May, 2011
Inactivation of Vibrio vulnificus hemolysin through mutation of the N- or C-terminus of the lectin-like domain
TOXICON
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- Volume
- 57
- Number
- 6
- First page
- 904
- Last page
- 908
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1016/j.toxicon.2011.03.013
- Publisher
- PERGAMON-ELSEVIER SCIENCE LTD
Vibrio vulnificus is an etiological agent causing serious systemic infections in the immu-nocompromised 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. (C) 2011 Elsevier Ltd. All rights reserved.
- Link information
- ID information
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- DOI : 10.1016/j.toxicon.2011.03.013
- ISSN : 0041-0101
- Pubmed ID : 21426913
- Web of Science ID : WOS:000290696900009