| Literature DB >> 14688145 |
Marie-Claude Jobin1, Julie Brassard, Sylvain Quessy, Marcelo Gottschalk, Daniel Grenier.
Abstract
In this study, the plasminogen-binding activity of Streptococcus suis serotype 2 was investigated. Bound human plasminogen was activated by purified streptokinase, urokinase, or Streptococcus dysgalactiae subsp. equisimilis culture supernatant. Both human and porcine plasminogen were bound by S. suis. Binding was inhibited by epsilon-aminocaproic acid, and the plasminogen receptor was heat and sodium dodecyl sulfate resistant. One of the receptors was identified as glyceraldehyde-3-phosphate dehydrogenase. S. suis-associated plasmin activity was capable of activating free plasminogen, which in turn could contribute to degradation of fibronectin. This is the first report on the plasminogen-binding activity of S. suis. Further studies may reveal a contribution of this activity to the virulence of S. suis.Entities:
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Year: 2004 PMID: 14688145 PMCID: PMC343993 DOI: 10.1128/IAI.72.1.606-610.2004
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441