Essential Residues, W177 and R198, of LukF for Phosphatidylcholine-Binding and Pore-Formation by Staphylococcal  -Hemolysin on Human Erythrocyte Membranes

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  • Monma Naota
    Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University
  • Nguyen Vananh T.
    Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University
  • Kaneko Jun
    Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University
  • Higuchi Hideo
    Center for Interdisciplinary Research, Tohoku University
  • Kamio Yoshiyuki
    Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University

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タイトル別名
  • Essential Residues, W 177 and R 198, of LukF for Phosphatidylcholine-Binding and Pore-Formation by Staphylococcal γ-Hemolysin on Human Erythrocyte Membranes
  • Essential Residues W177 and R198 of LukF for Phosphatidylcholine Binding and Pore Formation by Staphylococcal ガンマ Hemolysin on Human Erythrocyte Membranes
  • Essential residues, W177 and R198, of LukF for phosphatidylcholine-binding and pore-formation by staphylococcal gamma-hemolysin on human erythrocyte membranes

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抄録

LukF and Hlg 2 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 W 177 T/R 198 T mutant of LukF, which exhibits no binding activity toward phosphatidylcholine, could form intermediate oligomers with Hlg 2, 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 W 177 and R 198 residues are essential for proper pore-formation by staphylococcal γ-hemolysin. We also suggest that the interaction between the W 177 and R 198 residues, and phosphatidylcholine on membranes is the key to the formation of functional pores.

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