mice and rats) . “Anti-cancer therapeutic” refers to an agent useful for treating cancer. Exemplary anti- cancer therapeutics include, but are not limited to, chemotherapeutic agents, growth inhibitory agents, cytotoxic agents, agents used in radiation therapy, anti-angiogenesis agents, apoptotic agents, anti-tubulin agents, and other agents to treat cancer, anti-CD20 antibodies, platelet derived growth factor inhibitors, a COX-2 inhibitor, interferons, cytokines, antagonists that bind to one or more targets (e.g., PDGFR-beta, APRIL, BCMA receptor, TRAIL / Apo2), other bioactive and organic chemical agents, and combinations thereof. A further embodiment of the present invention is a diagnostic kit for the detection of cells expressing on their surface Globo H comprising antibody or antigen-binding fragment thereof specifically binding Globo H as described herein. A diagnostic kit as described herein may further comprise reagents needed for the labeling and / or detection and / or quantification of the antigen-binding cells. One embodiment thus refers to a diagnostic kit for the detection of cells expressing on their surface Globo H comprising antibody specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No.6. Slightly reworded, the present invention is also directed to a diagnostic kit comprising antibody or antigen-binding fragment as as described herein, e.g. an antibody specifically binding Globo H comprising (1) a heavy chain variable region VHcomprising a VHCDR1 region as set forth in SEQ ID No.1, a VHCDR2 region as set forth in SEQ ID No.2, and a VHCDR3 region as set forth in SEQ ID No. 3, and (2) a light chain variable region VLcomprising a VLCDR1 region as set forth in SEQ ID No.4, a VLCDR2 region as set forth in SEQ ID No.5, and a VLCDR3 region as set forth in SEQ ID No. 6, for screening for a cancer characterized by cells expressing on their surface at least one globo-series glycan. As mentioned above, the single domain antibodies of the present invention can be used for diagnostic purposes when linked to effector molecules being detectable labels. Suitable detectable labels and techniques for attaching, using and detecting them will be clear to the skilled person and, for example, include, but are not limited to, fluorescent molecules (such as fluorescein, isothiocyanate, rhodamine, phycoerythrin, phycocyanin, allophycocyanin, o-phthaldehyde, and fluorescamine and fluorescent metals such as Eu or others metals from the lanthanide series), phosphorescent molecules, chemiluminescent molecules or bioluminescent molecules (such as luminal, isoluminol, theromatic acridinium ester, imidazole, acridinium salts, oxalate ester, dioxetane or GFP and its analogs), radio- isotopes, metals, metal chelates or metallic cations or other metals or metallic cations that are particularly suited for use in in vivo, in vitro or in situ diagnosis and imaging, as well as chromophores and enzymes (such as malate dehydrogenase, staphylococcal nuclease, delta-V-steroid isomerase, yeast alcohol dehydrogenase, alpha-glycerophosphate dehydrogenase, triose phosphate isomerase, biotinavidin peroxidase, horseradish peroxidase, alkaline phosphatase, asparaginase, glucose oxidase, beta-galactosidase, ribonuclease, urease, catalase, glucose-VI-phosphate dehydrogenase, glucoamylase and acetylcholine esterase). Therefore, a further embodiment of the present invention is a diagnostic kit comprising a polypeptide specifically binding a globo-series glycan comprising at least one single domain antibody, or a variant of said variable domain, wherein said single domain antibody binds at least one globo-series glycan selected from Globo H, Gb3, Gb4, and Gb5, and further comprising at least one effector molecule linked to said single domain antibody, for screening for a cancer characterized by cells expressing on their surface at least one globo- series glycan selected from Globo H, Gb3, Gb4, and Gb5, wherein the effector molecule is selected from the group comprising fluorescent molecules, phosphorescent molecules, chemiluminescent molecules, bioluminescent molecules, radio-isotopes, and chromophores. The application further comprises the following embodiments: 1. An antibody or antigen-binding fragment thereof binding a globo-series glycan. 2. The antibody or fragment thereof according to embodiment 1, wherein said antibody binds to a terminal α-L-Fuc-(1→2)-β-D-Gal-(1– moiety of the globo-series glycan. 3. The antibody or fragment thereof according to embodiment 1 or 2, wherein the globo- series glycan is Globo H. 4. The antibody or antigen-binding fragment thereof according to any one of embodiment 1 to 3, wherein the antibody comprises: (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.1, a HCDR2 as set forth in SEQ ID No.2, and a HCDR3 as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No. 4, a LCDR2 region as set forth in SEQ ID No.5, and a LCDR3 region as set forth in SEQ ID No.6. 5. The antibody or antigen-binding fragment thereof according to any one of the previous embodiments, wherein the antibody comprises (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.7, a HCDR2 as set forth in SEQ ID No.8, and a HCDR3 as set forth in SEQ ID No.9, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No. 10, a LCDR2 region as set forth in SEQ ID No.11, and a LCDR3 region as set forth in SEQ ID No.12. 6. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments comprising: a. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively; b. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 54and SEQ ID NO: 55, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;c. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 54and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;d. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 69, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;e. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 71, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;f. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 75, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;g. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 76, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;h. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 61and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;i. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 62and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;j. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 63and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;k. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 64and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;l. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 66and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;m. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;n. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO:59, SEQ ID NO:60 andSEQ ID NO:68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;o. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 98 and SEQ ID NO: 58, respectively;p. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 92, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;q. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;r. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 95, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;s. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 101, respectively;a. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 102, respectively;b. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 103, respectively;c. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 87, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;d. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 88, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;e. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 89, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 95, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;f. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 90, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 95, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;g. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 87, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;h. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 90, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;i. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 88, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively; j. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 101, respectively; 7. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, comprising:a. A heavy chain variable region VH comprisingHFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 13, HFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 14, HFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 15, HFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 16, and A light chain variable region VLcomprising LFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 17, LFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 18, LFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 19, LFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 20,b. A heavy chain variable region VH comprisingHFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 21, HFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 22, HFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 23, HFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 24, and A light chain variable region VLcomprising LFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 25, LFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 26, LFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 27, LFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 28,c. A heavy chain variable region VH comprisingHFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 21, HFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 22, HFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 23, HFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 24, and A light chain variable region VLcomprising LFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 25, LFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 34, LFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 27, LFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 28,d. A heavy chain variable region VH comprisingHFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 21, HFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 14, HFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 39, HFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 24, and A light chain variable region VLcomprising LFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 25, LFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 26, LFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 27, LFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 28,e. A heavy chain variable region VH comprisingHFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 45, HFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 46, HFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 47, HFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 24, and A light chain variable region VLcomprising LFR1 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 25, LFR2 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 26, LFR3 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 27, LFR4 sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 28. 8. The antibody or fragment thereof according to any one of the preceding embodiments, comprising: a. A heavy chain variable region VH comprising HFR1, HFR2, HFR3 and HFR4 of SEQID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 16, respectively and A light chain variable region VLcomprising LFR1, LFR2, LFR3 and LFR4 of SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, and SEQ ID NO: 20, respectively. b. A heavy chain variable region VH comprising HFR1, HFR2, HFR3 and HFR4 of SEQID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23 and SEQ ID NO: 24, respectively and A light chain variable region VLcomprising LFR1, LFR2, LFR3 and HFR4 of SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, and SEQ ID NO: 28, respectively. c. A heavy chain variable region VH comprising HFR1, HFR2, HFR3 and HFR4 of SEQID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, and SEQ ID NO: 24, respectively and A light chain variable region VLcomprising LFR1, LFR2, LFR3 and HFR4 of SEQ ID NO: 25, SEQ ID NO: 34, SEQ ID NO: 27, and SEQ ID NO: 28, respectively. d. A heavy chain variable region VH comprising HFR1, HFR2, HFR3 and HFR4 of SEQID NO: 21, SEQ ID NO: 14, SEQ ID NO: 39, and SEQ ID NO: 24, respectively and A light chain variable region VLcomprising LFR1, LFR2, LFR3 and HFR4 of SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, and SEQ ID NO: 28, respectively. e. A heavy chain variable region VH comprising HFR1, HFR2, HFR3 and HFR4 of SEQID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47, and SEQ ID NO: 24, respectively and A light chain variable region VLcomprising LFR1, LFR2, LFR3 and HFR4 of SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, and SEQ ID NO: 28, respectively. 9. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, comprising: a VHsequence selected from the group consisting of: a. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 106; b. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 108; c. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 109;d. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 110; e. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 111; f. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 113; g. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 117; h. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 118; i. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 128; j. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 129; k. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 130; l. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 131; m. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 132; n. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 133; o. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 134; p. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 135; q. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 136; r. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 138; s. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 140; t. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 141; u. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 142; v. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 143; w. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 144; and x. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 145; and a VLsequence selected from the group consisting of: a. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 146;b. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 150;c. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 152;d. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 154;e. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 155;f. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 156;g. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 158;h. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 159;i. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 160;j. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 161;k. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 162;l. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 163;m. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 164;n. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 165;o. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 166;p. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 167;q. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 169;r. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 170;s. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 172;t. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 173;u. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 174;v. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 175;w. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 176;x. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 177;y. a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 178. 10. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, comprising: a VHsequence selected from the group consisting of: a. a VH sequence having the amino acid sequence of SEQ ID NO: 106;b. a VH sequence having the amino acid sequence of SEQ ID NO: 108;c. a VH sequence having the amino acid sequence of SEQ ID NO: 109;d. a VH sequence having the amino acid sequence of SEQ ID NO: 110;e. a VH sequence having the amino acid sequence of SEQ ID NO: 111;f. a VH sequence having the amino acid sequence of SEQ ID NO: 113;g. a VH sequence having the amino acid sequence of SEQ ID NO: 117;h. a VH sequence having the amino acid sequence of SEQ ID NO: 118;i. a VH sequence having the amino acid sequence of SEQ ID NO: 128;j. a VH sequence having the amino acid sequence of SEQ ID NO: 129;k. a VH sequence having the amino acid sequence of SEQ ID NO: 130;l. a VH sequence having the amino acid sequence of SEQ ID NO: 131;m. a VH sequence having the amino acid sequence of SEQ ID NO: 132;n. a VH sequence having the amino acid sequence of SEQ ID NO: 133;o. a VH sequence having the amino acid sequence of SEQ ID NO: 134;p. a VH sequence having the amino acid sequence of SEQ ID NO: 135;q. a VH sequence having the amino acid sequence of SEQ ID NO: 136;r. a VH sequence having the amino acid sequence of SEQ ID NO: 138;s. a VH sequence having the amino acid sequence of SEQ ID NO: 140;t. a VH sequence having the amino acid sequence of SEQ ID NO: 141;u. a VH sequence having the amino acid sequence of SEQ ID NO: 142;v. a VH sequence having the amino acid sequence of SEQ ID NO: 143;w. a VH sequence having the amino acid sequence of SEQ ID NO: 144; andx. a VH sequence having the amino acid sequence of SEQ ID NO: 145;and a VLsequence selected from the group consisting of: a. a VL sequence having the amino acid sequence of SEQ ID NO: 146;b. a VL sequence having the amino acid sequence of SEQ ID NO: 150;c. a VL sequence having the amino acid sequence of SEQ ID NO: 152;d. a VL sequence having the amino acid sequence of SEQ ID NO: 154;e. a VL sequence having the amino acid sequence of SEQ ID NO: 155;f. a VL sequence having the amino acid sequence of SEQ ID NO: 156;g. a VL sequence having the amino acid sequence of SEQ ID NO: 158;h. a VL sequence having the amino acid sequence of SEQ ID NO: 159;i. a VL sequence having the amino acid sequence of SEQ ID NO: 160;j. a VL sequence having the amino acid sequence of SEQ ID NO: 161;k. a VL sequence having the amino acid sequence of SEQ ID NO: 162;l. a VL sequence having the amino acid sequence of SEQ ID NO: 163;m. a VL sequence having the amino acid sequence of SEQ ID NO: 164;n. a VL sequence having the amino acid sequence of SEQ ID NO: 165;o. a VL sequence having the amino acid sequence of SEQ ID NO: 166;p. a VL sequence having the amino acid sequence of SEQ ID NO: 167;q. a VL sequence having the amino acid sequence of SEQ ID NO: 169;r. a VL sequence having the amino acid sequence of SEQ ID NO: 170;s. a VL sequence having the amino acid sequence of SEQ ID NO: 172;t. a VL sequence having the amino acid sequence of SEQ ID NO: 173;u. a VL sequence having the amino acid sequence of SEQ ID NO: 174;v. a VL sequence having the amino acid sequence of SEQ ID NO: 175;w. a VL sequence having the amino acid sequence of SEQ ID NO: 176;x. a VL sequence having the amino acid sequence of SEQ ID NO: 177; andy. a VL sequence having the amino acid sequence of SEQ ID NO: 178;11. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, comprising:a. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 106 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;b. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 108 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 107;c. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO:109 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;d. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 110 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;e. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 111 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;f. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO:113 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;g. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 117 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;h. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 118 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;i. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 128 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;j. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 129 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;k. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 130 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;l. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 131 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;m. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 132 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;n. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 133 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;o. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 134 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;p. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 135 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;q. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 136 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;r. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 138 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;s. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 140 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;t. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 141 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;u. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 142 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 105;v. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 146;w. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 150;x. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 152;y. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 154;z. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 155;aa. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 156;bb. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 158;cc. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 159;dd. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 160;ee. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 161;ff. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 162;gg. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 163;hh. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 164;ii. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 165;jj. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 166;kk. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 167;ll. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 169;mm. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 170;nn. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 143 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 154;oo. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 144 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 154;pp. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 143 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 172;qq. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 145 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 172;rr. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 143 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 173;ss. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 144 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 173;tt. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 145 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 173;uu. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 174;vv. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 175;ww. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 176;xx. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 177; andyy. a VH sequence having at least 80%, at least 85%, at least 90%, at least 95% or atleast 98% sequence identity with the amino acid sequence of SEQ ID NO: 104 and a VL sequence having at least 80%, at least 85%, at least 90%, at least 95% or at least 98% sequence identity with the amino acid sequence of SEQ ID NO: 178. 12. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, comprising:a. a VH sequence of SEQ ID NO: 106 and a VL sequence of SEQ ID NO: 105;b. a VH sequence of SEQ ID NO: 108 and a VL sequence of SEQ ID NO: 107;c. a VH sequence of SEQ ID NO: 109 and a VL sequence of SEQ ID NO: 105;d. a VH sequence of SEQ ID NO: 110 and a VL sequence of SEQ ID NO: 105;e. a VH sequence of SEQ ID NO: 111 and a VL sequence of SEQ ID NO: 105;f. a VH sequence of SEQ ID NO: 117 and a VL sequence of SEQ ID NO: 105;g. a VH sequence of SEQ ID NO: 118 and a VL sequence of SEQ ID NO: 105;h. a VH sequence of SEQ ID NO: 128 and a VL sequence of SEQ ID NO: 105;i. a VH sequence of SEQ ID NO: 129 and a VL sequence of SEQ ID NO: 105;j. a VH sequence of SEQ ID NO: 130 and a VL sequence of SEQ ID NO: 105;k. a VH sequence of SEQ ID NO: 131 and a VL sequence of SEQ ID NO: 105;l. a VH sequence of SEQ ID NO: 132 and a VL sequence of SEQ ID NO: 105;m. a VH sequence of SEQ ID NO: 133 and a VL sequence of SEQ ID NO: 105;n. a VH sequence of SEQ ID NO: 134 and a VL sequence of SEQ ID NO: 105;o. a VH sequence of SEQ ID NO: 135 and a VL sequence of SEQ ID NO: 105;p. a VH sequence of SEQ ID NO: 136 and a VL sequence of SEQ ID NO: 105;q. a VH sequence of SEQ ID NO: 138 and a VL sequence of SEQ ID NO: 105;r. a VH sequence of SEQ ID NO: 140 and a VL sequence of SEQ ID NO: 105;s. a VH sequence of SEQ ID NO: 141 and a VL sequence of SEQ ID NO: 105;t. a VH sequence of SEQ ID NO: 142 and a VL sequence of SEQ ID NO: 105;u. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 146;v. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 150;w. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 152;x. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 154;y. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 155;z. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 156;aa.a VHsequence of SEQ ID NO: 104 and a VLsequence of SEQ ID NO: 158; bb.a VHsequence of SEQ ID NO: 104 and a VLsequence of SEQ ID NO: 159;cc. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 160;dd.a VHsequence of SEQ ID NO: 104 and a VLsequence of SEQ ID NO: 161; ee.a VHsequence of SEQ ID NO: 104 and a VLsequence of SEQ ID NO: 162;ff. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 163;gg.a VHsequence of SEQ ID NO: 104 and a VLsequence of SEQ ID NO: 164; hh.a VHsequence of SEQ ID NO: 104 and a VLsequence of SEQ ID NO: 165;ii. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 166;jj. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 167;kk. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 169;ll. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 170;mm. a VH sequence of SEQ ID NO: 143 and a VL sequence of SEQ ID NO: 154;nn.a VHsequence of SEQ ID NO: 144 and a VLsequence of SEQ ID NO: 172; oo.a VHsequence of SEQ ID NO: 145 and a VLsequence of SEQ ID NO: 172; pp.a VHsequence of SEQ ID NO: 143 and a VLsequence of SEQ ID NO: 173; qq.a VHsequence of SEQ ID NO: 144 and a VLsequence of SEQ ID NO: 173;rr. a VH sequence of SEQ ID NO: 145 and a VL sequence of SEQ ID NO: 173;ss. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 174;tt. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 175;uu.a VHsequence of SEQ ID NO: 104 and a VLsequence of SEQ ID NO: 176;vv. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 177; orww. a VH sequence of SEQ ID NO: 104 and a VL sequence of SEQ ID NO: 178;13. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, wherein the antibody does not substantially bind to SSEA-5. 14. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, wherein the antibody or antigen-binding fragment thereof has a 20-fold higher affinity to GloboH compared to SEEA-5. 15. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, wherein the antibody does not substantially bind to Gb5. 16. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, wherein the antibody or antigen-binding fragment thereof has a 10-fold higher affinity to GloboH compared to Gb5. 17. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, wherein the antibody exhibits an increased binding to Globo H as compared to antibody VK9 and / or OBI-888. 18. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, wherein the antibody exhibits a KD of 8E-06 or less for GloboH. 19. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, wherein the antibody exhibits a KD of 1E-06 or more for SSEA-5. 20. The antibody or antigen-binding fragment thereof according to any one of the preceding embodiments, wherein the antibody is humanized. 21. The antibody thereof according to any one of the preceding embodiments, wherein the antibody is a monoclonal antibody. 22. The antibody or an antigen-binding fragment thereof according to any one of the previous claims, wherein the antibody, or the antigen-binding fragment thereof, is a multispecific antibody or a multispecific antigen-binding fragment. 23. Antibody drug conjugate comprising the antibody or antigen-binding fragment thereof according to any one of the previous embodiments. 24. Chimeric antigen receptor (CAR) comprising the antigen-binding fragment according to any one of embodiments 1 to 21. 23. Nucleotide sequence encoding the antibody of antigen-binding fragment according to any one of the embodiments 1 to 21 or the CAR according to claim 24. 24. Vector comprising the nucleotide sequence according to embodiment 23. 25. Cell comprising the nucleotide sequence according to claim 23 or the vector according to claim 24. 26. The antibody or antigen-binding fragment thereof according to any one of the embodiments 1 to 22, the Antibody drug conjugate according to claim 23, the CAR according to claim 24, the nucleotide sequence according to claim 23, the vector according to claim 24 or the cell according to claim 24 for use as a medicament. 27. The antibody or antigen-binding fragment thereof according to any one of the embodiments 1 to 22, the Antibody drug conjugate according to claim 23, the CAR according to claim 24, the nucleotide sequence according to claim 23, the vector according to claim 24 or the cell according to claim 24 for use in the treatment of cancer. 28. Diagnostic kit comprising the antibody or antigen-binding fragment thereof according to any one of the embodiments 1 to 22.

