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

@article{Monma2004EssentialRW,
  title={Essential residues, W177 and R198, of LukF for phosphatidylcholine-binding and pore-formation by staphylococcal gamma-hemolysin on human erythrocyte membranes.},
  author={Naota Monma and Vananh T Nguyen and Jun Kaneko and Hideo Higuchi and Yoshiyuki Kamio},
  journal={Journal of biochemistry},
  year={2004},
  volume={136 4},
  pages={427-31}
}
LukF and Hlg2 of staphylococcal gamma-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… CONTINUE READING