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Variations in binding of mammalian fibrinogens to streptococci groups A, B, C, E, G and to Staphylococcus aureus

Reutersward, A; Miörner, Håkan LU ; Wagner, M and Kronvall, G (1985) In Acta pathologica, microbiologica, et immunologica Scandinavica. Section B, Microbiology 93(2). p.77-82
Abstract
Twenty-eight beta-hemolytic streptococci of groups A, B, E, G and Streptococcus equisimilis as well as four Staphylococcus aureus strains were tested for their ability to bind fibrinogen preparations from different animal species: homo, baboon, rabbit, rat, guinea-pig, dog, horse, pig, cow and sheep. The patterns of binding indicated differences in the structures of the bacterial fibrinogen receptors. There were higher binding levels in streptococci groups A, G, and S. equisimilis than in representative group B and E strains. Considerable differences in the binding capacity were found within streptococci groups A and E. Group C and group G strains showed rather similar patterns and could be further divided into high-level and low-level... (More)
Twenty-eight beta-hemolytic streptococci of groups A, B, E, G and Streptococcus equisimilis as well as four Staphylococcus aureus strains were tested for their ability to bind fibrinogen preparations from different animal species: homo, baboon, rabbit, rat, guinea-pig, dog, horse, pig, cow and sheep. The patterns of binding indicated differences in the structures of the bacterial fibrinogen receptors. There were higher binding levels in streptococci groups A, G, and S. equisimilis than in representative group B and E strains. Considerable differences in the binding capacity were found within streptococci groups A and E. Group C and group G strains showed rather similar patterns and could be further divided into high-level and low-level binding strains. There is no correlation between binding levels of different animal fibrinogen preparations and the strains isolated from corresponding animals. Recent studies by others have shown that resistance to phagocytosis is mediated by fibrinogen-binding in streptococci group A. The existence of similar fibrinogen-binding structures in several streptococcal species indicates an important role with a definite survival value. It also suggests that M or T protein analogues are present in streptococci groups C, G and E. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Acta pathologica, microbiologica, et immunologica Scandinavica. Section B, Microbiology
volume
93
issue
2
pages
77 - 82
publisher
Munksgaard International Publishers
external identifiers
  • pmid:2990156
  • scopus:0021951155
ISSN
0108-0180
language
English
LU publication?
yes
id
5185e234-369b-4715-a936-46d4c2d899ff (old id 1103412)
date added to LUP
2008-08-11 13:27:22
date last changed
2017-08-27 05:20:41
@article{5185e234-369b-4715-a936-46d4c2d899ff,
  abstract     = {Twenty-eight beta-hemolytic streptococci of groups A, B, E, G and Streptococcus equisimilis as well as four Staphylococcus aureus strains were tested for their ability to bind fibrinogen preparations from different animal species: homo, baboon, rabbit, rat, guinea-pig, dog, horse, pig, cow and sheep. The patterns of binding indicated differences in the structures of the bacterial fibrinogen receptors. There were higher binding levels in streptococci groups A, G, and S. equisimilis than in representative group B and E strains. Considerable differences in the binding capacity were found within streptococci groups A and E. Group C and group G strains showed rather similar patterns and could be further divided into high-level and low-level binding strains. There is no correlation between binding levels of different animal fibrinogen preparations and the strains isolated from corresponding animals. Recent studies by others have shown that resistance to phagocytosis is mediated by fibrinogen-binding in streptococci group A. The existence of similar fibrinogen-binding structures in several streptococcal species indicates an important role with a definite survival value. It also suggests that M or T protein analogues are present in streptococci groups C, G and E.},
  author       = {Reutersward, A and Miörner, Håkan and Wagner, M and Kronvall, G},
  issn         = {0108-0180},
  language     = {eng},
  number       = {2},
  pages        = {77--82},
  publisher    = {Munksgaard International Publishers},
  series       = {Acta pathologica, microbiologica, et immunologica Scandinavica. Section B, Microbiology},
  title        = {Variations in binding of mammalian fibrinogens to streptococci groups A, B, C, E, G and to Staphylococcus aureus},
  volume       = {93},
  year         = {1985},
}