Electron microscopic evaluation of a two-step theory of pore formation by streptolysin O.
The formation of pores by streptolysin O (SLO) was analyzed in erythrocyte membranes and liposomes by immunoelectron microscopy and electron spectroscopic imaging. The binding of SLO molecules to membranes was temperature independent, while the polymerization of SLO molecules was temperature dependent. Our results also suggest that proteins in erythrocyte membranes are not involved in the formation of SLO rings.
Sekiya
K
K
Department of Microbiology, School of Pharmaceutical Sciences, Kitasato University, Minato-ku, Tokyo, Japan. sekiyak@platinum.pharm.kitasato-u.ac.jp.
Danbara
H
H
Yase
K
K
Futaesaku
Y
Y
D000327:Adsorption; D001426:Bacterial Proteins; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000648:ultrastructure; D008081:Liposomes / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008854:Microscopy, Electron; D016253:Microscopy, Immunoelectron; D013301:Streptolysins / Q000737:chemistry / Q000378:metabolism*; D013696:Temperature
D001426:Bacterial Proteins; D008081:Liposomes; D008565:Membrane Proteins; D013301:Streptolysins; C025964:streptolysin O