[0002] Description of the FiguresFigure 1: Structure of globo-series glycans GloboH, Gb3, Gb4, Gb5, SSEA3, and SSEA4.Figure 2: Glycan Array of day 49 sera (diluted 1:1,000) from 3 chicken (A1, A2, A3) immunized with CRM197-Globo H. From the glycans included in the array, the ones numbered with 1, 2, and 8 (grid on the right) represent GloboH structures.Figure 3: Flow cytometry results of chicken sera at day 35 or 49. The cell lines MCF7 wildtype (MCF7_WT) or GloboH knockout (MCF7_KO) were employed. Control mAb VK9 was diluted from a 10 mg / mL stock. Figure 4 Chromatogram of the eluted AB1cs pAb from GloboH-sepharose matrix by pH gradient from pH 6.8 to 2.5. Fractions F1 to F5 were collected and analyzed individually.Figure 5: Glycan array performed with the purified IgY (diluted 1:1,000) from egg yolks ofchickens A1, A2, and A3. From the glycans included in the array, the ones numbered with 1, 2, and 8 (grid on the right) represent Globo H structures.Figure 6: Cell binding of the AB1cs mAb in comparison to VK9 to MCF7_WT andMCF7_KO cells. Data shown as MFI post subtraction of isotype IgG2a signal. MFI: Median Fluorescence Intensity, n=3. Figure 7: Sensograms of the AB1cs and VK9 against GloboH. (A) Sensograms of the mAb AB1cs at different concentrations (from 10 µM to 0.0001 µM). (B) Sensograms of VK9 at different concentrations (from 10 µM to 0.0001 µM). (C) Affinity (KD) of the AB1cs mAb or VK9. Figure 8: Antibody internalization and surface-removal kinetics of AB1cs mAbs on MCF7 cells. (A) Internalization and (B) Surface removal kinetics of AB1cs, VK9, and Trastuzumab (n=3). (C) Internalization and (D) Surface removal kinetics of the AB1cs mAb, as MMAE- or DXT-ADC, both at a DAR 4 (n=1). All antibody incubations were performed at their respective EC80 concentrations on MCF7_WT cells.Figure 9: Proliferation of cells after mAb treatment for 8 days. No significant differencesare observed between the treatments and the negative control.Figure 10: CDC activity of AB1cs mAb, and VK9. A mouse IgG2a was used as isotypecontrol, while an binding IgM was used as positive control. Data shown as viability (%) relative to cells treated with complement only, n=4.Figure 11: ADCC activation of CD16 NFAT Jurkat cells. Data shown as activation (%)relative to max signal, n=3.Figure 12: ADCP of the AB1cs mAb, VK9, and Trastuzumab, performed on MCF7_WTcells, employing Jurkat-CD32 NFAT-lucia cells.Figure 13: ADCC killing assay of AB1cs mAb and VK9 measured in a MCF7_WT- NK92co-culture assay.Figure 14: Determination of the IC50 of AB1cs mAb coupled to MMAE (ADC) againstMCF7_WT cells. MMAE only was used as reference. n=3.Figure 15: Ab1CS-MMAE ADC cytotoxicity evaluation GloboH-positive spheroids. (A)Cytotoxicity against MCF7_WT cells. (B) Cytotoxicity against B16-GloboH cells. Timepoints span from 2-3 days (timepoint 1), 4-6 days (timepoint 2), and 7-8 days (timepoint 3). Statistical analysis consisted of a Two-way ANOVA, with Bonferroni’s multiple comparisons test, performed on GraphPad Prism. n=3.Figure 16: AB1cs -MMAE and -DXT cytotoxicity evaluation on MCF7_WT (A) or MCF7_KO(B) in 2D setting, and (C) its EC50calculations. (n=2). Figure 17: AB1cs -MMAE and -DXT cytotoxicity evaluation on MCF7_WT (A) or MCF7_KO (B) in 3D setting (n=2).Figure 18: Animal weight (g) of Athymic nude mice were treated. Data are displayed asmeans + / - SEM.Figure 19: Total radiant efficiency [p / s] / [μW / cm²] of blood and organ. Data are displayedas means + / - SEM and given in logarithmic scale. Statistical analysis was performed with unpaired student’s t-test (Group 2 vs.3) and one-way ANOVA with Tukey’s post-test (comparing all groups, in brackets) and displayed if significant.Figure 20: Predicted plasma concentration of the AB1cs mAb in two doses (1 or 7.5 mg / Kg)injected 3 times per week, for 3 weeks in mice.Figure 21: Tumor volume (cm³) in vehicle, and in AB1cs as naked mAb or MMAE ADCagainst MCF7_WT, n=2 or 3.Figure 22: Tumor volume (mm³) in untreated (n=50), vehicle (n=10), and in AB1cs-MMAE(group 5, n=10) for accessing efficacy in early-intervention setting against MCF7_WT.Figure 23: Tumor volume (mm³) in vehicle, Beriglobin (7.5 mg / Kg), and AB1cs- MMAE(n=10) using two doses (7.5 or 1.0 mg / Kg) for accessing efficacy in therapeutic setting.Figure 24: Binding curves of mAbs AB1cs, AB1csh7, and AB1csh7.34, performed by flowcytometry against MCF7_WT and MCF7_KO.Figure 25: Glycan Array of AB1cs against GloboH, Gb5, and SSEA-5. (A) Relativefluorescent intensity (RFI) of the interaction between AB1cs over GloboH. (B) RFI of the interaction between AB1cs over Gb5 or SSEA-5.Figure 26: Sensograms of the AB1csh7.34 against GloboH and SSEA-5. (A) Sensogramsof the AB1csh7.34 mAb against GloboH at different concentrations (from 10 µM to 0.0001 µM). (B) Sensograms of the AB1csh7.34 mAb against SSEA-5 at different concentrations (from 10 µM to 0.0001 µM). (C) Affinity (KD) of the AB1csh7.34 mAb against GloboH or SSEA-5.Figure 27: Binding evaluation of 33 additional variants of humanized Ab1CS to GloboHpositive MCF7 cells.Figure 28: Binding evaluation of 26 additional variants of humanized Ab1CS to GloboHpositive MCF7 cells. Figure 29: Binding curves of mAbs AB1csh7.34, VK9(B13), and OBI-888, performed by flow cytometry against MCF7_WT. The superiority of Ab1CSh7.34 in binding is noticed to be around 5-fold in comparison to VK9(B13), and 10-fold in comparison to OBI-888. Figure 30: Sensograms of the AB1csh7.34, VK9(B13), and OBI-888 against GloboH. (A) Sensograms of the mAb AB1csh7.34. (B) Sensograms of VK9(B13) at different concentrations. (C) Sensograms of OBI-888 at different concentrations. Figure 31: Tumor volume (mm³) in vehicle, Anti-HIV MMAE (7.5 mg / Kg), Ab1CSh7.34 ADC MMAE (7.5 mg / Kg), and SoC for accessing efficacy in NCI-H526 (lung cancer) cells on day 25 after randomization Figure 32: Test of Ab1CSh7.34 as a bispecific T-cell engager. Cell binding properties of the IgG and the bispecific form of Ab1CSh7.34 (BsAb1CSh7.34) against (A) MCF7_WT and (B) MCF7_KO. Figure 33: Use of Ab1CSh7.34 as a T-cell engager, bispecific mAb (BsAB1csh7.34). (A) Levels of TDCC and (B) stimulation of T-cell proliferation (lower panel) of the bispecific mAbs over MCF7_WT or MCF7_KO. The following examples are included to demonstrate preferred embodiments of the invention. It should be appreciated by those of skill in the art that the techniques disclosed in the examples which follow represent techniques discovered by the inventor to function well in the practice of the invention, and thus can be considered to constitute preferred modes for its practice. However, those of skill in the art should, in light of the present disclosure, appreciate that many changes can be made in the specific embodiments which are disclosed and still obtain a like or similar result without departing from the scope of the invention. Further modifications and alternative embodiments of various aspects of the invention will be apparent to those skilled in the art in view of this description. Accordingly, this description is to be construed as illustrative only and is for the purpose of teaching those skilled in the art the general manner of carrying out the invention. It is to be understood that the forms of the invention shown and described herein are to be taken as examples of embodiments. Elements and materials may be substituted for those illustrated and described herein, parts and processes may be reversed, and certain features of the invention may be utilized independently, all as would be apparent to one skilled in the art after having the benefit of this description of the invention. Changes may be made in the elements described herein without departing from the scope of the invention as described in the following claims. EXAMPLES Methods: Chicken immunization and finding of anti-Globo H antibodies Globo H was coupled to the protein carrier CRM197via reductive amination using sodium cyanoborohydride as reductive agent. Mass spectrometry was used to check the loading of the glycan to the protein, which in this case was around 10:1 (glycan-protein molar ratio). This conjugate was used as antigen to immunize chicken (species Gallus gallus). Briefly, one injection of 40 µg of Globo H-CRM197with AddaVax (InvivoGen) as adjuvant was given to each animal every 2 weeks until a total of 5 injections. On day 52 splenocytes were isolated from animals with an antigen-specific immune response based on these techniques, and total RNA was isolated using TRIzol reagent. The mRNA was transcribed into cDNA and VH and VL sequences were amplified by PCR using commonly described oligonucleotides for the construction of an antibody gene library using a phagemid. The library was subjected to next generation sequencing (NGS) to analyze VH and VL sequences. Parallel to the immunization, egg yolks of the same animal were collected and the IgY fraction was isolated (Polson, 1990). The IgY fraction was subsequently subjected to affinity purification on NHS-Sepharose to which Globo H that carries a primary amino group at its reducing end was coupled. Bound antibodies were eluted under acidic or chaotropic conditions. Purified fractions containing anti-Globo H antibodies were subjected to incomplete proteolysis by different enzymes and the resulting peptide mixture was analyzed by mass spectrometry. Obtained peptide sequences supplemented by the information from the NGS sequencing were assembled to yield VH and VL sequences of the isolated antibodies on the protein level. One antibody was prominently present in the preparation having VH region of SEQ ID NO.106 and VL region of SEQ ID NO.107. Initial antibody sequence optimization, antibody expression, and purification Based on the sequence obtained in the previous section, an improvement was performed by replacing a free cysteine to a serine residue in the VH-CDR3 to improve biochemical characteristics in later steps, resulting in the modified VH region of SEQ ID NO: 108. This modification resulted in the CS variant of SEQ ID NO. 106, which avoids covalent dimerization or oxidation. Subsequently, expression of the chicken variable domains fused to murine IgG2a constant regions was conducted according to standard procedures in CHO cells. The mAbs were purified from culture supernatant by protein A-affinity, followed by size exclusion chromatography (SEC). Specificity assessment in glycan array To assess specificity of the antibody-containing samples, relevant carbohydrate structures among them that of Globo H were covalently coupled to glass slides in an array format using standard epoxy-based chemistry followed by respective quenching step to inactivate still functional epoxy groups. For the immunostaining, the array was incubated with the samples that was adjusted to 1 µg / mL anti-Globo H mAb in PBS containing 3 % (w / v) BSA (PBS- BSA) and incubated 1 h at room temperature. After washing with PBS-BSA detection of bound anti-Globo H Abs was performed by incubation with goat-anti Mouse IgG conjugated to AlexaFluor627 fluorophore (Thermo Scientific) diluted 1:500 in PBS-BSA for 1 h at room temperature. After a final washing step, slides were scanned using an Axon GenePix scanner with excitation / emission wavelength of 635 nm / 660 nm and analysis of the obtained signals using GenePix Pro7. Affinity determination Affinity values for the purified mAbs were obtained via surface plasmon resonance (SPR, Biacore T200; Cytiva). A CM7 chip was used to immobilize Globo H or SSEA-5 with a primary an amino group at its reducing end according to manufacturer’s instructions (Cytiva). Measurements were performed using varying concentrations all diluted in PBS containing 0.05 % (v / v) polysorbate 20 (PBS-T), which was also the assay buffer. Sample contact time was 60 s, while dissociation time was 900 s, all performed with 30 µL / min flow rate. All measurements were performed at 25 °C. Analysis was done with Biacore T200 Evaluation Software (Cytiva) using heterogeneous ligand curve fit. Binding assay in flow cytometry To evaluate the binding properties on cells expressing Globo H, breast cancer cell line MCF7 was used. In addition, MCF7 was genetically engineered to knock out the gene for the enzyme FUT1 and β3GalT5 gRNAs targeting to eliminate Globo H synthesis and serve as negative reference for the experiments (MCF7_KO). CRISPOR software was used for gRNA design. Three gRNA pairs were designed for each gene. Cells not expressing Globo H were selected and expanded. In addition, B16 (mouse melanoma cells, Merck), which are Globo H-negative, were transfected with the genes A4GALT, B3GALNT1, and FUT1 to reconstitute the biosynthesis of Globo H (B16_GH). These cells were transfected with plasmids encoding the genes of interest and sleeping beauty transposase mRNA to enhance stable expression of the introduced genes using Lipofecatamine3000 (Invitrogen) and cells expressing Globo H were selected and expanded. The above-described cell lines were incubated with the anti-Globo H mAb or an isotype control diluted in different concentrations with 2 % (v / v) FBS in PBS, and incubated for 30 min on ice. After washing, the cells were incubated with a secondary antibody labelled with CF488. In parallel, cells were also stained for viability with eFlour780 (ThermoFisher). After a final washing step, cells were subjected to analysis by flow cytometry. Cellular assays (internalization, CDC, ADCC, ADCP, cell activation) Internalization assay: MCF-7 cells were harvested and incubated with the anti-Globo H mAb or Trastuzumab as control at their respective EC80concentrations (1.32 μg / mL and 0.986 μg / mL, respectively) in 10% FBS-containing medium, for 5 min on ice. Following this initial incubation, cells were incubated at 37°C for various timepoints and bound antibodies were stripped off the cell surface via an acidic wash with PBS at 2.5 pH, which was followed by viability staining (eFlour780), fixation with 4% (v / v) paraformaldehyde (PFA), permeabilization with 0.05% (v / v) Triton X-100, and secondary antibody with CF-488. Stripping efficiency (ε) was calculated from the timepoint 0 of unpermeabilized samples, and surface fluorescence was then calculated by subtracting the mean-fluorescence intensity (MFI) values of the stripped samples from the non-stripped ones, divided by ε. Total fluorescence was the raw MFI values from non-stripped samples at each timepoint and internal fluorescence was finally calculated by subtracting surface fluorescence from the total fluorescence. Proliferation: MCF7 WT cells were seeded in 96-well plates and cultured overnight. The following day, medium was replaced to starving medium including mAb treatment. Cells were cultured for 8 days, while starving medium and antibody was refreshed every 3 days. The Click-iT EdU (Invitrogen) assay was performed as described in product sheet. For flow cytometry analysis, cells were stained with eFlour780 (Invitrogen #17344361). CellTiterGlo Assay (Promega) according to manufacturer instructions. Complement-dependent cytotoxicity (CDC): MCF7_WT cells were harvested and transferred into a V-shaped 96-Well plate. Cells were washed with culture medium and cells were incubated with culture medium containing 10% (v / v) baby rabbit complement (BioRad) and dilutions of the anti-Globo H mAb for 4 h at 37 °C. Afterwards, viability was measured by CellTiterGlo Assay (Promega) according to manufacturer’s instructions. ADCC / ADCP activation assays: MCF7_WT cells were incubated with different mAb dilutions for 30 min on ice. Jurkat NFAT CD16 (InvivoGen) effector cells were added in a 1:10 – 1:15 (T:E) ratio, whereas Jurkat NFAT CD32 (InvivoGen) cells were added at a 1:2 target / effector ratio. Co-cultures were incubated for 5h (CD32) or 6 h (CD16), at 37 °C. Activation was measured via QuantiLuc (InvivoGen) according to the manufacturer’s protocol. ADCC killing assay: Target cells were incubated with mAb dilutions for 30 min on ice. NK92- CD16 effector cells were added in a 1:2 (T:E) ratio. Co-cultures were incubated for 6 h at 37°C. Viability was measured via QuantiLuc (InvivoGen) according to manufacturer’s protocol. Assessing Globo H distribution in immunohistochemistry (IHC) Formalin-fixed, paraffin-embedded (FFPE): Normal human FFPE tissue FDA microtissue array (MTA) panels consisting of 132 spots (44 normal tissue types represented by 3 donors per tissue) were stained with 1 µg / mL of anti-Globo H mAb. Staining evaluation was performed according to the following procedure: 1) Classification of staining into positive and negative spots; 2) positive spots were further analyzed according to cell type, staining pattern (nuclear, cytoplasmic, and membranous), as well as staining intensity of the respective pattern; 3) Membrane staining was analyzed according to apical, basolateral, or whole membrane localization; 4) H-scoring of membrane staining. Fresh-frozen (FF) healthy tissues: Normal human tissue FDA MTA panels (BioChain) consisting of 90 spots (30 normal tissue types represented by 3 donors per tissue) were stained with 1 µg / mL of anti-Globo H mAb. Staining evaluation was according to the following procedure: 1) Classification of staining into positive and negative spots; 2) positive spots were further analyzed according to cell type, staining pattern (nuclear, cytoplasmic and membranous), as well as staining intensity of the respective pattern; 3) Membrane staining was analyzed according to apical, basolateral, or whole membrane localization; 4) H-scoring of membrane staining. Cancer tissues: Antibody-drug conjugate (ADC) production The anti-Globo H mAb was produced in the same manner as before and used for the conjugation of the drug monomethyl auristatin E (MMAE, Broadpharm) using Lys-Val-Cit- PABC linker (Merck). AB1cs mAb and the MMAE were mixed to a molar equivalent of 10 (MMAE:mAb) and stirred for 3 h. A NAP-25 column (Cytiva) was used to eliminate residual MMAE. The products were analyzed by MALDI-TOF mass spectrometry, where the targeted drug-antibody ratio (DAR) of ~4 was confirmed. After MS, the sample was changed to PBS using Amicon columns and stored. In vitro cytotoxicity of ADC in 2D cultures The cells MCF7_WT, HCC1428, and NCI-H526 were harvested during the logarithmic growth period and counted using Vi-cell cell counter. Seeding density per well were determined and adjusted to 90 μL of cell suspensions per well in a 96-well plate. An additional plate was set up for day 0 reading (T0) and the other plates were read at the end point of the assay. Plates were incubated overnight in a humidified incubator at 37 °C with 5% CO2. CellTiter-Glo® Reagent was added at 50µL / well. The plate was shaken for 10 min on an orbital shaker and incubated at room temperature for another 10 min. Luminescence was recorded using TECAN Plate Reader In vitro cytotoxicity in 2D and 3D cultures For assays in 2D cultures, MCF7_WT cells were seeded in 96-well tissue culture plates and cultured overnight. The following day, medium was replaced by medium containing the anti- Globo H ADC coupled to MMAE or naked, and compared to vehicle only. Cells were cultured for 7 days, while medium and antibody were refreshed after 3 days. For spheroid (3D) cytotoxicity, 8,000 MCF7_WT cells were seeded per well on 96-well low attachment plates followed by embedding in medium containing matrigel as of 1:8 of the volume. The cytotoxicity assay was repeated as described above. CellTiterGlo analysis(Promega) was performed according to manufacturer’s instructions. In vivo distribution and ex vivo imaging in mice Anti-Globo H mAb and an isotype control (BioLegend) were labelled with CF750 via amino coupling (Merck) following manufacturer’s instructions. In total, three female, athymic nude (Crl:NU(NCr)-Foxn1nu), 6-8 weeks, mice per antibody received 200 µg of labelled mAb intravenously. In vivo fluorescence measurement for the biodistribution of the CF750- labeled antibodies was performed in all animals after 30 min, 10.5 h and 24 h after treatment. For each measuring time point, a vehicle-treated mouse was used as reference for measurement. The fluorescence intensity of CF750 was monitored using an IVIS® Lumina III imaging system (Perkin Elmer) with a CCD-camera and an imaging sequence optimized for spectral unmixing. After 24 h, selected organs (both kidneys, spleen, lung, stomach, intestine divided into small intestine, ileum, caecum, and colon, heart, and liver) were isolated from terminated animals and their fluorescence was measured. Pharmacokinetics (PK) in mice Pharmacokinetic data on the lead antibody Ab1CS were generated by single intravenous injection of 10 mg / kg in female, C57BL / 6, 6-8 weeks-old mice. Anti-Globo H mAbs were tested either as free or as ADC variant, with human IgG1 constant regions. Serum samples were collected 15 min, 4 h, 24 h, 48 h, 168 h, and 336 h after injection. For quantification of the anti-Globo H mAb in sera, both indirect and capture ELISA were performed. Indirect ELISA was set up by coating ELISA plates with CRM197-Globo H, 100 ng / well, 50 μL / well, in 100 mM sodium carbonate buffer pH 9.6, 4°C overnight. Dilutions of the respective mAbs were made from 1,000-0.00316 ng / mL (12x √10-fold dilutions) for recording a standard curve. Mouse sera were diluted from 1:100-1:100,000 (7x √10-fold dilutions) in PBS-T. All samples were incubated on the coated ELISA plate for 1 h, RT. After washing the wells with PBS-T, secondary antibody anti-human HRP-conjugated pAb diluted according to the recommendation of the manufacturer was subsequently incubated for 1h, RT. After thorough washing, reaction was developed with TMB solution, stopped with 0.5 M HCl, and absorption was read at 450 nm using 620 nm as reference wavelength. For the capture ELISA, a commercial Human IgG1 ELISA kit (Invitrogen, BMS2092) was used according to manufacturer’s instructions. Quantification was used to calculate the PK of the tested antibodies. The resulting data was used to feed a 1- or 2-compartment model for determining different PK parameters, including half-life and clearance rate. In vivo investigation of safety and efficacy of antibodies targeting Globo H in mice Early-intervention treatment in syngeneic tumor model: A PBS suspension of 100 µL containing 2x105B16_GH cells were subcutaneously injected in mice (C57Bl6 strain, female, 6-8 weeks). Mice were treated on day 1, 8, and 23 after cell injection (T=0d) with 10 mg / kg of anti-Globo H MMAE ADC or with 25mg / kg of anti-Globo H naked mAb. A vehicle control group treated with PBS only included into that study. Body weight and tumor size was checked 3 times per week. Mice were terminated when tumors reached a size of 1.5 cm3. Efficacy was determined as percentage of tumor growth inhibition (%TGI) in comparison to the vehicle group. Early-intervention treatment in human breast cancer CDX model: On day -3, all mice (NMRI- Foxn1nu) strain, female, 6-8 weeks) received one 17ß-estradiol pellet (1.7 mg / pellet, 60- day-release, Innovative Research of America) by subcutaneous implantation. On day 0, MCF7_WT cells (5x106cells in 50 μL PBS) were implanted into the left mammary fat pad of each mouse. Two doses of anti-Globo H mAb-MMAE ADC were injected intravenously at 7.5 mg / kg on days 1 and 2. Animals with no treatment were used as control. Animal weights were determined three times per week, and tumor growth was assessed by calipering two times per week. Efficacy was determined as the percentage of tumor growth inhibition (%TGI) in comparison to the tumor-implanted, non-treated group until 59 days after tumor cell implantation. Therapeutic treatment in human breast cancer CDX model: On day -3, mice (NMRI- Foxn1nu) strain, female, 6-8 weeks) received one 17ß-estradiol pellet (1.7 mg / pellet, 60- day-release, Innovative Research of America) by subcutaneous implantation. On day 0, MCF7_WT cells (5x106cells in 50 μl PBS) were implanted into the left mammary fat pad of each mouse. On Day 39, when a mean tumor volume of 136.6 mm3was reached, tumor- bearing animals were randomized into 4 groups: 1) vehicle, 2) Beriglobin® (CSL Behring) MMAE ADC at 7.5 mg / kg (negative control), 3) anti-Globo H mAb-MMAE ADC at 7.5 mg / kg, 4) anti-Globo H mAb-MMAE ADC at 1 mg / kg. Antibody preparations were respectively injected intravenously on days 39, 42, 44, 46, 49, 51, and 53. Animals receiving vehicle served as control. Animal weights were determined three times per week, and tumor growth was monitored by calipering two times per week. Observation was ended on day 59, and efficacy was determined as the percentage of tumor growth inhibition (%TGI) in comparison to the tumor-implanted, vehicle-treated group. In vivo efficacy with NCI-H526 cells Mice (Balb / c nude strain, female, 4-8 weeks) received NCI-H526 cells (5x106cells in 100 μL PBS) were implanted subcutaneously. When a mean tumor volume of 80-120 mm3was reached, tumor-bearing animals were randomized into 4 groups: 1) vehicle, 2) Isotype AntiHIV-MMAE at 7.5 mg / kg (negative control), 3) Ab1CSh7.34-MMAE at 7.5 mg / kg, 4) Standard of Care (SoC), which is Carboplatin 30 mg / Kg (on days 1 and 11) plus Etoposide 1.5 mg / Kg (on days 1 until 5, and 11 until 15). Antibody preparations were respectively injected intravenously on days 1, 5, 8, 12, 15, 19, and 22. Animals receiving vehicle served as control. Animal weights were determined three times per week, and tumor growth was monitored by calipering two times per week. Observation was ended on day 25 after randomization, and efficacy was determined as the percentage of tumor growth inhibition (treatment over control, T / C) in comparison to the tumor-implanted, vehicle-treated group. Humanization and engineering of the anti-Globo H mAb The anti-Globo H mAb was humanized via CDR grafting resulting in 4 sequences for VH and 4 sequences for VL. 14 mAbs derived from combining these VH and VL sequences were tested in in flow cytometry binding to Globo H-positive cells, leading to the selection of one combination of VH and VL comprising SEQ ID NO.104 and SEQ ID NO.105. From this humanized sequence, several sequences with amino acid changes in the FR regions were generated. This mAb was produced, purified, and tested in in flow cytometry binding as previously described. In addition to the variants with changes in FR regions, several other variants with amino acid changes on the CDR were generated and tested either in flow cytometry or in glycan array for their activity against GloboH. Production and testing of a T-cell engager, bispecific, humanized anti-GloboH mAb The selected humanized mAb Ab1CSh7.34 was used to produce a version of a bispecific antibody comprising 2 binding arms against GloboH, and 1 binding arm against human CD3 (molecule was named BsAB1csh7.34). Following known techniques of mAb engineering, the different chains were paired with knob-into-hole (KIH) and CrossMab technologies. This mAb was produced in the same manner as before and analyzed by mass spectrometry. Bispecifics with only Ab1CSh7.34 (BsAB ctrl2) or anti-CD3 (BsAB ctrl3) activity were used as negative controls. The functional test of the bispecific anti-GloboH mAb was performed by seeding 103of either MCF7_WT or MCF7_KO cells in each well of 96-well plates. Human peripheral blood mononuclear cells (PBMC) were labelled with carboxyfluorescein succinimidyl ester (CFSE) and added at different amounts to the seeded cells representing 1:0.5, 1:1, 1:2, and 1:4 PBMC:target ratio. Then, different concentrations of the tested mAb were added (0.001, 0.01, 0.1 µg / mL) and incubated for 4 days. The readout of MCF7 viability was done with cell- titer glow, while the proliferation of PBMCs was assessed by flow cytometry. As controls, mAbs in the same format binding only to human CD3 (monovalent) or only to GloboH (bivalent) were used. Results: Immunization of chicken with GloboH elicits specific AB1cs antibodies that bind to cancer cells Chicken immunized with the CRM197-Globo H showed specific antibody response against the glycan target as verified in glycan array (Figure 2). The raised AB1cs antibodies were also specifically recognizing GloboH-positive human cancer cells (i.e., MCF7) analyzed by flow cytometry (Figure 3). Eggs from chicken A1 were harvested and the yolk was used for the preparation of the IgY fraction. This preparation was purified using a matrix containing GloboH (Figure 4), leading to AB1cs polyclonal antibodies (pAb), which were in glycan array as specific as the parental serum (Figure 5). Sequence-improved, recombinantly expressed, and purified AB1cs mAb show high- affinity while maintaining specificity and cancer cell recognition The anti-Globo H pAbs obtained by Globo H chromatography from the IgY fraction were subjected to MS analysis for the pAb sequence identification. These amino acid sequences were supported by mRNA sequencing of the chicken’s splenocytes, leading to a dominant antibody sequence in the used preparation comprising SEQ ID NO.106 and SEQ ID NO. 107. The VH sequence was improved by a single amino acid change (C->S mutation). and inserted in a vector, e.g., pcDNA3.4, for the production of IgG in CHO cells. In flow cytometry, this mAb (herein after called “AB1cs”) shows a strong binding to MCF7 WT cells, which is superior to VK9 (Figure 6). Affinity measurements were performed using Biacore T200 (Cytiva). As to the recognition of Globo H, AB1cs (Figure 7A) shows a slow dissociation (KOff) in contrast to VK9 (Figure 7B) which dissociates almost instantly, indicating remarkably lower affinity. The calculated affinity of AB1cs is at least 20-fold higher than that of VK9 (Figure 7C). As to the specificity, AB1cs was tested against a panel of carbohydrate structures in glycan array. Besides the expected binding to GloboH (Figure 25A), the described antibody is highly specific and shows no relevant cross-reactivity to structures like Gb5 and SSEA-5 (Figure 25B). High specificity to GloboH was also confirmed in SPR (Figure 26A and 26B), where AB1cs showed more than 20-fold more affinity to GloboH than to SSEA-5 (Figure 26C), and flow cytometry, where it shows no relevant binding to the Gb5-positive MCF7_KO (Figure 6). In accordance to these experiments, crystal structure data indicated that the antibody recognizes the non-reducing end of GloboH, specifically targeting the two distal glycans (Fucα1→2Gal). In this manner, despite recognizing an extremely small epitope, as expected for anti-TACA mAbs, AB1cs shows remarkable specificity to GloboH when compared to other structures containing its epitope. AB1cs mAb show internalization and immune activation that are compatible with therapeutic applications Internalization: the AB1cs mAb presented a faster internalization rate (observed by the shorter Int50 and SurfDec50) as compared to VK9 and Trastuzumab (Figure 8A and 8B). Trastuzumab was very faintly internalized by MCF-7 cells, with 50% of mAbs internalized from the cell surface after 30.73 hours (Figure 8B). Internalization rates of the AB1cs ADC with MMAE or Deruxtecan (DXT), both at a DAR4 show comparable internalization rates (Figure 8C and 8D). Proliferation: no significant difference in cell proliferation was observed in treated groups compared to untreated MCF7_WT cells (Figure 9). Complement-dependent cytotoxicity (CDC): A murine IgG2a was included as an isotype control. A concentration dependent CDC was observed with the IgM control indicating feasibility of the assay. However, no CDC activity on MCF7_WT was observed for the AB1cs or VK9 (Figure 10). Antibody-dependent cellular cytotoxicity and phagocytosis (ADCC / ADCP) activation assays: as to the ADCC, AB1cs show a ~2 fold higher activation of effector cells in comparison to VK9 (Figure 11). Regarding the ADCP, incubation with AB1cs mAb has led to increased CD32 / NFAT activation when compared to VK9. Trastuzumab presented a negligible effect on this assay (Figure 12). ADCC killing assay: AB1cs mAb and VK9 induce a comparable level of ADCC at high concentrations. Nevertheless, our AB1cs mAb induced a more ADCC at lower concentrations. Both mAbs induce more ADCC than Trastuzumab, whereas mouse IgG2a isotype control does not induce ADCC (Figure 13). Immunohistochemistry (IHC) in FFPE tissues for assessing GloboH distribution An FDA panel containing normal human tissues was stained with AB1cs mAb and evaluated by an external pathologist (Table 1 and 2). No nuclear staining was observed; cytoplasmic staining of 19 different tissues from 35 donor is regarded as irrelevant as it is not accessible by the mAb; membranous staining of 11 tissues from 18 donors was observed; 6 different tissues of 9 donors exhibit a staining of the apical membrane that is not accessible by the antibody; 2 tissues (uterus endometrial tissue, and fallopian tube) of 2 different donors exhibit a staining of small lesions in brush border or of the basolateral membrane with very low intensity, as indicated by H-scores of 2 and 3, respectively; 3 different tissues (esophagus, parotid gland and tonsil) of 7 donors exhibit a staining of the entire membrane with H-scores >100. Table 1: Cytoplasmic staining of the AB1cs mAb 1-25% totalDonor 25-50% total Donor >50% totalDonor cytoplasm stained cytoplasm cytoplasm stained stained Breast 2 Breast 1 Stomach 2,3Cecum (colon) 2 Cecum (colon) 1 Ileum 2 (goblet)(goblet) Ascending colon 2 Stomach 1 Jejunum 1Descending colon 1 Jejunum 2 Lung incl.3 (goblet) bronchioles Esophagus 1,2 Ileum 1 Pancreas 2Fallopian tube 1,3 Parotid gland 1,2Ileum 3 Uterus (cervix) 1,2,3(goblet) Kidney 3Liver (right lobe) 2Pancreas 1,3Pituitary gland 3Tonsil 1,2,3Ureter 3Uterus 1 (endometrial tissue) Table 2: Membrane staining, localization, and respective H-score of the AB1cs mAb. Tissue Donor Localization H-scoreBreast 1 apical 30Breast 2 apical 15Stomach 1 apical 45Stomach 2 apical 90Stomach 3 apical 60Jejunum 1 apical 270Pancreas 3 apical 30Pituitary gland 3 apical 1,5Cervix 1 apical 140Uterus endometrial1 basolateral 3tissue Fallopian tube 3 small lesions in brush2 border Esophagus 1 whole membrane 140Esophagus 2 whole membrane 120Parotid gland 1 whole membrane 225Parotid gland 2 whole membrane 220Tonsil 1 whole membrane 200Tonsil 2 whole membrane 170Tonsil 3 whole membrane 160Immunohistochemistry (IHC) in FF tissues for assessing GloboH distribution An FDA panel containing normal human tissues was stained with AB1cs mAb and evaluated by an external pathologist. In total, 10 different tissues (breast, brain pituitary, esophagus, fallopian tube, lung, pancreas, skin, stomach, thymus and ureter) of 20 donors exhibit a staining with H-scores >100: 6 donors from 4 different tissues (breast, brain pituitary, fallopian tube and lung) exhibit a staining of the apical membrane that is not accessible by the antibody under physiologic or in situ conditions; 8 donors from 4 different tissues (pancreas, skin, stomach and ureter) show a basolateral staining, being the staining of the pancreas restricted to acinar cells, skin and stomach had stained glands, whereas in ureter, urothelial cells were stained; 6 donors from 4 different tissues (breast, esophagus, thymus and ureter) show a staining of the whole membrane, being that in most tissues epithelial cells are recognized. The AB1cs mAb binds mostly to individual cell types within tissues, and the evaluation did not raise any major concern. AB1cs mAb is effective as ADC in vitro Results demonstrate an IC50 of 0.35 µg / mL (logIC50 of -0.45) for the AB1cs mAb coupled to MMAE, and 12.02 µg / mL (logIC50 of 1.08) for MMAE alone (see Figure 14). The cytotoxicity of the AB1cs-MMAE on MCF7_WT (Figure 15A) and B16-GH (Figure 15B) induces cell killing more efficiently than the equivalent dosage of MMAE in both cellular models. An additional toxophore, the Deruxtican (DXT), was tested alongside MMAE against MCF7_WT in both 2D (Figure 16A) and 3D settings (Figures 17A and 17C). Both models showed an increased cytotoxicity of the Ab1CS-MMAE compared to Ab1CS-DXT in both tested DAR, i.e., 4 and 10. This effect is likely due the higher specific toxicity of MMAE. The cytotoxic effect of Ab1CS-MMAE on MCF7_KO was also higher in both assays (Figures 16B and 16C; 17B and 17C), but significantly lower than those against the MCF7_WT. AB1cs mAb is well-tolerated even though it has off-targeting effect in gastrointestinal tract of mice After a single injection and imaging of the AB1cs mAb in mice, it was observed that no mice had significant weight loss along the experiment (Figure 18). Despite no signals of toxicity were observed as per analysis of weight loss, accumulation of the AB1cs mAb in stomach, small intestine, ileum, and colon were noted to be higher than the accumulation of the mouse IgG2a used as isotype control (Figure 19). PK of the AB1cs mAb and ADC is compatible with cancer therapy applications although clearance from bloodstream is higher than usual The quantification of the AB1cs mAb and ADC MMAE from the sera of mice allowed determining the PK parameters of the antibody. The half-life of the AB1cs (t½ >150 h) antibodies showed to be comparable to the clinically approved molecule Trastuzumab (Table 3). On the other hand, the clearance from bloodstream was around 10-fold away from the expected values. Nevertheless, the PK behaviour of the AB1cs antibodies showed to be compatible with therapeutic applications as dosing schemes can provide amounts of molecule that are potentially effective (Figure 20). Table 3. PK parameters of the AB1cs mAb and ADC compared to Trastuzumab. mAb Half-life (h) Clearance (mL / h / Kg)AB1cs mAb 175 2.59AB1cs ADC MMAE 167 2.86Trastuzumab 119 0.23AB1cs mAb and ADC show efficacy in early-intervention treatment using a syngeneic tumor model with GloboH-positive B16 cells in mice Tumors of the vehicle group showed a continuous growth until day 29. At day 29, animals of this group had to be killed due to animal welfare regulations as the tumor reached a volume of 1.5 cm3. Mice from both early-treatment groups showed a significant delay in tumor growth compared to the vehicle. Mice treated with AB1cs mAb developed a tumor around d22 (in three out of five mice). The ADC treated group showed first sights of tumor growth at day 27 (in two out of five mice). At day 34 (end of the study), two mice in the ADC group and one mouse in the naked mAb treatment group, were still tumor-free. Overall, the results indicate efficacy in treatment of B16 Globo-H tumors with the naked AB1cs or as ADC in an early-intervention setting (Figure 21). AB1cs ADC show efficacy in early-intervention and therapeutic setting using a human breast tumor model with MCF7 WT cells in mice Mice were treated at day 1 and 2 after tumor cell injection. This early-intervention treatment leads to complete regression of tumor in all mice, which stayed tumor-free until the end of the study, i.e. day 57 (Figure 22). As to the therapeutic treatment, both doses of the AB1cs ADC MMAE were effective compared to the vehicle group. When using Beriglobin as reference, only the dose of 7.5 mg / Kg showed efficacy, which was around 85% of tumor growth inhibition (TGI) (Figure 23, Table 4). When performing the RECIST classification of the tumor-bearing mice, it was possible to observe that treatment with AB1cs ADC MMAE at 7.5 mg / Kg resulted in a higher number of mice with complete recovery (CR) of the induced tumor, as they were tumor-free by the end of the experiment. Table 4. RECIST analysis of the vehicle, Beriglobin, and AB1cs ADC MMAE groups. TGI RECIST*Vehicle -- 7 / 2 / 0 / 0Beriglobin-MMAE 7.5 mg / kg 86.3% 0 / 1 / 7 / 0AB1cs-MMAE 7.5 mg / kg 97.9% 0 / 0 / 4 / 5AB1cs-MMAE 1 mg / kg 85.0% 0 / 2 / 7 / 1* PD / SD / PR / CR. PD, progressive disease. SD, stable disease. PR, partial recovery. CD, complete recovery. A humanized, engineered AB1cs mAb keeps its binding activity against GloboH- positive cancer cells The AB1cs mAb used in the efficacy study was humanized, and variants of it were tested in binding. The combination of SEQ ID NO.104 and SEQ ID NO.105 (AB1csh7), SEQ ID NO 109 and SEQ ID NO.105 (Ab1CSh3), SEQ ID NO.110 and SEQ ID NO.105 (Ab1CSh15) showed surprisingly good results. Ab1CSh7was chosen for further engineering. Using SEQ ID NO.104 and SEQ ID NO.105 as basis, many sequence modifications were made and tested. Among them, the one comprising SEQ ID NO.10 was showing binding properties that were comparable to the original AB1cs mAb (Figure 24, Table 5). Table 5. EC50 and max MFI of Ab1CS-hIgG1, Ab1CSh7, and Ab1CSh7.34. mAb EC50 (µg / mL) Max signal (MFI) Max signal / noise*AB1cs 1.22 49150 108.2AB1csh7 3.02 36766 299.0AB1csh7.34 0.94 43208 250.2* Signal / noise refers to the signal ratio of the GloboH-positive cell line (MCF7_WT) divided by the GloboH-negative cell line (MCF7_KO). Other sequences generated as variants were tested for their binding in comparison to the original AB1cs mAb (Table 6) and tested for maxMFI and signal-to-noise. Based on the maxMFI and S / N results functional antibodies were grouped by their functional performance (“*” referring to functional antibodies, “**” referring to antibodies with improved functionality and “***” referring to “particular improved functionality”.) Table 6. MaxMFI and signal-to-noise data for basis construct AB1CS and variants.

