Jobin Marie-Claude, Brassard Julie, Quessy Sylvain, Gottschalk Marcelo, Grenier Daniel
Groupe de Recherche en Ecologie Buccale, Faculté de Médecine Dentaire, Université Laval, Quebec City, Quebec, Canada.
Infect Immun. 2004 Jan;72(1):606-10. doi: 10.1128/IAI.72.1.606-610.2004.
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.
在本研究中,对猪链球菌2型的纤溶酶原结合活性进行了研究。结合的人纤溶酶原由纯化的链激酶、尿激酶或停乳链球菌马亚种培养上清液激活。猪链球菌能结合人和猪的纤溶酶原。结合被ε-氨基己酸抑制,且纤溶酶原受体耐热和耐十二烷基硫酸钠。其中一种受体被鉴定为甘油醛-3-磷酸脱氢酶。猪链球菌相关的纤溶酶活性能够激活游离纤溶酶原,这反过来可能有助于纤连蛋白的降解。这是关于猪链球菌纤溶酶原结合活性的首次报道。进一步的研究可能会揭示这种活性对猪链球菌毒力的作用。