Source:http://linkedlifedata.com/resource/pubmed/id/21426913
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2011-4-22
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1879-3150
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
904-8
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pubmed:meshHeading |
pubmed-meshheading:21426913-Bacterial Proteins,
pubmed-meshheading:21426913-Blotting, Western,
pubmed-meshheading:21426913-Cell Membrane,
pubmed-meshheading:21426913-Cholesterol,
pubmed-meshheading:21426913-Erythrocytes,
pubmed-meshheading:21426913-Hemolysin Proteins,
pubmed-meshheading:21426913-Mutagenesis,
pubmed-meshheading:21426913-Mutation,
pubmed-meshheading:21426913-Polymerase Chain Reaction,
pubmed-meshheading:21426913-Protein Structure, Tertiary,
pubmed-meshheading:21426913-Vibrio vulnificus
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pubmed:year |
2011
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pubmed:articleTitle |
Inactivation of Vibrio vulnificus hemolysin through mutation of the N- or C-terminus of the lectin-like domain.
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pubmed:affiliation |
Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Tsushima-Naka, Okayama 700-8530, Japan. miyoshi@pharm.okayama-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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