| Title |
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Activation process of the mosquitocidal δ-endotoxin Cry39A produced by Bacillus thuringiensis subsp aizawai BUN1-14 and binding property to Anopheles stephensi BBMV
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| Creator |
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| Accessrights |
open access |
| Subject |
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Other
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Bacillus thuringiensis
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Other
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δ-Endotoxin
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Other
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Anopheles stephensi
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Other
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Processing
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Other
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Mosquito
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Other
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BBMV
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NDC
486
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| Description |
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Abstract
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Most δ-endotoxins produced by Bacillus thuringiensis require proteolytic processing in order to become active. The in vitro and in vivo activation processes of Cry39A, a δ-endotoxin that is highly toxic to Anopheles stephensi, were investigated. Cry39A with a molecular mass of 72 kDa was processed in vitro into a 60 kDa fragment by trypsin and gut extract from A. stephensi larvae. N-terminal amino acid sequencing of the 60 kDa fragment revealed that trypsin and the protease(s) in the gut extract cleaved Cry39A between Arg61 and Gly62. In contrast, 40 and 25 kDa polypeptides were generated in vivo by intramolecular cleavage of the 60 kDa fragment in A. stephensi larvae. Further, a co-precipitation assay was used to investigate the binding property of the activated Cry39A to A. stephensi BBMV. Cry39A bound to A. stephensi BBMV specifically and did not compete with the Cry4Aa toxin. This indicated that the binding molecule(s) for Cry39A might differ from those for Cry4A. In addition, Cry39A preferentially bound to the Triton X-100-insoluble membrane fraction.
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| Publisher |
en
Elsevier B.V.
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| Date |
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| Language |
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| Resource Type |
journal article |
| Version Type |
AM |
| Identifier |
HDL
http://hdl.handle.net/2115/14743
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| Relation |
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URI
http://www.sciencedirect.com/science/journal/00222011
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isVersionOf
DOI
https://doi.org/10.1016/j.jip.2006.05.007
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PMID
16837008
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| Journal |
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PISSN
0022-2011
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EISSN
1096-0805
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en
Journal of Invertebrate Pathology
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Volume Number93
Issue Number1
Page Start29
Page End35
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| File |
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| Oaidate |
2023-07-26 |
