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Convergent evolution among immunoglobulin G-binding bacterial proteins

På svenska

Author

  • Inga-Maria Frick
  • M Wikström
  • S Forsen
  • Torbjörn Drakenberg
  • H Gomi
  • U Sjöbring
  • L Björck

Summary, in English

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.

Publishing year

1992

Language

English

Pages

8532-8536

Publication/Series

Proceedings of the National Academy of Sciences

Volume

89

Issue

18

Document type

Journal article

Publisher

National Academy of Sciences

Topic

  • Infectious Medicine

Status

Published

ISBN/ISSN/Other

  • ISSN: 1091-6490