Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41598-017-15123-z
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dc.titleShotgun Glycomics Identifies Tumor-Associated Glycan Ligands Bound by an Ovarian Carcinoma-Specific Monoclonal Antibody
dc.contributor.authorLiau, B
dc.contributor.authorTan, B
dc.contributor.authorTeo, G
dc.contributor.authorZhang, P
dc.contributor.authorChoo, A
dc.contributor.authorRudd, P.M
dc.date.accessioned2020-10-20T10:19:45Z
dc.date.available2020-10-20T10:19:45Z
dc.date.issued2017
dc.identifier.citationLiau, B, Tan, B, Teo, G, Zhang, P, Choo, A, Rudd, P.M (2017). Shotgun Glycomics Identifies Tumor-Associated Glycan Ligands Bound by an Ovarian Carcinoma-Specific Monoclonal Antibody. Scientific Reports 7 (1) : 14489. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-017-15123-z
dc.identifier.issn2045-2322
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/178562
dc.description.abstractCancers display distinctive carbohydrate molecules (glycans) on their surface proteins and lipids. mAb A4, an in-house generated monoclonal IgM antibody, is capable of distinguishing malignant ovarian carcinoma cells from benign ovarian epithelia by binding specifically to cancer cell-associated glycans. However, the structural details of the glycan targets of mAb A4 have been elusive. Here we developed a novel approach of isolating and fractionating glycan molecules released from glycoproteins in cancer cell lysates using HILIC-UPLC, and used them as probes on a microarray for affinity-based identification of the binding targets, allowing full-size, difficult to synthesize, cancer-associated glycans to be directly studied. As a result of this "shotgun" glycomics approach, we corroborate the previously assigned specificity of mAb A4 by showing that mAb A4 binds primarily to large (>15 glucose units), sialylated N-glycans containing the H-type 1 antigen (Fuc-?1,2-Gal-?1,3-GlcNAc). Although mAb A4 was also capable of directly binding to type 1 N-acetyl-lactosamine, this epitope was mostly shielded by sialylation and thus relatively inaccessible to binding. Knowledge of the structure of mAb A4 antigen will facilitate its clinical development as well as its use as a diagnostic biomarker. © 2017 The Author(s).
dc.publisherNature Publishing Group
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceUnpaywall 20201031
dc.subjectcancer antibody
dc.subjectmonoclonal antibody
dc.subjectpolysaccharide
dc.subjecttumor marker
dc.subjectanimal
dc.subjectcell line
dc.subjectepithelium
dc.subjectfemale
dc.subjectglycobiology
dc.subjecthuman
dc.subjectmetabolism
dc.subjectmicroarray analysis
dc.subjectmouse
dc.subjectovary
dc.subjectovary tumor
dc.subjectprocedures
dc.subjectsensitivity and specificity
dc.subjectAnimals
dc.subjectAntibodies, Monoclonal
dc.subjectAntibodies, Neoplasm
dc.subjectBiomarkers, Tumor
dc.subjectCell Line
dc.subjectEpithelium
dc.subjectFemale
dc.subjectGlycomics
dc.subjectHumans
dc.subjectMice
dc.subjectMicroarray Analysis
dc.subjectOvarian Neoplasms
dc.subjectOvary
dc.subjectPolysaccharides
dc.subjectSensitivity and Specificity
dc.typeArticle
dc.contributor.departmentBIOMEDICAL ENGINEERING
dc.description.doi10.1038/s41598-017-15123-z
dc.description.sourcetitleScientific Reports
dc.description.volume7
dc.description.issue1
dc.description.page14489
dc.published.statepublished
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