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Virulent aggregates of Streptococcus pyogenes are generated by homophilic protein-protein interactions

Frick, Inga-Maria LU ; Mörgelin, Matthias LU and Björck, Lars LU (2000) In Molecular Microbiology 37(5). p.1232-1247
Abstract
Many strains of the important human pathogen Streptococcus pyogenes form aggregates when grown in vitro in liquid medium. The present studies demonstrate that this property is crucial for the adherence, the resistance to phagocytosis and the virulence of S. pyogenes. A conserved sequence of 19 amino acid residues (designated AHP) was identified in surface proteins of common S. pyogenes serotypes. This sequence was found to promote bacterial aggregation through homophilic protein-protein interactions between AHP-containing surface proteins of neighbouring bacteria. A synthetic AHP peptide inhibited S. pyogenes aggregation, reduced the survival of S. pyogenes in human blood and attenuated its virulence in mice. In contrast, mutant bacteria... (More)
Many strains of the important human pathogen Streptococcus pyogenes form aggregates when grown in vitro in liquid medium. The present studies demonstrate that this property is crucial for the adherence, the resistance to phagocytosis and the virulence of S. pyogenes. A conserved sequence of 19 amino acid residues (designated AHP) was identified in surface proteins of common S. pyogenes serotypes. This sequence was found to promote bacterial aggregation through homophilic protein-protein interactions between AHP-containing surface proteins of neighbouring bacteria. A synthetic AHP peptide inhibited S. pyogenes aggregation, reduced the survival of S. pyogenes in human blood and attenuated its virulence in mice. In contrast, mutant bacteria devoid of surface proteins containing AHP-related sequences did not aggregate or adhere to epithelial cells. These bacteria are also rapidly killed in human blood and show reduced virulence in mice, underlining the pathogenic significance of the AHP sequence and S. pyogenes aggregation. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
37
issue
5
pages
1232 - 1247
publisher
Wiley-Blackwell
external identifiers
  • pmid:10972839
  • scopus:0033812360
ISSN
1365-2958
DOI
10.1046/j.1365-2958.2000.02084.x
language
English
LU publication?
yes
id
5e431ccf-32ec-477e-bd56-bf5f8eca2415 (old id 1117028)
date added to LUP
2008-07-02 14:57:39
date last changed
2017-09-03 03:57:58
@article{5e431ccf-32ec-477e-bd56-bf5f8eca2415,
  abstract     = {Many strains of the important human pathogen Streptococcus pyogenes form aggregates when grown in vitro in liquid medium. The present studies demonstrate that this property is crucial for the adherence, the resistance to phagocytosis and the virulence of S. pyogenes. A conserved sequence of 19 amino acid residues (designated AHP) was identified in surface proteins of common S. pyogenes serotypes. This sequence was found to promote bacterial aggregation through homophilic protein-protein interactions between AHP-containing surface proteins of neighbouring bacteria. A synthetic AHP peptide inhibited S. pyogenes aggregation, reduced the survival of S. pyogenes in human blood and attenuated its virulence in mice. In contrast, mutant bacteria devoid of surface proteins containing AHP-related sequences did not aggregate or adhere to epithelial cells. These bacteria are also rapidly killed in human blood and show reduced virulence in mice, underlining the pathogenic significance of the AHP sequence and S. pyogenes aggregation.},
  author       = {Frick, Inga-Maria and Mörgelin, Matthias and Björck, Lars},
  issn         = {1365-2958},
  language     = {eng},
  number       = {5},
  pages        = {1232--1247},
  publisher    = {Wiley-Blackwell},
  series       = {Molecular Microbiology},
  title        = {Virulent aggregates of Streptococcus pyogenes are generated by homophilic protein-protein interactions},
  url          = {http://dx.doi.org/10.1046/j.1365-2958.2000.02084.x},
  volume       = {37},
  year         = {2000},
}