Advanced

Convergent evolution among immunoglobulin G-binding bacterial proteins

Frick, Inga-Maria LU ; Wikström, M; Forsen, S; Drakenberg, Torbjörn LU ; Gomi, H; Sjöbring, U and Björck, L (1992) In Proceedings of the National Academy of Sciences 89(18). p.8532-8536
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Proceedings of the National Academy of Sciences
volume
89
issue
18
pages
8532 - 8536
publisher
National Acad Sciences
external identifiers
  • pmid:1528858
  • scopus:0026775142
ISSN
1091-6490
language
English
LU publication?
yes
id
292bb4d2-2209-4d21-8563-680faf3e007c (old id 1106411)
date added to LUP
2008-08-01 14:47:17
date last changed
2017-07-30 03:44:47
@article{292bb4d2-2209-4d21-8563-680faf3e007c,
  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.},
  author       = {Frick, Inga-Maria and Wikström, M and Forsen, S and Drakenberg, Torbjörn and Gomi, H and Sjöbring, U and Björck, L},
  issn         = {1091-6490},
  language     = {eng},
  number       = {18},
  pages        = {8532--8536},
  publisher    = {National Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {Convergent evolution among immunoglobulin G-binding bacterial proteins},
  volume       = {89},
  year         = {1992},
}