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Convergent evolution among immunoglobulin G-binding bacterial proteins

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  • I M Frick
  • M Wikström
  • S Forsén
  • T Drakenberg
  • H Gomi
  • U Sjöbring
  • L Björck
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.
TidsskriftProceedings of the National Academy of Sciences of the United States of America
Udgave nummer18
Sider (fra-til)8532-6
Antal sider5
StatusUdgivet - 15 sep. 1992
Eksternt udgivetJa

ID: 50165967