Inactivation of Vibrio vulnificus hemolysin through mutation of the N- or C-terminus of the lectin-like domain

Shin ichi Miyoshi, Yuki Abe, Mitsutoshi Senoh, Tamaki Mizuno, Yoko Maehara, Hiroshi Nakao

Research output: Contribution to journalArticle

3 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)904-908
Number of pages5
JournalToxicon
Volume57
Issue number6
DOIs
Publication statusPublished - May 1 2011

Keywords

  • Cell-free translation
  • Hemolysin
  • Site-directed mutagenesis
  • Vibrio vulnificus

ASJC Scopus subject areas

  • Toxicology

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