Convergent evolution among immunoglobulin G-binding bacterial proteins

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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.

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Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Infektionsmedicin
Originalspråkengelska
Sidor (från-till)8532-8536
TidskriftProceedings of the National Academy of Sciences
Volym89
Utgivningsnummer18
StatusPublished - 1992
PublikationskategoriForskning
Peer review utfördJa