-
Role of cysteine at positions 67, 161 and 241 of a Bacillus sphaericus binary toxin BinB
- Back
Document Title
Role of cysteine at positions 67, 161 and 241 of a Bacillus sphaericus binary toxin BinB
Author
Boonyos P., Soonsanga S., Boonserm P., Promdonkoy B.
Name from Authors Collection
Affiliations
Institute of Molecular Biosciences, Mahidol University, Salaya Campus, Putthamonthon 4 Road, Nakhonpathom 73170, Thailand; National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, 113 Phaholyothin Road, Klong 1, Klong Luang, Pathumthani 12120, Thailand
Type
Article
Source Title
BMB Reports
ISSN
19766696
Year
2010
Volume
43
Issue
1
Page
23-28
Open Access
Gold, Green
Publisher
The Biochemical Society of the Republic of Korea
DOI
10.5483/BMBRep.2010.43.1.023
Abstract
Binary toxin consisting of BinA and BinB from Bacillus sphaericus is toxic to mosquito larvae. BinB is responsible for specific binding to the larval gut cell membrane while BinA is crucial for toxicity. To investigate functional role of cysteine in BinB, three cysteine residues at positions 67, 161, and 241 were replaced by alanine or serine. Mutations at these positions did not affect protein production and overall structure of BinB. These cysteine residues are not involved in disulfide bond formation between BinB molecules. Mosquito-larvicidal assays revealed that C67 and C161 are essential for toxicity, whereas C241 is not. Mutations at C67 and C161 resulted in weaker BinA-BinB interaction. The loss of toxicity may be due to the reduction of interactions between BinA and BinB or BinB and its receptor. C67 and C161 could also play a part during conformational changes or internalization of the binary toxin into the target cell.
Industrial Classification
Knowledge Taxonomy Level 1
Knowledge Taxonomy Level 2
Knowledge Taxonomy Level 3
License
Public Nuri
Rights
Korea Institute of Science and Technology Information https://www.kisti.re.kr/pageView/521?t=1648956401355
Publication Source
Scopus