Intermolecular ionic interactions serve as a possible switch for stem release in the staphylococcal bi-component toxin for β-barrel pore assembly

Kein Takeda, Yoshikazu Tanaka, Naoki Abe, Jun Kaneko

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

The β-strand stem release system of staphylococcal β-barrel pore-forming toxin γ-hemolysin was investigated. Mutations at K15 and R16 in the cap domain of Hlg2 decreased hemolytic activity more markedly than their effect on erythrocyte binding. In addition, D122N mutation of LukF prestem lost the activity with Hlg2 R16A, indicating that electrostatic interactions between residues in the Hlg2 cap and prestem of adjacent LukF in the ring-shaped complex might serve as a switch for stem release.

Original languageEnglish
Pages (from-to)43-48
Number of pages6
JournalToxicon
Volume155
DOIs
Publication statusPublished - 2018 Dec 1

Keywords

  • Intermolecular switch
  • Staphylococcal bi-component toxin
  • β-barrel pore
  • γ-hemolysin

ASJC Scopus subject areas

  • Toxicology

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