ArticleCurrent microbiology2010
Isolation, characterization and biological role of camelysin from Bacillus thuringiensis subsp. israelensis.
Article in Current microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 24 citations in OpenAlex.
- Dissecting the Environmental Consequences ofToxins · 2021Review
- The Distribution of Several Genomic Virulence Determinants Does Not Corroborate the Established Serotyping Classification ofInternational journal of molecular sciences · 2021Article
- Repertoire of theToxins · 2019Review
- Increased copper bioremediation ability of new transgenic and adapted Saccharomyces cerevisiae strains.Environmental science and pollution research international · 2016Article
- Genomic and transcriptomic insights into the efficient entomopathogenicity of Bacillus thuringiensis.Scientific reports · 2015Article
- The metabolic regulation of sporulation and parasporal crystal formation in Bacillus thuringiensis revealed by transcriptomics and proteomics.Molecular & cellular proteomics : MCP · 2013Article
- Cloning and analysis of a large plasmid pBMB165 from Bacillus thuringiensis revealed a novel plasmid organization.PloS one · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
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Abstract
The present study reports a simple rapid method for isolating the zinc-containing metalloprotease camelysin from Bacillus thuringiensis subsp. israelensis (Bti) by extraction from intact bacterial cells with egg L-alpha-phosphatidylcholine containing monolamellar liposomes, followed by separation on a sucrose gradient. Characterization of the isolated camelysin revealed a molecular weight of 23 kDa and a pI of 6.2. The camelysin exhibited maximal activity against the substrate azocasein at a temperature of 37 degrees C and pH 7.5. However, the enzyme's activity remained high also at basic pH values (8-10). In a rich growth medium (LB), camelysin appeared at the late logarithmic phase of Bti growth and reached its maximum in the stationary phase. Camelysin was shown to activate the protoxins Cyt1Aa and Cyt2Ba produced by Bti. The hemolytic activity of Cyt1Aa increased from 40 to 70% and that of Cyt2Ba from 6 to 50% in the presence of 50% (w/w) camelysin. It is concluded that these protoxins can be activated not only by insect gut proteases, but also by the endogeneous metalloprotease camelysin of the Bti bacterium.
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