Convergent evolution among immunoglobulin G-binding bacterial proteins
(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:
https://lup.lub.lu.se/record/1106411
- author
- Frick, Inga-Maria LU ; Wikström, M ; Forsen, S ; Drakenberg, Torbjörn LU ; Gomi, H ; Sjöbring, U and Björck, L
- organization
- publishing date
- 1992
- 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 Academy of 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
- 2016-04-01 12:11:22
- date last changed
- 2021-08-01 03:58:26
@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 Academy of Sciences}}, series = {{Proceedings of the National Academy of Sciences}}, title = {{Convergent evolution among immunoglobulin G-binding bacterial proteins}}, volume = {{89}}, year = {{1992}}, }