The primary structure of Clostridium septicum alpha-toxin exhibits similarity with that of Aeromonas hydrophila aerolysin
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چکیده
منابع مشابه
Alpha Toxin Purification and Antibody Production Against Local Strain of Clostridium septicum NH2
BACKGROUND: Clostridium septicum has played a significant role as a causative agent of many acute fetal diseases in man and animals. Alpha- toxin is the main factor in the pathogenesis of C. septicum with hemolytic, necrotic and lethal activities. OBJECTIVES: The study was designed to evaluate alpha-toxin purification and antibody production rate against a local strain of C. septicum NH2 which ...
متن کاملThe cytotoxic enterotoxin of Aeromonas hydrophila is aerolysin.
The channel-forming toxin aerolysin was identified 25 years ago by Bernheimer and Avigad (1), who gave the protein its name. Aerolysin was purified by Buckley et al. (2), and its structural gene, named aerA, was cloned and sequenced almost simultaneously by two groups (6, 7). Since then more than 50 articles describing the expression, secretion, and properties of aerolysin have appeared, and ae...
متن کاملMolecular cloning of Clostridium septicum vaccine strain alpha toxin gene in E. coli
Clostridium septicum a Gram positive anaerobic bacterium produces several toxins including alpha, beta, gamma and delta. C. septicum alpha toxin is lethal and is responsible for a serious disease known as gas gangrene. The aim of the present study was to molecular cloning and sequencing of C. septicum vaccine strain alpha toxin gene. Genomic DNA was extracted using standard phenol and chlorofor...
متن کاملThe identification and structure of the membrane-spanning domain of the Clostridium septicum alpha toxin.
Alpha toxin (AT) is a pore-forming toxin produced by Clostridium septicum that belongs to the unique aerolysin-like family of pore-forming toxins. The location and structure of the transmembrane domains of these toxins have remained elusive. Using deletion mutagenesis, cysteine-scanning mutagenesis and multiple spectrofluorimetric methods a membrane-spanning amphipathic beta-hairpin of AT has b...
متن کاملClostridium septicum alpha-toxin is proteolytically activated by furin.
Clostridium septicum alpha-toxin is secreted as an inactive 46,450-Da protoxin. The protoxin is activated by proteolytic cleavage near the C terminus, which eventually causes the release of a 45-amino-acid fragment. Proteoytic activation and loss of the propeptide allow alpha-toxin to oligomerize and form pores on the plasma membrane, which results in colloidal-osmotic lysis. Activation may be ...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1995
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.63.1.340-344.1995