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Protein H--a bacterial surface protein with affinity for both immunoglobulin and fibronectin type III domains

Frick, Inga-Maria LU ; Crossin, Kathryn L ; Edelman, Gerald M and Björck, Lars LU (1995) In EMBO Journal 14(8). p.1674-1679
Abstract
Several bacterial species express surface proteins with affinity for the constant region (Fc) of immunoglobulin (Ig) G. The biological consequences of the interaction with IgG are poorly understood but it has been demonstrated that genes encoding different IgG Fc-binding proteins have undergone convergent evolution, suggesting that these surface molecules are connected with essential microbial functions. One of the molecules, protein H, is present in some strains of Streptococcus pyogenes, the most significant streptococcal species in clinical medicine. In contrast to other Ig-binding bacterial proteins tested, protein H was found to interact also with the neural cell adhesion molecule (N-CAM), a eukaryotic cell surface glycoprotein... (More)
Several bacterial species express surface proteins with affinity for the constant region (Fc) of immunoglobulin (Ig) G. The biological consequences of the interaction with IgG are poorly understood but it has been demonstrated that genes encoding different IgG Fc-binding proteins have undergone convergent evolution, suggesting that these surface molecules are connected with essential microbial functions. One of the molecules, protein H, is present in some strains of Streptococcus pyogenes, the most significant streptococcal species in clinical medicine. In contrast to other Ig-binding bacterial proteins tested, protein H was found to interact also with the neural cell adhesion molecule (N-CAM), a eukaryotic cell surface glycoprotein mediating homo- and heterophilic cell-cell interactions. The affinity for the interaction between protein H and N-CAM was 1.6 x 10(8)/M and the binding site on protein H was mapped to the NH2-terminal 80 amino acid residues. N-CAM and IgG are both members of the Ig superfamily and analogous to N-CAM, IgG binds to the NH2-terminal part of protein H. However, the binding sites for the two proteins were found to be separate, an unexpected result which was explained by the observation that the fibronectin type III (FNIII) domains and not the Ig-like domains of N-CAM are responsible for the interaction with protein H. Thus, the binding of N-CAM to protein H was blocked with fibronectin but not with IgG. Moreover, apart from fibronectin itself and N-CAM, fragments of fibronectin and the matrix protein cytotactin/tenascin containing FNIII domains also showed affinity for protein H.(ABSTRACT TRUNCATED AT 250 WORDS) (Less)
Please use this url to cite or link to this publication:
author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
evolution/fibronectin/immunoglobulin/streptococci
in
EMBO Journal
volume
14
issue
8
pages
1674 - 1679
publisher
Oxford University Press
external identifiers
  • pmid:7737120
  • scopus:0029030848
ISSN
1460-2075
language
English
LU publication?
yes
id
0c2b62e0-6593-4571-bb47-51cd8eec20e6 (old id 1109047)
alternative location
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=398260
date added to LUP
2016-04-01 16:06:27
date last changed
2021-08-29 05:08:06
@article{0c2b62e0-6593-4571-bb47-51cd8eec20e6,
  abstract     = {{Several bacterial species express surface proteins with affinity for the constant region (Fc) of immunoglobulin (Ig) G. The biological consequences of the interaction with IgG are poorly understood but it has been demonstrated that genes encoding different IgG Fc-binding proteins have undergone convergent evolution, suggesting that these surface molecules are connected with essential microbial functions. One of the molecules, protein H, is present in some strains of Streptococcus pyogenes, the most significant streptococcal species in clinical medicine. In contrast to other Ig-binding bacterial proteins tested, protein H was found to interact also with the neural cell adhesion molecule (N-CAM), a eukaryotic cell surface glycoprotein mediating homo- and heterophilic cell-cell interactions. The affinity for the interaction between protein H and N-CAM was 1.6 x 10(8)/M and the binding site on protein H was mapped to the NH2-terminal 80 amino acid residues. N-CAM and IgG are both members of the Ig superfamily and analogous to N-CAM, IgG binds to the NH2-terminal part of protein H. However, the binding sites for the two proteins were found to be separate, an unexpected result which was explained by the observation that the fibronectin type III (FNIII) domains and not the Ig-like domains of N-CAM are responsible for the interaction with protein H. Thus, the binding of N-CAM to protein H was blocked with fibronectin but not with IgG. Moreover, apart from fibronectin itself and N-CAM, fragments of fibronectin and the matrix protein cytotactin/tenascin containing FNIII domains also showed affinity for protein H.(ABSTRACT TRUNCATED AT 250 WORDS)}},
  author       = {{Frick, Inga-Maria and Crossin, Kathryn L and Edelman, Gerald M and Björck, Lars}},
  issn         = {{1460-2075}},
  keywords     = {{evolution/fibronectin/immunoglobulin/streptococci}},
  language     = {{eng}},
  number       = {{8}},
  pages        = {{1674--1679}},
  publisher    = {{Oxford University Press}},
  series       = {{EMBO Journal}},
  title        = {{Protein H--a bacterial surface protein with affinity for both immunoglobulin and fibronectin type III domains}},
  url          = {{http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=398260}},
  volume       = {{14}},
  year         = {{1995}},
}