Back to Search
Start Over
Inactivation of Vibrio vulnificus hemolysin through mutation of the N- or C-terminus of the lectin-like domain
- Source :
-
Toxicon . May2011, Vol. 57 Issue 6, p904-908. 5p. - Publication Year :
- 2011
-
Abstract
- 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. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 00410101
- Volume :
- 57
- Issue :
- 6
- Database :
- Academic Search Index
- Journal :
- Toxicon
- Publication Type :
- Academic Journal
- Accession number :
- 60157833
- Full Text :
- https://doi.org/10.1016/j.toxicon.2011.03.013