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dc.contributorSreeramulu, Kurubaen_US
dc.contributorAkbar, Mohammad S.en_US
dc.contributorSharma, Hari C.en_US
dc.creatorRegode, Visweshwaren_US
dc.date2016-10-06en_US
dc.date.accessioned2017-04-12T10:01:47Z
dc.date.available2017-04-12T10:01:47Z
dc.identifierhttp://oar.icrisat.org/9736/en_US
dc.identifierhttps://mel.cgiar.org/reporting/download/hash/GZX7E9OBen_US
dc.identifier.citationVisweshwar Regode, Kuruba Sreeramulu, Mohammad S. Akbar, Hari C. Sharma. (6/10/2016). Isolation and Characterization of Gut Bacterial Proteases Involved in Inducing Pathogenicity of Bacillus thuringiensis Toxin in Cotton Bollworm, Helicoverpa armigera. Frontiers in Microbiology, 7: 1567.en_US
dc.identifier.urihttps://hdl.handle.net/20.500.11766/6736
dc.description.abstractBacillus thuringiensis toxin proteins are deployed in transgenic plants for pest management. The present studies were aimed at characterization of gut bacterial proteases involved in activation of inactive Cry1Ac protoxin (pro-Cry1Ac) to active toxin in Helicoverpa armigera. Bacterial strains were isolated from H. armigera midgut and screened for their proteolytic activation toward pro-Cry1Ac. Among 12 gut bacterial isolates seven isolates showed proteolytic activity, and proteases from three isolates (IVS1, IVS2, and IVS3) were found to be involved in the proteolytic conversion of proCry1Ac into active toxin. The proteases from IVS1, IVS2, and IVS3 isolates were purified to 11.90-, 15.50-, and 17.20-fold, respectively. The optimum pH and temperature for gut bacterial protease activity was 8.0 and 40◦C. Maximum inhibition of total proteolytic activity was exerted by phenylmethane sulfonyl fluoride followed by EDTA. Fluorescence zymography revealed that proteases from IVS1, IVS2, and IVS3 were chymotrypsinlike and showing protease band at ∼15, 65, and 15 kDa, respectively. Active Cry1Ac formed from processing pro-Cry1Ac by gut bacterial proteases exhibited toxicity toward H. armigera. The gut bacterial isolates IVS1, IVS2, and IVS3 showed homology with B. thuringiensis (CP003763.1), Vibrio fischeri (CP000020.2), and Escherichia coli (CP011342.1), respectively. Proteases produced by midgut bacteria are involved in proteolytic processing of B. thuringiensis protoxin and play a major role in inducing pathogenicity of B. thuringiensis toxins in H. armigera.en_US
dc.formatPDFen_US
dc.languageenen_US
dc.publisherFrontiers Mediaen_US
dc.rightsCC-BY-4.0en_US
dc.sourceFrontiers in Microbiology; 7:1567,(2016)en_US
dc.subjectmidgut bacteriaen_US
dc.subjectcry1ac proteinsen_US
dc.titleIsolation and Characterization of Gut Bacterial Proteases Involved in Inducing Pathogenicity of Bacillus thuringiensis Toxin in Cotton Bollworm, Helicoverpa armigeraen_US
dc.typeJournal Articleen_US
cg.subject.agrovocagricultureen_US
cg.subject.agrovochelicoverpa armigeraen_US
cg.subject.agrovocproteasesen_US
cg.subject.agrovoctransgenicsen_US
cg.contributor.centerInternational Crops Research Institute for the Semi-Arid Tropics - ICRISATen_US
cg.contributor.centerGulbarga Universityen_US
cg.contributor.crpCGIAR Research Program on Grain Legumes - GLen_US
cg.contributor.funderCGIAR System Organization - CGIARen_US
cg.coverage.regionGlobalen_US
cg.contactH.SHARMA@CGIAR.ORGen_US
cg.identifier.doihttps://dx.doi.org/10.3389/fmicb.2016.01567en_US
dc.identifier.statusOpen accessen_US
mel.impact-factor4.019en_US


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