The interaction of Streptococcus dysgalactiae with plasmin and plasminogen
The interaction of Streptococcus dysgalactiae with plasmin and plasminogen
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DOI：
10.1016/s0378-1135(98)00179-5
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发表时间：
1998-03-15
影响因子：
3.3
通讯作者：
Lincoln, RA
中科院分区：
文献类型：
--
作者：
Leigh, JA;Hodgkinson, SM;Lincoln, RA
纤溶酶原的激活和纤溶酶被细菌结合可能具有促进感染的许多作用。链球菌中这种活性的发生是有据可查的，然而，链球菌中这种活性还有待证实。停乳因此，研究了该细菌激活哺乳动物纤溶酶原并结合纤溶酶或其酶原的能力。牛纤溶酶原的激活取决于菌株和用于培养的生长培养基。18株菌株能够激活牛和绵羊纤溶酶原，其中一些菌株还激活了来自马、兔和猪的纤溶酶原。无激活人纤溶酶原，1株菌株（CE 127）未激活任何来源的纤溶酶原。Tricine-SDS PAGE和酶谱分析的培养上清液表明，牛纤溶酶原激活的四个6株在两个位置对应于16 kDa和10 kDa。在牛纤溶酶原存在下生长5种菌株后，除菌株CE 127外，所有菌株均结合高水平的纤溶酶活性。相比之下，在人纤溶酶原中生长后，没有菌株表现出结合纤溶酶活性，尽管所有菌株都可以直接结合人纤溶酶。所有菌株还能够以允许其被尿激酶激活的方式结合牛和人纤溶酶原。我们的结论是S.停乳菌能够以物种特异性方式激活哺乳动物纤溶酶原，并且该细菌还能够结合纤溶酶和纤溶酶原，其中明显偏好牛纤溶酶而不是人纤溶酶和/或来自任一物种的纤溶酶原。(C)1998年Elsevier Science B.V.
The activation of plasminogen and the binding of plasmin by bacteria may have many effects which promote infection. The occurrence of such activities in streptococci is well documented; however, these are yet to be demonstrated for S. dysgalactiae. Consequently, the ability of this bacterium to activate mammalian plasminogen and bind either plasmin or its zymogen was investigated. Activation of bovine plasminogen was dependant on both the strain and the growth medium used for cultivation. Eighteen strains were able to activate bovine and ovine plasminogen and some of these also activated plasminogen from the horse, rabbit and pig. None activated human plasminogen and one strain (CE127) did not activate plasminogen from any source. Tricine-SDS PAGE and zymographic analysis of culture supernatants showed that bovine plasminogen was activated by four out of six strains at two locations corresponding to 16 kDa and IO kDa. Following the growth of five strains in the presence of bovine plasminogen, all but strain CE127 bound high levels of plasmin activity. In contrast, following growth in human plasminogen none of the strains exhibited bound plasmin activity although all could bind human plasmin directly. Ail strains were also able to bind bovine and human plasminogen in such a way as to allow its activation by urokinase. We conclude that S. dysgalactiae is capable of activating mammalian plasminogen in a species-specific fashion and that the bacterium is also capable of binding plasmin and plasminogen with an apparent preference for bovine plasmin over human plasmin and/or plasminogen from either species. (C) 1998 Elsevier Science B.V.