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Plasminogen enhances virulence of group A streptococci by streptokinase-dependent and streptokinase-independent mechanisms

Khil, J ; Im, M ; Heath, A ; Ringdahl, Ulrika LU ; Mundada, L ; Engleberg, NC and Fay, WP (2003) In Journal of Infectious Diseases 188(4). p.497-505
Abstract
Interactions between host plasminogen (Plg) and streptokinase (SK) secreted by group A streptococci ( GAS) have been hypothesized to promote bacterial invasion of tissues. The virulence of GAS strain UMAA2616, after being subcutaneously inoculated into mice, was studied. Skin lesions and mortality were observed after inoculation of 7 x 10(6) cfu. Coadministration of human Plg with UMAA2616 markedly increased virulence. SK-deficient UMAA2616 (UMAA2616-SK-) was generated. Mean skin-lesion area and mortality, after bacterial inoculation (3 x 10(5) cfu), were significantly greater with UMAA2616 in the presence of human Plg than with UMAA2616-SK- in the presence of human Plg (P = .0001). Human Plg also enhanced UMAA2616-SK- vir ulence.... (More)
Interactions between host plasminogen (Plg) and streptokinase (SK) secreted by group A streptococci ( GAS) have been hypothesized to promote bacterial invasion of tissues. The virulence of GAS strain UMAA2616, after being subcutaneously inoculated into mice, was studied. Skin lesions and mortality were observed after inoculation of 7 x 10(6) cfu. Coadministration of human Plg with UMAA2616 markedly increased virulence. SK-deficient UMAA2616 (UMAA2616-SK-) was generated. Mean skin-lesion area and mortality, after bacterial inoculation (3 x 10(5) cfu), were significantly greater with UMAA2616 in the presence of human Plg than with UMAA2616-SK- in the presence of human Plg (P = .0001). Human Plg also enhanced UMAA2616-SK- vir ulence. Exogenous human Plg enhanced the virulence of MGAS166, a human clinical isolate. These findings suggest that SK-Plg interactions are an important determinant of GAS invasiveness in vivo and that both SK and host Plg activators appear to promote virulence of GAS by catalyzing plasmin formation. (Less)
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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Infectious Diseases
volume
188
issue
4
pages
497 - 505
publisher
Oxford University Press
external identifiers
  • pmid:12898435
  • wos:000184567000003
  • scopus:0041440157
ISSN
1537-6613
DOI
10.1086/377100
language
English
LU publication?
yes
id
bfb6fe3c-51e1-4ba6-8409-032fcda9eae1 (old id 304307)
date added to LUP
2016-04-01 16:37:10
date last changed
2022-01-28 20:55:57
@article{bfb6fe3c-51e1-4ba6-8409-032fcda9eae1,
  abstract     = {{Interactions between host plasminogen (Plg) and streptokinase (SK) secreted by group A streptococci ( GAS) have been hypothesized to promote bacterial invasion of tissues. The virulence of GAS strain UMAA2616, after being subcutaneously inoculated into mice, was studied. Skin lesions and mortality were observed after inoculation of 7 x 10(6) cfu. Coadministration of human Plg with UMAA2616 markedly increased virulence. SK-deficient UMAA2616 (UMAA2616-SK-) was generated. Mean skin-lesion area and mortality, after bacterial inoculation (3 x 10(5) cfu), were significantly greater with UMAA2616 in the presence of human Plg than with UMAA2616-SK- in the presence of human Plg (P = .0001). Human Plg also enhanced UMAA2616-SK- vir ulence. Exogenous human Plg enhanced the virulence of MGAS166, a human clinical isolate. These findings suggest that SK-Plg interactions are an important determinant of GAS invasiveness in vivo and that both SK and host Plg activators appear to promote virulence of GAS by catalyzing plasmin formation.}},
  author       = {{Khil, J and Im, M and Heath, A and Ringdahl, Ulrika and Mundada, L and Engleberg, NC and Fay, WP}},
  issn         = {{1537-6613}},
  language     = {{eng}},
  number       = {{4}},
  pages        = {{497--505}},
  publisher    = {{Oxford University Press}},
  series       = {{Journal of Infectious Diseases}},
  title        = {{Plasminogen enhances virulence of group A streptococci by streptokinase-dependent and streptokinase-independent mechanisms}},
  url          = {{http://dx.doi.org/10.1086/377100}},
  doi          = {{10.1086/377100}},
  volume       = {{188}},
  year         = {{2003}},
}