Oligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers

Biophysical Journal
Jun YangDavid P Weliky

Abstract

The human immunodeficiency virus type 1 (HIV-1) fusion peptide serves as a useful model system for understanding viral/target cell fusion, at least to the lipid mixing stage. Previous solid-state NMR studies have shown that the peptide adopts an oligomeric beta-strand structure when associated with a lipid and cholesterol mixture close to that of membranes of host cells of the virus. In this study, this structure was further investigated using four different peptide constructs. In aqueous buffer solution, two of the constructs were primarily monomeric whereas the other two constructs had significant populations of oligomers/aggregates. NMR measurements for all membrane-associated peptide constructs were consistent with oligomeric beta-strand structure. Thus, constructs that are monomeric in solution can be converted to oligomers as a result of membrane association. In addition, samples prepared by very different methods had very similar NMR spectra, which indicates that the beta-strand structure is an equilibrium rather than a kinetically trapped structure. Lipid mixing assays were performed to assess the fusogenicities of the different constructs, and there was not a linear correlation between the solution oligomeric state and...Continue Reading

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Citations

Nov 27, 2007·European Biophysics Journal : EBJ·J OlleschD Langosch
Apr 8, 2014·Chemistry and Physics of Lipids·Beatriz ApellánizJosé L Nieva
Oct 20, 2007·Biochimica Et Biophysica Acta·Walter R P ScottSuzana K Straus
Jun 5, 2013·Biology·William J Allen, Robert C Rizzo
Nov 8, 2006·European Biophysics Journal : EBJ·Johannes ReichertAnne S Ulrich
Dec 4, 2012·Biochimica Et Biophysica Acta·Yechiel Shai
Dec 3, 2014·Archives of Biochemistry and Biophysics·Shin-Yi YangLong-Sen Chang
Sep 30, 2020·Viruses·Lauriane LecoqAnja Böckmann
Jul 3, 2007·Archives of Biochemistry and Biophysics·S MazziniI Haro

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