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M9630472.TXT
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1996-02-27
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Document 0472
DOCN M9630472
TI Lysophosphatidylcholine inhibits vesicles fusion induced by the
NH2-terminal extremity of SIV/HIV fusogenic proteins.
DT 9603
AU Martin I; Ruysschaert JM; Laboratoire de Chimie-Physique des
Macromolecules aux Interfaces; CP206/2, Universite Libre de Bruxelles,
Belgium.
SO Biochim Biophys Acta. 1995 Nov 22;1240(1):95-100. Unique Identifier :
AIDSLINE MED/96096712
AB 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.
DE Amino Acid Sequence Cholesterol/METABOLISM Fluoresceins/METABOLISM
Gene Products, env/*CHEMISTRY/PHARMACOLOGY HIV/CHEMISTRY HIV Envelope
Protein gp41/*CHEMISTRY/PHARMACOLOGY Indicators and Reagents/METABOLISM
Lipid Bilayers/METABOLISM Liposomes/*METABOLISM
Lysophosphatidylcholines/*PHARMACOLOGY Molecular Sequence Data
Peptides/CHEMISTRY/PHARMACOLOGY Permeability
Phosphatidylcholines/METABOLISM Phosphatidylethanolamines/METABOLISM
Retroviridae Proteins, Oncogenic/*CHEMISTRY/PHARMACOLOGY Support,
Non-U.S. Gov't SIV/CHEMISTRY Temperature Viral Fusion
Proteins/*CHEMISTRY/*PHARMACOLOGY JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).