[0003] AB Variant Mutation Location CDR1-CDR2 CDR3 CDR1 CDR2 CDR3-Ranking Max MFI S / NVH -VH -VH -VL -VL VLAb1CS_VH C108S VH- 53 54 68 56 57 58 Reference 62105 96,7CDR3 9 Ab1CSh7mutD104A VH- 53 60 69 56 57 58 *** 55582 97,618 CDR3 6 Ab1CSh7mutD104T VH- 53 60 70 56 57 58 Non-functional 22 3,9617 CDR3 Ab1CSh7mutD104S VH- 53 60 71 56 57 58 ** 32675 94,116 CDR3 Ab1CSh7mutD104L VH- 53 60 72 56 57 58 Non-functional 151 19,215 CDR3 2 Ab1CSh7mutD104Y VH- 53 60 73 56 57 58 Non-functional -29 0,2114 CDR3 Ab1CSh7mutD104I VH- 53 60 74 56 57 58 Non-functional 26 3,4713 CDR3 Ab1CSh7mutL103A VH- 53 60 75 56 57 58 ** 31448 95,212 CDR3 5 Ab1CSh7mutL103Y VH- 53 60 76 56 57 58 * 4802 79,511 CDR3 9 Ab1CSh7mutG102A VH- 53 60 77 56 57 58 Non-functional -7 1,3710 CDR3 Ab1CSh7mutG102E VH- 53 60 78 56 57 58 Non-functional -16 19 CDR3

