ACTIVATION AND MECHANISM OF CLOSTRIDIUM-SEPTICUM ALPHA-TOXIN

被引:72
作者
BALLARD, J
SOKOLOV, Y
YUAN, WL
KAGAN, BL
TWETEN, RK
机构
[1] UNIV OKLAHOMA HLTH SCI CTR, HLTH SCI CTR, DEPT MICROBIOL & IMMUNOL, OKLAHOMA CITY, OK 73190 USA
[2] UNIV CALIF LOS ANGELES, INST NEUROPSYCHIAT, DEPT PSYCHIAT, LOS ANGELES, CA 90024 USA
[3] W LOS ANGELES DEPT VET AFFAIRS MED CTR, LOS ANGELES, CA 90024 USA
关键词
D O I
10.1111/j.1365-2958.1993.tb00934.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Clostridium septicum produces a single lethal factor, alpha toxin (AT), which is a cytolytic protein with a molecular mass of approximately 48 kDa. The 48 kDa toxin was found to be an inactive protoxin (AT(pro)) which could be activated via a carboxy-terminal cleavage with trypsin. The cleavage site was located approximately 4 kDa from the carboxy-terminus. Proteolytically activated AT(pro) had a specific activity of approximately 1.5 x 10(6) haemolytic units mg-1. The trypsin-activated toxin (AT(act)) was haemolytic, stimulated a prelytic release of potassium ions from erythrocytes which was followed by haemoglobin release, induced channel formation in planar membranes and aggregated into a complex of M(r) > 210 000 on erythrocyte membranes. AT(pro) did not exhibit these properties. AT(act) formed pores with a diameter of at least 1.3-1.6 nm. We suggest that pore formation on target cell membranes is responsible for the cytolytic activity of alpha toxin.
引用
收藏
页码:627 / 634
页数:8
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