PMID: 3480537Dec 1, 1987

A model of high-affinity antibody binding to type III group B Streptococcus capsular polysaccharide

Proceedings of the National Academy of Sciences of the United States of America
M R WesselsD L Kasper

Abstract

We recently reported that the single repeating-unit pentasaccharide of type III group B Streptococcus (GBS) capsular polysaccharide is only weakly reactive with type III GBS antiserum. To further elucidate the relationship between antigen-chain length and antigenicity, tritiated oligosaccharides derived from type III capsular polysaccharide were used to generate detailed saturation binding curves with a fixed concentration of rabbit antiserum in a radioactive antigen-binding assay. A graded increase in affinity of antigen-antibody binding was seen as oligosaccharide size increased from 2.6 repeating units to 92 repeating units. These differences in affinity of antibody binding to oligosaccharides of different molecular size were confirmed by immunoprecipitation and competitive ELISA, two independent assays of antigen-antibody binding. Analysis of the saturation binding experiment indicated a difference of 300-fold in antibody-binding affinity for the largest versus the smallest tested oligosaccharides. Unexpectedly, the saturation binding values approached by the individual curves were inversely related to oligosaccharide chain length on a molar basis but equivalent on a weight basis. This observation is compatible with a model...Continue Reading

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Citations

Apr 1, 1978·The Journal of Clinical Investigation·C J BakerD L Kasper
Oct 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·Craig E RubensD L Kasper

Related Concepts

Immunoglobulin Activity
Structure-Activity Relationship
Immune Sera
Streptococcus
Immunoglobulins
Polysaccharides, Bacterial
Antibody Avidity
Streptococcus agalactiae
Antigens
Antigen-Antibody Reactions

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