[0004] Ab1CSh7mutG102N VH- 53 60 79 56 57 58 Non-functional -4 0,958 CDR3 Ab1CSh7mutG102S VH- 53 60 80 56 57 58 Non-functional -9 1,987 CDR3 Ab1CSh7mutG102D VH- 53 60 81 56 57 58 Non-functional -19 1,496 CDR3 Ab1CSh7mutG101A VH- 53 60 82 56 57 58 Non-functional 740 32,75 CDR3 9 Ab1CSh7mutG101E VH- 53 60 83 56 57 58 Non-functional 20 1,514 CDR3 Ab1CSh7mutG101N VH- 53 60 84 56 57 58 Non-functional 106 21,23 CDR3 2 Ab1CSh7mutG101S VH- 53 60 85 56 57 58 Non-functional 149 8,742 CDR3 Ab1CSh7mutG101D VH- 53 60 86 56 57 58 Non-functional 161 7,931 CDR3Ab1CSh7.15 T119L VH-FR4 53 60 68 56 57 58 ** 31135 94,91Ab1CSh7.14 V79L VH-FR3 53 60 68 56 57 58 ** 26311 98,38Ab1CSh7.13 S78T VH-FR3 53 60 68 56 57 58 ** 24619 97,44Ab1CSh7.12 D74N VH-FR3 53 60 68 56 57 58 ** 31866 95,6Ab1CSh7.11 A62D VH- 53 61 68 56 57 58 ** 22685 95,9CDR2 3

