Open AccessAcquisition of Host Plasmin Activity by the Swine PathogenStreptococcus suisSerotype 2
Author(s) -
Marie-Claude Jobin,
Julie Brassard,
Sylvain Quessy,
Marcelo Gottschalk,
Daniel Grenier
Publication year - 2004
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.72.1.606-610.2004
Subject(s) - streptococcus suis , plasmin , microbiology and biotechnology , biology , streptokinase , serotype , urokinase , pathogen , virulence , streptococcus dysgalactiae , streptococcus pyogenes , protease , receptor , virology , biochemistry , streptococcus , enzyme , streptococcus agalactiae , bacteria , staphylococcus aureus , medicine , genetics , psychiatry , myocardial infarction , gene
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.