Specificity of human anti-carbohydrate IgG antibodies as probed with polyacrylamide-based glycoconjugates View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-03

AUTHORS

E.P. Smorodin, O.A. Kurtenkov, B.L. Sergeyev, G.V. Pazynina, N.V. Bovin

ABSTRACT

The TF, Tn, and SiaTn glycotopes are frequently expressed in cancer-associated mucins. Antibodies to these glycotopes were found in human serum. A set of polyacrylamide (PAA)--based glycoconjugates was applied to the direct and competitive enzyme-linked immunosorbent assays (ELISA) to characterize the specificity of serum IgG antibodies. The anti-TF, -Tn and -SiaTn IgG were affinity purified from serum of cancer patients and characterized using PAA-conjugates and free saccharides. The anti-TF and -Tn antibodies were shown to be specific. The anti-TF IgG bound both Galbeta1-3GalNAcalpha- and Galbeta1-3GalNAcbeta-PAA, the latter was three-four times more effective inhibitor of antibody binding. The anti-Tn IgG reacted only with GalNAcalpha-PAA. The anti-SiaTn IgG cross-reacted with Tn-PAA but SiaTn-PAA was five-six times more effective inhibitor in a competitive assay. The IC50 values for PAA-conjugates with the corresponding antibodies typically ranged from 2 to 5 x 10(-8) M. The antibodies display a low specificity to mucin-type glycoconjugates in comparison with PAA-conjugates as was shown for mucins isolated from human malignant tumor tissues, ovine submaxillary mucin (OSM) and asialo-OSM. The unusual IgG-antibody specificity to GalNAcbeta and GalNAcbeta1-3GalNAcbeta ligands was found in human serum. More... »

PAGES

83-89

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/b:glyc.0000018582.83813.04

DOI

http://dx.doi.org/10.1023/b:glyc.0000018582.83813.04

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001055336

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15001840


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