[0005] Ab1CSh7.10 G61A VH- 53 62 68 56 57 58 ** 22702 90,6CDR2 3Ab1CSh7.9 R59S VH- 53 63 68 56 57 58 ** 11643 89,5CDR2Ab1CSh7.8 Y57S VH- 53 64 68 56 57 58 ** 11183 86,3CDR2 6Ab1CSh7.7 R52N VH- 53 65 68 56 57 58 Non-functional 69 6,13CDR2Ab1CSh7.6 L51I VH- 53 66 68 56 57 58 ** 18730 96,3CDR2 8Ab1CSh7.5 S50R VH- 53 67 68 56 57 58 Non-functional -10 0,81CDR2Ab1CSh7.4 A49S VH-FR2 53 60 68 56 57 58 ** 40573 93,62Ab1CSh7.3 E46V VH-FR2 53 60 68 56 57 58 ** 23345 93,04Ab1CSh7_VH VH 53 60 68 56 57 58 Reference 11137 92,69Ab1CSh7.1 D31S VH- 59 60 68 56 57 58 ** 20844 87,5CDR1 7Ab1CS_VL VL 53 54 68 56 57 58 Reference 62105 96,79Ab1CSh7.34 Position41-42 Ser (S) insertion VL-FR2 53 60 68 56 57 58 *** 74375 95,6Ab1CSh7.30 Position96-97 Leu (L) insertion VL-CDR3 53 60 68 56 57 99 Non-functional 91 3,92

