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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Nouha, Abdelmalek Sameh, Sellami Fakher, Frikha Slim, Tounsi Souad, Rouis |
| Description | Country affiliation: Tunisia Author Affiliation: Nouha A ( Laboratory of Plant Protection and Improvement (Biopesticides Team), Center of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, 3018 Sfax, Tunisia.); Sameh S ( Laboratory of Plant Protection and Improvement (Biopesticides Team), Center of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, 3018 Sfax, Tunisia.); Fakher F ( Faculté des Sciences de Sfax, B.P. nÌ 1171, 3000 Sfax, Tunisia.); Slim T ( Laboratory of Plant Protection and Improvement (Biopesticides Team), Center of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, 3018 Sfax, Tunisia.); Souad R ( Laboratory of Plant Protection and Improvement (Biopesticides Team), Center of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, 3018 Sfax, Tunisia. Electronic address: souad.rouis@cbs.rnrt.tn.) |
| Abstract | The Bacillus thuringiensis subsp. kurstaki strain MEB4 was previously found to be highly toxic to Ephestia kuehniella. SDS-PAGE analysis of the recombinant strain DH5 (pBS-cry2Aa-MEB4) showed that Cry2Aa-MEB4 delta-endotoxins were forming inclusion bodies, and were 2.75 fold more toxic towards E. kuehniella than those of Cry2Aa-BNS3. Besides to the 65kDa active toxin, proteolysis activation of Cry2Aa-BNS3 protein with E. kuehniella midgut juice generated an extra proteolysis form of 49kDa, which was the result of another chymotrypsin cleavage located in Leu144. The amino acid sequences alignment of Cry2Aa-MEB4 and Cry2Aa-BNS3 showed that among the different 15 amino acids, the Q139R substitution was found to be interesting. In fact, due to its presence within the loop 3- 4, the chymotrypsin-like protease was unable to access to its site in Cry2Aa-MEB4, resulting to the production of only the 65kDa form. The accessible surface and the stability studies of the structure model of the Cry2Aa-BNS3-49 form showed a lower hydrophobicity surface due to the omission of 144 amino acids from the N-terminal comparing with the active Cry2Aa-MEB4 protein. All these features caused the diminishing of Cry2Aa-BNS3 toxicity towards E. kuehniella. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 81 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-11-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Antibiosis Bacillus Thuringiensis Genetics Metabolism Codon Endotoxins Chemistry Moths Microbiology Mutation Amino Acid Sequence Amino Acid Substitution Animals Toxicity Gene Expression Hydrophobic And Hydrophilic Interactions Insect Control Models, Molecular Molecular Sequence Data Protein Conformation Protein Stability Proteolysis Recombinant Proteins Sequence Alignment Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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