Convergent evolution among IgGFc-binding proteins

I. Frick, M. Wikström, Sture Forsen, Torbjörn Drakenberg, H. Gomi, U. Sjöbring, Lars Björk

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Abstract

Protein G, a bacterial cell-wall protein with high affinity for the constant region of IgG (IgGFc) antibodies, contains homologous repeats responsible for the interaction with IgGFc. A synthetic peptide corresponding to an 11-amino acid-long sequence in the COOH-terminal region of the repeats was found to bind to IgGFc and block the interaction with protein G.
Moreover, two other IgGFc-binding bacterial proteins (proteins A and H), which do not contain any sequences homologous to the peptide, were also inhibited in their interactions with IgGFc by the peptide. Finally, a decapeptide based on a sequence in IgGFc blocked the binding of all three proteins to IgGFc.
This unusually clear example of convergent evolution emphasizes the complexity of protein-protein interactions and suggests that bacterial surface-protein interaction with host protein adds selective advantages to the microorganism.
Original languageEnglish
Pages (from-to)8532-8536
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number18
DOIs
Publication statusPublished - 1992
MoE publication typeA1 Journal article-refereed

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Frick, I., Wikström, M., Forsen, S., Drakenberg, T., Gomi, H., Sjöbring, U., & Björk, L. (1992). Convergent evolution among IgGFc-binding proteins. Proceedings of the National Academy of Sciences of the United States of America, 89(18), 8532-8536. https://doi.org/10.1073/pnas.89.18.8532