Acquisition of Host Plasmin Activity by the Swine Pathogen Streptococcus suis Serotype 2
AUTOR(ES)
Jobin, Marie-Claude
FONTE
American Society for Microbiology
RESUMO
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 ɛ-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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=343993Documentos Relacionados
- Production and Properties of Bacteriocin-Like Inhibitory Substances from the Swine Pathogen Streptococcus suis Serotype 2
- Cloning, Purification, and Enzymatic Properties of Dipeptidyl Peptidase IV from the Swine Pathogen Streptococcus suis
- Virulent strains of Streptococcus suis serotype 2 and highly virulent strains of Streptococcus suis serotype 1 can be recognized by a unique ribotype profile.
- Invasion of Porcine Brain Microvascular Endothelial Cells by Streptococcus suis Serotype 2
- Investigation of a Novel DNase of Streptococcus suis Serotype 2†
