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Membrane binding requirements for the cytolytic activity of Leishmania amazonensis leishporin
Author(s) -
Castro-Gomes Thiago,
Almeida-Campos Flávia Regina,
Calzavara-Silva Carlos Eduardo,
da Silva Rosiane Aparecida,
Frézard Frédéric,
Horta Maria Fátima
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.09.005
Subject(s) - cytolysin , lysis , cytolysis , lytic cycle , hemolysis , biochemistry , receptor , dipalmitoylphosphatidylcholine , liposome , chemistry , biology , microbiology and biotechnology , membrane , in vitro , cytotoxicity , phospholipid , immunology , phosphatidylcholine , virus , virulence , gene
To lyse cells, some pore‐forming proteins need to bind to receptors on their targets. Studying the binding requirements of Leishmania amazonensis leishporin, we have shown that protease‐treated erythrocytes are as sensitive to leishporin‐mediated lysis as untreated cells, indicating that protein receptors are dispensable. Similarly, carbohydrate receptors do not seem to be needed, since several sugars do not inhibit leishporin‐mediated hemolysis. Conversely, dipalmitoylphosphatidylcholine (DPPC), but not cholesterol, completely inhibits leishporin‐mediated lysis. DPPC liposomes, with or without cholesterol, are lysed by leishporin and remove its lytic activity. Our results demonstrate that leishporin is a cholesterol‐independent cytolysin that binds directly to phospholipids.