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

Abstract:

: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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Monma N,Nguyen VT,Kaneko J,Higuchi H,Kamio Y

doi

10.1093/jb/mvh140

keywords:

subject

Has Abstract

pub_date

2004-10-01 00:00:00

pages

427-31

issue

4

eissn

0021-924X

issn

1756-2651

pii

136/4/427

journal_volume

136

pub_type

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