Variable Region Identical IgA and IgE to Cryptococcus neoformans Capsular Polysaccharide Manifest Specificity Differences.

The Journal of Biological Chemistry
Alena JandaA Casadevall

Abstract

In recent years several groups have shown that isotype switching from IgM to IgG to IgA can affect the affinity and specificity of antibodies sharing identical variable (V) regions. However, whether the same applies to IgE is unknown. In this study we compared the fine specificity of V region-identical IgE and IgA to Cryptococcus neoformans capsular polysaccharide and found that these differed in specificity from each other. The IgE and IgA paratopes were probed by nuclear magnetic resonance spectroscopy with (15)N-labeled peptide mimetics of cryptococcal polysaccharide antigen (Ag). IgE was found to cleave the peptide at a much faster rate than V region-identical IgG subclasses and IgA, consistent with an altered paratope. Both IgE and IgA were opsonic for C. neoformans and protected against infection in mice. In summary, V-region expression in the context of the ϵ constant (C) region results in specificity changes that are greater than observed for comparable IgG subclasses. These results raise the possibility that expression of certain V regions in the context of α and ϵ C regions affects their function and contributes to the special properties of those isotypes.

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Citations

Feb 13, 2016·Frontiers in Microbiology·Alena JandaArturo Casadevall
Apr 17, 2016·Clinical Immunology : the Official Journal of the Clinical Immunology Society·Nancy A Stearns, David S Pisetsky
Jul 5, 2017·Infection and Immunity·Anthony BowenArturo Casadevall
Jan 31, 2021·Proceedings of the National Academy of Sciences of the United States of America·Conor J CrawfordStefan Oscarson

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