[0006] Ab1CSh7mutT53A VL-CDR2 53 60 68 56 96 58 Non-functional -18 0,5526 Ab1CSh7mutT53D VL-CDR2 53 60 68 56 97 58 Non-functional -17 0,3125 Ab1CSh7mutT53S VL-CDR2 53 60 68 56 98 58 * 8900 11,624 8 Ab1CSh7mutY34A VL-CDR1 53 60 68 91 57 58 Non-functional -18 0,0423 Ab1CSh7mutY34F VL-CDR1 53 60 68 92 57 58 * 1644 33,822 8 Ab1CSh7mutY29A VL-CDR1 53 60 68 93 57 58 Non-functional 180 7,9521 Ab1CSh7mutY29F VL-CDR1 53 60 68 94 57 58 ** 20306 95,820 1 Ab1CSh7mutY29W VL-CDR1 53 60 68 95 57 58 *** 83953 83,019 1Ab1CSh7.32 T107K VL-FR4 53 60 68 56 57 58 ** 30392 97,47Ab1CSh7.31 G100V VL-CDR3 53 60 68 56 57 100 Non-functional 11 1,7Ab1CSh7.29 D98A VL-CDR3 53 60 68 56 57 101 ** 41078 94,13Ab1CSh7.28 Y93W VL-CDR3 53 60 68 56 57 102 * 5105 75,86Ab1CSh7.27 S92T VL-CDR3 53 60 68 56 57 103 ** 9711 84,51

