Insecticidal activity of Bacillus latesporus
Article Abstract:
Bioassays were conducted to examine whether crystal-forming strains of Bacillus laterosporus possess mosquitocidal activity similar to other Bacillus species. Tests showed that the B. laterosporus strains 921 and 615 were toxic for larval populations of the Aedes aegypti, Anopheles stephensi and Culex pipiens mosquitoes. Strain 615 in particular, exhibited a high entomopathogenic activity. This could make the strain a potential candidate for controlling mosquitoes.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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Distribution and characterization of mosquitocidal toxin genes in some strains of Bacillus sphaericus
Article Abstract:
The distribution of binary toxin (btx) and mosquitocidal toxin (mtx) genes in 53 strains of bacillus sphaericus was investigated by hybridization of specific gene probes to chromosomal DNA in Southern blots. btx genes were observed in all strains of serotypes 5a5b and in some strains of serotypes 1a, 3, 6, 25 and 48, while mtx genes were found in strains of serotypes 1a, 2a2b, 5a5b, 6, 9a9c, 25 and 48. Serotype 26a26b strains did not have both toxin genes.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
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Efficient expression of a 100-kilodalton mosquitocidal toxin in protease-deficient recombinant Bacillus sphaericus
Article Abstract:
Protease does not degrade the mosquitocidal toxin Mtx in the bacterium Bacillus sphaericus 1693. This protease-negative strain exhibits adequate expression of the mtx gene which encodes Mtx. The 100 kilo dalton toxin is expressed in the vegetative phase of growth. Toxin content is low in sporulated cells in all strains. The protease-negative strains of Bacillus sphaericus can serve as efficient means of mosquito control.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
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- Abstracts: Gene cloning, transcriptional analysis, purification, and characterization of phenolic acid decarboxylase from Bacillus subtilis
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