Vitronectin and its fragments purified as serum inhibitors of Staphylococcus aureus γ-hemolysin and leukocidin, and their specific binding to the Hlg2 and the LukS components of the toxins

Harue Katsumi, Toshio Tomita, Jun Kaneko, Yoshiyuki Kamio

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

Staphylococcal γ-hemolysin and leukocidin are bi-component cytolysins, consisting of LukF (or Hlg1)/Hlg2 and LukF/LukS, respectively. Here, we purified serum inhibitors of γ-hemolysin and leukocidin from human plasma. Protein sequencing showed that the purified inhibitors of 62, 57, 50 and 38 kDa were the vitronectin fragments with truncation(s) of the C-terminal or both N- and C-terminal regions. The purified vitronectin fragments specifically bound to the Hlg2 component of γ-hemolysin and the LukS component of leukocidin to form high-molecular-weight complexes with them, leading to inhibition of the toxin-induced lysis of human erythrocytes and human polymorphonuclear leukocytes, respectively. Intact vitronectin also showed inhibitory activity to the toxins. The ability of γ-hemolysin and leukocidin to bind vitronectin and its fragments is a novel function of the pore-forming cytolysins.

Original languageEnglish
Pages (from-to)451-456
Number of pages6
JournalFEBS Letters
Volume460
Issue number3
DOIs
Publication statusPublished - 1999 Nov 5

Keywords

  • Pore-forming toxin
  • Serum inhibitor
  • Staphylococcal leukocidin
  • Staphylococcal γ-hemolysin
  • Vitronectin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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