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A role for the fibrinogen-binding regions of streptococcal M proteins in phagocytosis resistance

Ringdahl, Ulrika LU ; Svensson, Henrik LU ; Kotarsky, Heike LU ; Gustafsson, Maria; Weineisen, Maria LU and Sjöbring, Ulf LU (2000) In Molecular Microbiology 37(6). p.1318-1326
Abstract
All virulent group A streptococcal isolates bind fibrinogen, a property that is closely linked to expression of type-specific antiphagocytic surface molecules designated M proteins. Here we show that although the M proteins from two different strains, M1 and M5, both bind fibrinogen with high affinity, they interact with different regions in the ligand. Moreover, mapping experiments demonstrated that the fibrinogen-binding regions in the M1 and M5 proteins are quite dissimilar at the amino acid sequence level and that they bind to different regions in the plasma protein. In spite of these differences, the fibrinogen-binding regions of M1 and M5 could both be shown to contribute to streptococcal survival in human blood, providing evidence... (More)
All virulent group A streptococcal isolates bind fibrinogen, a property that is closely linked to expression of type-specific antiphagocytic surface molecules designated M proteins. Here we show that although the M proteins from two different strains, M1 and M5, both bind fibrinogen with high affinity, they interact with different regions in the ligand. Moreover, mapping experiments demonstrated that the fibrinogen-binding regions in the M1 and M5 proteins are quite dissimilar at the amino acid sequence level and that they bind to different regions in the plasma protein. In spite of these differences, the fibrinogen-binding regions of M1 and M5 could both be shown to contribute to streptococcal survival in human blood, providing evidence for the distinct function of a plasma protein interaction in bacterial pathogenesis. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
37
issue
6
pages
1318 - 1326
publisher
Wiley-Blackwell
external identifiers
  • pmid:10998165
  • scopus:0033779403
ISSN
1365-2958
DOI
10.1046/j.1365-2958.2000.02062.x
language
English
LU publication?
yes
id
09e94f69-5420-48c0-8704-88176cfeb9d3 (old id 1116932)
date added to LUP
2008-07-02 13:36:39
date last changed
2017-06-18 03:48:37
@article{09e94f69-5420-48c0-8704-88176cfeb9d3,
  abstract     = {All virulent group A streptococcal isolates bind fibrinogen, a property that is closely linked to expression of type-specific antiphagocytic surface molecules designated M proteins. Here we show that although the M proteins from two different strains, M1 and M5, both bind fibrinogen with high affinity, they interact with different regions in the ligand. Moreover, mapping experiments demonstrated that the fibrinogen-binding regions in the M1 and M5 proteins are quite dissimilar at the amino acid sequence level and that they bind to different regions in the plasma protein. In spite of these differences, the fibrinogen-binding regions of M1 and M5 could both be shown to contribute to streptococcal survival in human blood, providing evidence for the distinct function of a plasma protein interaction in bacterial pathogenesis.},
  author       = {Ringdahl, Ulrika and Svensson, Henrik and Kotarsky, Heike and Gustafsson, Maria and Weineisen, Maria and Sjöbring, Ulf},
  issn         = {1365-2958},
  language     = {eng},
  number       = {6},
  pages        = {1318--1326},
  publisher    = {Wiley-Blackwell},
  series       = {Molecular Microbiology},
  title        = {A role for the fibrinogen-binding regions of streptococcal M proteins in phagocytosis resistance},
  url          = {http://dx.doi.org/10.1046/j.1365-2958.2000.02062.x},
  volume       = {37},
  year         = {2000},
}