Essential residues, W177 and R198, of LukF for phosphatidylcholine-binding and pore-formation by staphylococcal γ-hemolysin on human erythrocyte membranes

Naota Monma, Vananh T. Nguyen, Jun Kaneko, Hideo Higuchi, Yoshiyuki Kamio

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

LukF and Hlg2 of staphylococcal γ-hemolysin assemble into hetero-oligomeric pores on human red blood cells (HRBC). Here, we demonstrate, using a single-molecule imaging technique, that a W177T/R198T mutant of LukF, which exhibits no binding activity toward phosphatidylcholine, could form intermediate oligomers with Hlg2, including dimers, tetramers, and hexamer/heptamers, on HRBC. But, the mutant neither caused K+ efflux nor lysed HRBC, indicating that functional pores were not formed. Hence, we conclude that the W177 and R198 residues are essential for proper pore-formation by staphylococcal γ-hemolysin. We also suggest that the interaction between the W177 and R198 residues, and phosphatidylcholine on membranes is the key to the formation of functional pores.

Original languageEnglish
Pages (from-to)427-431
Number of pages5
JournalJournal of biochemistry
Volume136
Issue number4
DOIs
Publication statusPublished - 2004 Oct 1

Keywords

  • Bi-component cytolysin
  • Hetero-heptameric pore
  • Membrane binding
  • Single-FRET
  • Staphylococcal γ-hemolysin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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