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ID 48278
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Author
Abe, Yuki
Senoh, Mitsutoshi
Maehara, Yoko
Nakao, Hiroshi
Abstract
Vibrio vulnificus is an etiological agent causing serious systemic infections in the immunocompromised humans or cultured eels. This species commonly produces a hemolytic toxin consisting of the cytolysin domain and the lectin-like domain. For hemolysis, the lectin-like domain specifically binds to cholesterol in the erythrocyte membrane, and to form a hollow oligomer, the toxin is subsequently assembled on the membrane. The cytolysin domain is essential for the process to form the oligomer. Three-dimensional structure model revealed that two domains connected linearly and the C-terminus was located near to the joint of the domains. Insertion of amino acid residues between two domains was found to cause inactivation of the toxin. In the C-terminus, deletion, substitution or addition of an amino acid residue also elicited reduction of the activity. However, the cholesterol-binding ability was not affected by the mutations. These results suggest that mutation of the C- or N-terminus of the lectin-like domain may result in blockage of the toxin assembly.
Keywords
Vibrio vulnificus
Hemolysin
Cell-free translation
Site-directed mutagenesis
Published Date
2011-05
Publication Title
Toxicon
Volume
volume57
Issue
issue6
Publisher
Elsevier
Start Page
904
End Page
908
ISSN
0041-0101
NCID
AA00864479
Content Type
Journal Article
Project
Collaborative Research of Okayama University for Infectious Diseases in India
Official Url
http://www.sciencedirect.com/science/article/pii/S0041010111000997
language
英語
Copyright Holders
©2011 Elsevier Ltd. All rights reserved.
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True
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