Simple jQuery Dropdowns
Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/30981
Full metadata record
DC FieldValueLanguage
dc.contributor.authorKamonnut Singkhamananen_US
dc.contributor.authorBoonhiang Promdonkoyen_US
dc.contributor.authorToemsak Srikhirinen_US
dc.contributor.authorPanadda Boonsermen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherPrince of Songkla Universityen_US
dc.contributor.otherThailand National Center for Genetic Engineering and Biotechnologyen_US
dc.date.accessioned2018-10-19T04:29:22Z-
dc.date.available2018-10-19T04:29:22Z-
dc.date.issued2013-09-01en_US
dc.identifier.citationJournal of Invertebrate Pathology. Vol.114, No.1 (2013), 65-70en_US
dc.identifier.issn10960805en_US
dc.identifier.issn00222011en_US
dc.identifier.other2-s2.0-84879203017en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84879203017&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/30981-
dc.description.abstractThe binary toxin produced by Lysinibacillus sphaericus is composed of BinA and BinB subunits that work together in governing toxicity against mosquito larvae. BinA is proposed to be important for toxicity, whereas BinB has been shown to act as a specific receptor-binding component. The precise function of both subunits, however, is not well established. Here, we investigated the function of the N-terminal region of BinB subunit initially by introducing triple alanine substitutions at positions35PEI37and41FYN43. Both block mutations abolished the larvicidal activity. Single point mutations (P35A, E36A, I37A, F41A, Y42A, N43A) were generated in order to identify amino acids that are critical for the toxin activity. Mosquito-larvicidal activity was significantly reduced in P35A, E36A, F41A and Y42A mutants. However, these mutants retained ability to form in vitro interaction with the BinA counterpart. Immunohistochemistry analysis revealed that P35A, F41A and N43A bind to the larval midgut membrane at comparable levels to that of the wild type BinB. In contrast, greatly reduced binding activity was observed in the Y42A, suggesting an important role of this residue in receptor binding. Alanine substitution at P35 resulted in a marked decrease in membrane penetration, indicating its functional importance for the membrane insertion. These results suggest the important roles of the N-terminal region of BinB in both the receptor recognition and the membrane interaction. © 2013 Elsevier Inc.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84879203017&origin=inwarden_US
dc.subjectAgricultural and Biological Sciencesen_US
dc.titleAmino acid residues in the N-terminal region of the BinB subunit of Lysinibacillus sphaericus binary toxin play a critical role during receptor binding and membrane insertionen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/j.jip.2013.05.008en_US
Appears in Collections:Scopus 2011-2015

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.