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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