Lysophosphatidylcholine inhibits vesicles fusion induced by the NH2-terminal extremity of SIV/HIV fusogenic proteins
Biochimica et Biophysica Acta (BBA) - BiomembranesPublished 1 November 1995
Isabelle Martin, J.M. Ruysschaert
Citations31
SJR quartileQ1
SJR score0.81
SNIP0.77
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TL;DR
Evidence is provided that lipid mixing of large unilamellar lipid vesicles (LUV) mediated by the NH2-terminal sequence of the SIV gp32 and of HIV gp41 is inhibited by external addition of lysophosphatidylcholine (lysoPC) to LUV containing phosphatidylethanolamine in their lipid bilayer.
Abstract
Intermediate lipid structures such as inverted micelles and interlamellar attachments are thought to play a crucial role in different biological processes like exocytosis, intracellular trafficking and viral infection. In the present study, we provide evidence that lipid mixing of large unilamellar lipid vesicles (LUV) mediated by the NH2-terminal sequence of the SIV gp32 and of HIV gp41 is inhibited by external addition of lysophosphatidylcholine (lysoPC) to LUV containing phosphatidylethanolamine in their lipid bilayer. Leakage experiments confirm that lysoPC enhances the stability of the lipids organization. The temperature dependence of the two processes as well as the complementary shape of PE and lysoPC suggest that the PE-lysoPC interaction is involved in the fusion inhibition and stabilization of the bilayer.
Keywords
Immunology and MicrobiologyBiochemistry, Genetics and Molecular Biology
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