More than meets the Kappa for Antibody Superantigen Protein L (PpL)

Ling, W. L.; Yeo, J. Y.; Ng, Y. L.; Wipat, A.; Gan, S. K.

doi:10.1101/2021.11.26.470168

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bioRxiv · 10.1101/2021.11.26.470168

More than meets the Kappa for Antibody Superantigen Protein L (PpL)

Ling, W. L.·Yeo, J. Y.·Ng, Y. L.·Wipat, A.·Gan, S. K.

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Abstract

Immunoglobulin superantigens play an important role in the affinity purification of antibodies and underlie the microbiota-immune axis at mucosal areas Focussing on the Staphylococcal Protein A (SpA), Streptococcal Protein G (SpG), and the Finegoldia Protein L (PpL) that were previously thought to bind to only specific regions of human antibodies, a systematic and holistic analysis of the antibody regions using 63 antibody permutations involving six V{kappa} and seven VH region IgG1 revealed showed novel PpL-antibody interactions. While SpA and SpG showed relatively consistent interactions with the antibodies, our findings showed PpL binding to certain VH-V{kappa}2, 5 and 6 interactions had contribution by other antibody regions. The findings of this have implications on PpL-based affinity antibody purifications and antibody design as well as provides novel insights to PpL-based microbiota-immune axis effects.

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Ling, W. L., Yeo, J. Y., Ng, Y. L., Wipat, A., Gan, S. K.. 2021-11-27. More than meets the Kappa for Antibody Superantigen Protein L (PpL). https://doi.org/10.1101/2021.11.26.470168

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