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The pre‐transmembrane region of the human immunodeficiency virus type‐1 glycoprotein: a novel fusogenic sequence
Author(s) -
Suárez Tatiana,
Nir Shlomo,
Goñi Félix M.,
Saéz-Cirión Asier,
Nieva José L.
Publication year - 2000
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/s0014-5793(00)01785-3
Subject(s) - sequence (biology) , transmembrane protein , glycoprotein , virology , human immunodeficiency virus (hiv) , peptide sequence , biology , chemistry , microbiology and biotechnology , biochemistry , gene , receptor
We have investigated membrane interactions and perturbations induced by NH 2 ‐DKWASLWNWFNITNWLWYIK‐COOH (HIV c ), representing the membrane interface‐partitioning region that precedes the transmembrane anchor of the human immunodeficiency virus type‐1 gp41 fusion protein. The HIV c peptide bound with high affinity to electrically neutral vesicles composed of dioleoylphosphatidylcholine, dioleoylphosphatidylethanolamine and cholesterol (molar ratio, 1:1:1), and induced vesicle leakage and lipid mixing. Infrared spectra suggest that these effects were promoted by membrane‐associated peptides adopting an α‐helical conformation. A sequence representing a defective gp41 phenotype unable to mediate both cell–cell fusion and virus entry, was equally unable to induce vesicle fusion, and adopted a non‐helical conformation in the membrane. We conclude that membrane perturbation and adoption of the α‐helical conformation by this gp41 region might be functionally meaningful.