[0007] Ab1CSh7.26 F89Y VL-FR3 53 60 68 56 57 58 ** 25337 96,44Ab1CSh7.25 I87D VL-FR3 53 60 68 56 57 58 ** 20321 95,82Ab1CSh7.24 G73A VL-FR3 53 60 68 56 57 58 ** 10213 78,71Ab1CSh7.23 T72S VL-FR3 53 60 68 56 57 58 ** 21502 93,21Ab1CSh7.22 S71T VL-FR3 53 60 68 56 57 58 ** 27601 96,8Ab1CSh7.21 T68K VL-FR3 53 60 68 56 57 58 *** 57319 91,72Ab1CSh7.20 V49L VL-FR2 53 60 68 56 57 58 * 6737 77,07Ab1CSh7.18 L46P VL-FR2 53 60 68 56 57 58 ** 30960 92,08Ab1CSh7_VL VL 53 60 68 56 57 58 Basis 11137 92,69Ab1CSh7.17 A2S VL-FR1 53 60 68 56 57 58 ** 25181 94,27Ab1CSh7.34 Position41-42 Ser (S) insertion VL-FR2 53 60 68 56 57 58 Reference 28201 64,02 Ab1CSh7mutL103I+Y29F VH- 53 60 87 94 57 58 * 11392 82,838 CDR3+V 2 L-CDR1

[0008] Ab1CSh7mutL103S+Y29F VH- 53 60 88 94 57 58 ** 21745 21,740 CDR3+V 1 L-CDR1 Ab1CSh7mutL103I+Y29W VH- 53 60 89 95 57 58 ** 20679 10,648 CDR3+V 5 L-CDR1 Ab1CSh7mutL103V+Y29W VH- 53 60 90 95 57 58 *** 31278 27,649 CDR3+V 5 L-CDR1 Ab1CSh7mutL103I+Y29F VH- 53 60 87 94 57 58 ** 15248 56,758 CDR3+V 2 L-CDR1 Ab1CSh7mutL103V+Y29F VH- 53 60 90 94 57 58 ** 16160 64,159 CDR3+V 1 L-CDR1 Ab1CSh7mutL103S+Y29F VH- 53 60 88 94 57 58 ** 15421 83,260 CDR3+V L-CDR1 Ab1CSh7mutA2S / L46P / D98A / T107K / Y29F VL+VL- 53 60 68 94 57 101 ** 17524 73,067 CDR1- 7 CDR3 Ab1CSh7mutA2S / T107K / F89Y / Y29F VL+VL- 53 60 68 94 57 58 * 10025 73,769 CDR1 8

[0009] Ab1CSh7mutA2S / L46P / D98A / T107K / Y29F VL+VL- 53 60 68 94 57 101 ** 15926 81,573 CDR1- 5 CDR3 Ab1CSh7mutA2S / T107K / F89Y / Y29F VL+VL- 53 60 68 94 57 58 ** 21714 42,175 CDR1 8 Ab1CSh7mut A2S / D98A / T107K / T68K / S71T / T72S / Y VL+VL-53 60 68 94 57 101 *** 27745 51,776 29F CDR1- 6 CDR3

[0010] From the above data it can be concluded that: -S108 (located in CDR3-VH) alternatively can be C.- D104 (located in CDR3-VH) alternatively can be A, S, C, N or G.- L103 (located in CDR3-VH) alternatively can be A, Y, I, V, W, F or S.- S63 (located in CDR2-VH) alternatively can be A, C, N or G.- A62 (located in CDR2-VH) alternatively can be D, C, N, G or S.- G61 (located in CDR2-VH) alternatively can be A, S, C, N or D.- R59 (located in CDR2-VH) alternatively can be S, C, T, N, Q, D, E, K or Y.- Y57 (located in CDR2-VH) alternatively can be S, C, T, N, Q, D, E, K or R.- L51 (located in CDR2-VH) alternatively can be I, A, V, W, F or Y.- D31 (located in CDR1-VH) alternatively can be S, C, N, G or A.- D98 (located in CDR3-VL) alternatively can be A, C, N, G or S.- Y93 (located in CDR3-VL) alternatively can be W or F.- S92 (located in CDR3-VL) alternatively can be T.- T53 (located in CDR2-VL) alternatively can be S.- Y34 (located in CDR1-VL) alternatively can be F or W.- Y29 (located in CDR1-VL) alternatively can F or W.The tested variants are represented by the antibody comprising (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.7, a HCDR2 as set forth in SEQ ID No.8, and a HCDR3 as set forth in SEQ ID No.9, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.10, a LCDR2 region as set forth in SEQ ID No.11, and a LCDR3 region as set forth in SEQ ID No. 12. All variants including the further variants identified above as having the same properties are represented by the antibody comprising (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.1, a HCDR2 as set forth in SEQ ID No.2, and a HCDR3 as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No.4, a LCDR2 region as set forth in SEQ ID No.5, and a LCDR3 region as set forth in SEQ ID No.6. In the following the amino acid sequences of VH and VL regions are set out, wherein CDRs according to Kabat are underlined and CDRs according to IMGT are in bold. ORIGINAL mAb (chicken) >Ab1_VH AVTLDESGGGLQTPGGALSLVCKASGFTFSDYGMHWVRQAPGKGLEWLASLRSDGSYTRYGAAVKGRATISRD DGQSTVRLQLNNLRADDTATYYCARHAGGLDTTWCDNIDAWGHGTEVIVSS >Ab1_VL QAALTQPSAVSANPGETVKITCSGGSRGYAGSYYYGWFQQKSPGSALVTVIYTNDRRPSGIPSRFSGSTSGST GTLTITGVQAEDEAIYFCGSYDSSSDSGVFGAGTTLTVL >Ab1CS_VH AVTLDESGGGLQTPGGALSLVCKASGFTFSDYGMHWVRQAPGKGLEWLASLRSDGSYTRYGAAVKGRATISRD DGQSTVRLQLNNLRADDTATYYCARHAGGLDTTWSDNIDAWGHGTEVIVSS HUMANIZATION VH sequences >cAb9494-VH(Ab1CSh3) EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWLASLRSDGSYTRYGASVKGRATISRD DAQSTVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >cAb9498-VH(Ab1CSh7) EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >cAb9506-VH(Ab1CSh15) QVQLVQSGAEVKKPGASVKVSCKASGFTFSDYGMHWVRQAPGQGLEWMASLRSDGSYTRYGAKFQGRVTMTRD DSTSTVYMELSSLRSEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS VL sequences >cAb9496-VL(Ab1CSh7, h3, h15) QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL

