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J. Biochem, 2004, Vol. 136, No. 4 427-431
© 2004 The Japanese Biochemical Society

BIOCHEMISTRY

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

Naota Monma1, Vananh T. Nguyen1, Jun Kaneko1, Hideo Higuchi2 and Yoshiyuki Kamio1,*

1 Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555; and 2 Center for Interdisciplinary Research, Tohoku University, Sendai 980-8579

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. Hence, we conclude that the W177 and R198 residues are essential for proper pore-formation by staphylococcal {gamma}-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.

* To whom correspondence should be addressed. Tel: +81-22-717-8779, Fax: +81-22-717-8780, E-mail: ykamio{at}biochem.tohoku.ac.jp


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