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 Biochemjournal_title
Journal of biochemistryauthors
Monma N,Nguyen VT,Kaneko J,Higuchi H,Kamio Ydoi
10.1093/jb/mvh140keywords:
subject
Has Abstractpub_date
2004-10-01 00:00:00pages
427-31issue
4eissn
0021-924Xissn
1756-2651pii
136/4/427journal_volume
136pub_type
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