Convergent evolution among IgGFc-binding proteins

I. Frick, M. Wikström, Sture Forsen, Torbjörn Drakenberg, H. Gomi, U. Sjöbring, Lars Björk

Research output: Contribution to journalArticleScientificpeer-review

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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.
Original languageEnglish
Pages (from-to)8532-8536
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number18
DOIs
Publication statusPublished - 1992
MoE publication typeA1 Journal article-refereed

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convergent evolution
binding proteins
bacterial proteins
proteins
peptides
synthetic peptides
surface proteins
protein-protein interactions
sequence homology
cell walls
microorganisms
amino acids
antibodies

Cite this

Frick, I., Wikström, M., Forsen, S., Drakenberg, T., Gomi, H., Sjöbring, U., & Björk, L. (1992). Convergent evolution among IgGFc-binding proteins. Proceedings of the National Academy of Sciences of the United States of America, 89(18), 8532-8536. https://doi.org/10.1073/pnas.89.18.8532
Frick, I. ; Wikström, M. ; Forsen, Sture ; Drakenberg, Torbjörn ; Gomi, H. ; Sjöbring, U. ; Björk, Lars. / Convergent evolution among IgGFc-binding proteins. In: Proceedings of the National Academy of Sciences of the United States of America. 1992 ; Vol. 89, No. 18. pp. 8532-8536.
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title = "Convergent evolution among IgGFc-binding proteins",
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 = "I. Frick and M. Wikstr{\"o}m and Sture Forsen and Torbj{\"o}rn Drakenberg and H. Gomi and U. Sj{\"o}bring and Lars Bj{\"o}rk",
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Frick, I, Wikström, M, Forsen, S, Drakenberg, T, Gomi, H, Sjöbring, U & Björk, L 1992, 'Convergent evolution among IgGFc-binding proteins', Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 18, pp. 8532-8536. https://doi.org/10.1073/pnas.89.18.8532

Convergent evolution among IgGFc-binding proteins. / Frick, I.; Wikström, M.; Forsen, Sture; Drakenberg, Torbjörn; Gomi, H.; Sjöbring, U.; Björk, Lars.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, No. 18, 1992, p. 8532-8536.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Convergent evolution among IgGFc-binding proteins

AU - Frick, I.

AU - Wikström, M.

AU - Forsen, Sture

AU - Drakenberg, Torbjörn

AU - Gomi, H.

AU - Sjöbring, U.

AU - Björk, Lars

PY - 1992

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N2 - 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.

AB - 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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SP - 8532

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