[0011] VH Human level improvement >Ab1CSh7.1 EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKG RFTISRDDAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.3 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLVWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.4 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVSSLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.5 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVARLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.6 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASIRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.7 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLNSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.8 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSSTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.9 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTSYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.10 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYAASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.11 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGDSVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.12 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD NAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.13 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNTVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.14 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSLYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7.15 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLDTTWSDNIDAWGQGTLVTVSS Affinity / specificity improvement >Ab1CSh7mut1 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHADGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut2 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHASGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut3 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHANGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut4 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAEGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut5 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAAGLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut6 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGDLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut7 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGSLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut8 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGNLDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut9 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGELDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut10 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGALDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut11 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGYDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut12 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGADTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut13 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLITTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut14 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLYTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut15 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLLTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut16 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLSTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut17 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLTTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut18 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGLATTWSDNIDAWGQGTTVTVSS VL Human level improvement >Ab1CSh7.17 QSVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7.18 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTAPKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7.20 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTLIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7.21 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSKSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7.22 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGTTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7.23 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSSG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7.24 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTA TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7.25 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEADYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7.26 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYYCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7.27 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGTYDSSSDSGVFGGGTTLTVL >Ab1CSh7.28 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSWDSSSDSGVFGGGTTLTVL >Ab1CSh7.29 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSASGVFGGGTTLTVL >Ab1CSh7.31 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSVVFGGGTTLTVL >Ab1CSh7.32 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTKLTVL >Ab1CSh7.34 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLSPGTALKTVIYTNDRRPSGIPDRFSGSTSGST GTLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL Affinity / specificity improvement >Ab1CSh7mut19 QAVLTQPPSVSAAPGQKVTISCSGGSRGWAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7mut20 QAVLTQPPSVSAAPGQKVTISCSGGSRGFAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7mut21 QAVLTQPPSVSAAPGQKVTISCSGGSRGAAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7mut22 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYFYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7mut23 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYAYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7mut24 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYSNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7mut25 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYDNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7mut26 QAVLTQPPSVSAAPGQKVTISCSGGSRGYAGSYYYGWYQQLPGTALKTVIYANDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL Examples of combinations VH >Ab1CSh7mut38 / 48 / 58 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGIDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut40 / 60 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGSDTTWSDNIDAWGQGTTVTVSS >Ab1CSh7mut49 / 59 EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVASLRSDGSYTRYGASVKGRFTISRD DAKNSVYLQMNSLRAEDTAVYYCARHAGGVDTTWSDNIDAWGQGTTVTVSS VL >Ab1CSh7mut37-46 QAVLTQPPSVSAAPGQKVTISCSGGSRGFAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7mut47-56 QAVLTQPPSVSAAPGQKVTISCSGGSRGWAGSYYYGWYQQLSPGTALKTVIYTNDRRPSGIPDRFSGSTSGST GTLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL >Ab1CSh7mut57-66 QAVLTQPPSVSAAPGQKVTISCSGGSRGFAGSYYYGWYQQLSPGTALKTVIYTNDRRPSGIPDRFSGSTSGST GTLGITGLQTGDEAIYFCGSYDSSSDSGVFGGGTTLTVL VL >Ab1CSh7mut67 QSVLTQPPSVSAAPGQKVTISCSGGSRGFAGSYYYGWYQQLPGTAPKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYFCGSYDSSSASGVFGGGTKLTVL >Ab1CSh7mut69 QSVLTQPPSVSAAPGQKVTISCSGGSRGFAGSYYYGWYQQLPGTALKTVIYTNDRRPSGIPDRFSGSTSGSTG TLGITGLQTGDEAIYYCGSYDSSSDSGVFGGGTKLTVL >Ab1CSh7mut73 QSVLTQPPSVSAAPGQKVTISCSGGSRGFAGSYYYGWYQQLSPGTAPKTVIYTNDRRPSGIPDRFSGSTSGST GTLGITGLQTGDEAIYFCGSYDSSSASGVFGGGTKLTVL >Ab1CSh7mut75 QSVLTQPPSVSAAPGQKVTISCSGGSRGFAGSYYYGWYQQLSPGTALKTVIYTNDRRPSGIPDRFSGSTSGST GTLGITGLQTGDEAIYYCGSYDSSSDSGVFGGGTKLTVL >Ab1CSh7mut76 QSVLTQPPSVSAAPGQKVTISCSGGSRGFAGSYYYGWYQQLSPGTALKTVIYTNDRRPSGIPDRFSGSKSGTS GTLGITGLQTGDEAIYFCGSYDSSSASGVFGGGTKLTVL Binding and Affinity After binding assays performed by flow cytometry against MCF7_WT, it is possible to observe binding superiority of Ab1CSh7.34 of around 5-fold in comparison to VK9(B13), and 10-fold in comparison to OBI-888 (Figure 29). Affinity measurements were performed using Biacore T200 (Cytiva). As to the recognition of Globo H, Ab1CSh7.34 kept its superiority when compared to VK9(B13), and OBI-888 (Figure 30, Table 7). In addition, it shows superior affinity in comparison to its parental variant Ab1CSh7, resembling practically the same affinity as the original mAb when tested with mIgG2a (Ab1CS-mIgG2a). Ab1CSh7.34 also keeps low level of reactivity against SSEA-5, being more than 20-fold more affine to the target GloboH. Table 7. Calculated affinity for different Ab1CS mAbs, VK(B13), and OBI-888. mAb Affinity (KD)GloboH SSEA-5VK9(B13)-hIgG1 3.745E-05 6.908E-01Ab1CSh7.34-hIgG1 5.653E-07 1.353E-05Ab1CSh7-hIgG1 6.652E-06 1.832E-04OBI-888-hIgG1 >1E-05* >1E-05*Ab1CS-mIgG2a 5.87E-07 1.44E-05* Measurement indicates reactivity, but values do not meet minimum requirements for calculation. In vitro cytotoxicity On MCF7, results demonstrate an IC50 of 1.09 µg / mL (max. inh. 87.31%) for the AB1csh7.34-MMAE mAb and 11.5 µg / mL (max. inh.76.74) for the isotype control antiHIV- MMAE. On NCI-H526, AB1csh7.34-MMAE had an IC50 of 1.3 µg / mL (max. inh. 99.82), while the isotype control showed 23.77 µg / mL (max. inh.90.78). An additional toxophore, the Exatecan (XTC), was tested alongside MMAE on both cells. In all of them, it was observed an increased cytotoxicity of the ADC-MMAE compared to ADC- XTC. This effect is likely due the higher specific toxicity of MMAE and encouraged an in vivo efficacy study with such Ab1CSh7.34 against one of these cell models. Table 8. On MCF7_WT. Compound Absolute IC50 (µg / mL) Max inhibition %Ab1CSh7.34- 1.09 ug / mL 87.31MMAE AntiHIV-MMAE 11.5 ug / mL 76.74Ab1CSh7.34- 7.16 ug / mL 66.94Exatecan AntiHIV-Exatecan >37.5 ug / mL 41.80Table 9. On NCI-H526. Compound Absolute IC50 (µg / mL) Max inhibition %Ab1CSh7.34-MMAE 1.3 99.82AntiHIV-MMAE 23.77 90.78Ab1CSh7.34- 1.69 99.87Exatecan AntiHIV-Exatecan 24.38 89.95Ab1CSh7.34 ADC show efficacy in lung cancer model In the model with NCI-H526 cells, Ab1CSh7.34-MMAE was effective compared to the vehicle group, with a T / C of 0.52. This was superior to the control with AntiHIV-MMAE, which showed T / C of 0.79, and comparable to the standard of care (SoC), which had T / C of 0.62. This shows that the improved humanized variant Ab1CSh7.34 can be used as a molecule with anti-cancer activity (Figure 31). A humanized bispecific T-cell engager AB1cs mAb shows high T-cell dependent cytotoxicity (TDCC) against GloboH-positive cancer cells The anti-GloboH mAb produced as a bispecific T-cell engager, named BsAB1csh7.34, showed TDCC against MCF7_WT cells even when used with low PBMC:target cell ratio and low concentrations of the mAb (Figure 32 and 33). In this case, ratio as low as 1:0.5 and concentration as low as 0.01 µg / mL were still showing cytotoxicity in superior level when compared to all controls, including those with MCF7_KO. Molecules BsAB ctrl2 and BsAB ctrl3 used as negative controls showed neither TDCC nor PBMC activation, except in the highest PBMC:target ratio.

Claims

Claims 1. An antibody or antigen-binding fragment thereof specifically binding GloboH, wherein the antibody comprises: (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.1, a HCDR2 as set forth in SEQ ID No.2, and a HCDR3 as set forth in SEQ ID No.3, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No. 4, a LCDR2 region as set forth in SEQ ID No.5, and a LCDR3 region as set forth in SEQ ID No.

6.

2. The antibody or antigen-binding fragment thereof according to claim 1, wherein the antibody comprises (1) a heavy chain variable region VHcomprising a HCDR1 as set forth in SEQ ID No.7, a HCDR2 as set forth in SEQ ID No.8, and a HCDR3 as set forth in SEQ ID No.9, and (2) a light chain variable region VLcomprising a LCDR1 region as set forth in SEQ ID No. 10, a LCDR2 region as set forth in SEQ ID No.11, and a LCDR3 region as set forth in SEQ ID No.

12.

3. An antibody or antigen-binding fragment thereof according to any one of claims 1 or 2, wherein the antibody comprises the HCDR2 as set forth in SEQ ID NO: 60 and the LCDR2 as set forth in SEQ ID NO:

57.

4. The antibody or antigen-binding fragment thereof according to any one of the preceding claims comprising: a. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively; b. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 54and SEQ ID NO: 55, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively; c. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 54and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;d. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 69, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;e. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 71, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;f. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 75, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;g. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 76, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;h. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 61and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;i. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 62and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;j. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 63and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;k. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 64and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;l. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 66and SEQ ID NO: 68, respectively andthe LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;m. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;n. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO:59, SEQ ID NO:60 andSEQ ID NO:68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;o. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 98 and SEQ ID NO: 58, respectively;p. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 92, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;q. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;r. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 95, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;s. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 101, respectively;t. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 102, respectively;u. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 56, SEQ ID NO: 57 and SEQ ID NO: 103, respectively;v. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 87, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;w. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 88, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;x. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 89, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 95, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;y. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 90, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 95, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;z. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 87, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;aa. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 90, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;bb. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 88, respectively and the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 58, respectively;cc. the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 53, SEQ ID NO: 60and SEQ ID NO: 68, respectively andthe LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 94, SEQ ID NO: 57 and SEQ ID NO: 101, respectively.

5. The antibody or antigen-binding fragment thereof according to any one of the preceding claims, wherein the antibody or antigen-binding fragment thereof has a 20-fold higher affinity to GloboH compared to SEEA-5.

6. The antibody or antigen-binding fragment thereof according to any one of the preceding claims, wherein the antibody or antigen-binding fragment thereof has a 10-fold higher affinity to GloboH compared to Gb5.

7. The antibody or antigen-binding fragment thereof according to any one of the preceding claims, wherein the antibody exhibits an increased binding to Globo H as compared to antibody VK9 and / or OBI-888.

8. The antibody or an antigen-binding fragment thereof according to any one of the previous claims, wherein the antibody, or the antigen-binding fragment thereof, is a multispecific antibody or a multispecific antigen-binding fragment.

9. Antibody drug conjugate comprising the antibody or antigen-binding fragment thereof according to any one of the previous claims.

10. CAR comprising the antigen-binding fragment according to any one of claims 1 to 8.

11. Nucleotide sequence encoding the antibody of antigen-binding fragment according to any one of the claims 1 to 8 or the CAR according to claim 10.

12. Vector comprising the nucleotide sequence according to claim 11.

13. Cell comprising the nucleotide sequence according to claim 11 or the vector according to claim 12.

14. The antibody or antigen-binding fragment thereof according to any one of the claims 1 to 8, the antibody drug conjugate according to claim 9, the CAR according to claim 10, the nucleotide sequence according to claim 11, the vector according to claim 12 or the cell according to claim 13 for use as a medicament.

15. The antibody or antigen-binding fragment thereof according to any one of the claims 1 to 8, the antibody drug conjugate according to claim 9, the CAR according to claim 10, the nucleotide sequence according to claim 11, the vector according to claim 12 or the cell according to claim 13 for use in the treatment of cancer.

16. Diagnostic kit comprising the antibody or antigen-binding fragment thereof according to any one of the claims 1 to 8.

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