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SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1.

Nyberg, Patrik LU ; Rasmussen, Magnus LU ; von Pawel-Rammingen, Ulrich LU and Björck, Lars LU (2004) In Microbiology1994-01-01+01:00 150(Pt 5). p.1559-1569
Abstract
SpeB is a cysteine proteinase and virulence determinant secreted by the important human pathogen Streptococcus pyogenes. Recent investigations have suggested a role for SpeB in streptococcal entry into human cells. However, conflicting data concerning the contribution of SpeB to internalization have been presented. Protein F1 is a cell-wall-attached fibronectin (Fn)-binding protein that is present in a majority of streptococcal isolates and is important for internalization. This study shows that protein F1 is efficiently degraded by SpeB, and that removal of protein F1 from the bacterial surface leads to reduced internalization. Whereas M1 protein and protein H, two additional surface proteins of S. pyogenes that bind human plasma... (More)
SpeB is a cysteine proteinase and virulence determinant secreted by the important human pathogen Streptococcus pyogenes. Recent investigations have suggested a role for SpeB in streptococcal entry into human cells. However, conflicting data concerning the contribution of SpeB to internalization have been presented. Protein F1 is a cell-wall-attached fibronectin (Fn)-binding protein that is present in a majority of streptococcal isolates and is important for internalization. This study shows that protein F1 is efficiently degraded by SpeB, and that removal of protein F1 from the bacterial surface leads to reduced internalization. Whereas M1 protein and protein H, two additional surface proteins of S. pyogenes that bind human plasma proteins, are protected from proteolytic degradation by their ligands, protein F1 is readily cleaved by SpeB also when in complex with Fn. This finding, and the connection between the presence of Fn at the bacterial surface and entry into human cells, suggest that SpeB plays a role in the regulation of the internalization process. (Less)
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Contribution to journal
publication status
published
subject
in
Microbiology1994-01-01+01:00
volume
150
issue
Pt 5
pages
1559 - 1569
publisher
MAIK Nauka/Interperiodica
external identifiers
  • wos:000221538000052
  • pmid:15133117
  • scopus:2942618331
ISSN
1465-2080
DOI
10.1099/mic.0.27076-0
language
English
LU publication?
yes
id
aa3c41f4-f04a-4e53-a96e-9080165a5bef (old id 123569)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15133117&dopt=Abstract
date added to LUP
2007-07-05 09:07:31
date last changed
2017-08-20 03:48:52
@article{aa3c41f4-f04a-4e53-a96e-9080165a5bef,
  abstract     = {SpeB is a cysteine proteinase and virulence determinant secreted by the important human pathogen Streptococcus pyogenes. Recent investigations have suggested a role for SpeB in streptococcal entry into human cells. However, conflicting data concerning the contribution of SpeB to internalization have been presented. Protein F1 is a cell-wall-attached fibronectin (Fn)-binding protein that is present in a majority of streptococcal isolates and is important for internalization. This study shows that protein F1 is efficiently degraded by SpeB, and that removal of protein F1 from the bacterial surface leads to reduced internalization. Whereas M1 protein and protein H, two additional surface proteins of S. pyogenes that bind human plasma proteins, are protected from proteolytic degradation by their ligands, protein F1 is readily cleaved by SpeB also when in complex with Fn. This finding, and the connection between the presence of Fn at the bacterial surface and entry into human cells, suggest that SpeB plays a role in the regulation of the internalization process.},
  author       = {Nyberg, Patrik and Rasmussen, Magnus and von Pawel-Rammingen, Ulrich and Björck, Lars},
  issn         = {1465-2080},
  language     = {eng},
  number       = {Pt 5},
  pages        = {1559--1569},
  publisher    = {MAIK Nauka/Interperiodica},
  series       = {Microbiology1994-01-01+01:00},
  title        = {SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1.},
  url          = {http://dx.doi.org/10.1099/mic.0.27076-0},
  volume       = {150},
  year         = {2004},
}