ArticleInfection and immunity1996
Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease.
Article in Infection and immunity, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 88 citations in OpenAlex.
- The Molecular Architecture and Mode of Action ofToxins · 2024Review
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- In silico characterization and structural modeling of bacterial metalloprotease of family M4.Journal, genetic engineering & biotechnology · 2021Article
- Characterization and Diversity Analysis of the Extracellular Proteases of ThermophilicFrontiers in microbiology · 2021Article
- Virulence Plasmids of the Pathogenic Clostridia.Microbiology spectrum · 2019Article
- PathogenicFrontiers in microbiology · 2017Article
- Clostridium perfringens epsilon toxin mutant Y30A-Y196A as a recombinant vaccine candidate against enterotoxemia.Vaccine · 2014Article
- Review
- Clostridium perfringens epsilon toxin H149A mutant as a platform for receptor binding studies.Protein science : a publication of the Protein Society · 2013Article
- Article
- Article
- Article
- Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Characterization of virulence plasmid diversity among Clostridium perfringens type B isolates.Infection and immunity · 2010Article
- Removal of proteases from Clostridium perfringens fermented broth by aqueous two-phase systems (PEG/citrate).Journal of industrial microbiology & biotechnology · 2007Article
- Virulence plasmid diversity in Clostridium perfringens type D isolates.Infection and immunity · 2007Article
- Comparison of virulence plasmids among Clostridium perfringens type E isolates.Infection and immunity · 2007Article
- Microbial metalloproteinases mediate sensing of invading pathogens and activate innate immune responses in the lepidopteran model host Galleria mellonella.Infection and immunity · 2007Article
- Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins.Microbiology and molecular biology reviews : MMBR · 2004Review
- Clostridium perfringens iota-toxin requires activation of both binding and enzymatic components for cytopathic activity.Infection and immunity · 2000Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lambda-toxin of Clostridium perfringens type B NCIB10691 was purified by ammonium sulfate precipitation, followed by size exclusion, anion-exchange, and hydrophobic interaction chromatography. The purified toxin had an apparent molecular mass of 36 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The toxin possessed casein-hydrolyzing activity, which was inhibited specifically by metal chelators, indicating that the toxin is a metalloprotease. The gene encoding the lambda-toxin (lam), which was shown by Southern analysis to be located on a 70-kb plasmid, was cloned into Escherichia coli cells. Nucleotide and N-terminal amino acid sequencing revealed that the lam gene encodes a 553-amino-acid protein, which is processed into a mature form, the molecular mass of which was calculated to be 35,722 Da. The deduced amino acid sequence of the mature enzyme contains an HEXXH motif characteristic of zinc metalloproteases and is homologous to other known enzymes belonging to the thermolysin family. The purified toxin degraded various biologically important substances, such as collagen, fibronectin, fibrinogen, immunoglobulin A, and the complement C3 component. It caused an increase in vascular permeability and hemorrhagic edema on injection into the dorsal skin of mice. These results suggest that the toxin contributes to the pathogenesis of histolytic infection by lambda-toxin-producing C. perfringens.
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