Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein

被引：203

作者：

Bergmann, S

Rohde, M

Hammerschmidt, S

机构：

[1] Univ Wurzburg, Res Ctr Infect Dis, D-97070 Wurzburg, Germany

[2] GBF Gernam Res Ctr Biotechnol, Braunschweig, Germany

来源：

INFECTION AND IMMUNITY | 2004年 / 72卷 / 04期

关键词：

D O I：

10.1128/IAI.72.4.2416-2419.2004

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

The recruitment of plasminogen endows the bacterial cell surface of Streptococcus pneumoniae with proteolytic activity. In this study we demonstrate specific plasmin- and plasminogen-binding activity for the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is located in the cytoplasm as well as on the surface of pneumococci. GAPDH exhibits a high affinity for plasmin and a significantly lower affinity for plasminogen.

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页码：2416 / 2419

页数：4

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