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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/41717
Title: pH regulates pore formation of a protease activated Vip3Aa from Bacillus thuringiensis
Authors: Thittaya Kunthic
Hirokazu Watanabe
Ryuji Kawano
Yoshikazu Tanaka
Boonhiang Promdonkoy
Min Yao
Panadda Boonserm
Mahidol University
Tokyo University of Agriculture and Technology
Hokkaido University
Tohoku University
Japan Science and Technology Agency
Thailand National Center for Genetic Engineering and Biotechnology
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Nov-2017
Citation: Biochimica et Biophysica Acta - Biomembranes. Vol.1859, No.11 (2017), 2234-2241
Abstract: © 2017 Elsevier B.V. Vip3Aa insecticidal protein is produced from Bacillus thuringiensis and exerts a broad spectrum of toxicity against lepidopteran insect species. Although Vip3Aa has been effectively used as part of integrated pest management strategies, the mechanism of the toxin remains unclear. Here, we investigated the effect of pH in a range from 5.0 to 10.0 on the pore-forming activity of the trypsin activated Vip3Aa (actVip3Aa) by in vitro pore-forming assays. Based on calcein release assay, actVip3Aa could permeabilize the artificial neutral liposomes under all the pH tested, except pH 10.0. The maximum membrane permeability of actVip3Aa was detected at pH 8.0 and the permeability decreased and abolished when exposing to acidic and alkaline conditions, respectively. The planar lipid bilayer experiment revealed that actVip3Aa formed ion channels at pH 5.0–8.0 but no current signals were detected at pH 10.0, consistent with the observation from calcein release assay. The toxin formed ion channels with a diameter of 1.4 nm at pH 8.0 and pore size was gradually decreased when reducing the pH. This study provided a view of the molecular mechanism of Vip3Aa by which the pore-forming activity is regulated by pH.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85029142807&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/41717
ISSN: 18792642
00052736
Appears in Collections:Scopus 2016-2017

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