Protein Science, Vol 1, Issue 11 1454-1464, Copyright © 1992 by Cold Spring Harbor Laboratory Press

ARTICLE

A molecular model for membrane fusion based on solution studies of an amphiphilic peptide from HIV gp41

G. FUJII, S. HORVATH, S. WOODWARD, F. EISERLING and D. EISENBERG
Molecular Biology Institute and Departments of Chemistry and Biochemistry, University of California, Los Angels, California 90024-1570 Vestar, Inc., San Dimas, California 91773

The mechanism of protein-mediated membrane fusion and lysis has been investigated by solution-state studies of the effects of peptides on liposomes. A peptide (SI) corresponding to a highly amphiphilic C-terminal segment from the envelope protein (gp41) of the human immunodeficiency virus (HIV) was synthesized and tested for its ability to cause lipid membranes to fuse together (fusion) or to break open (lysis). These effects were compared to those produced by the lytic and fusogenic peptide from bee venom, melittin. Other properties studied included the changes in visible absorbance and mean particle size, and the secondary structure of peptides as judged by CD spectroscopy. Taken together, the observations suggest that protein-mediated membrane fusion is dependent not only on hydrophobic and electrostatic forces but also on the spatial arrangement of the amino acid residues to form an amphiphilic structure that promotes the mixing of the lipids between membranes. A speculative molecular model is proposed for membrane fusion by {alpha}-helical peptides, and its relationship to the forces involved in protein-membrane interactions is discussed.
CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				S. S.-L. Chen, S.-F. Lee, and C.-T. Wang Cellular Membrane-Binding Ability of the C-Terminal Cytoplasmic Domain of Human Immunodeficiency Virus Type 1 Envelope Transmembrane Protein gp41 J. Virol., October 15, 2001; 75(20): 9925 - 9938. [Abstract] [Full Text] [PDF]

				B. A. Rabinovich, J. Shannon, R.-C. Su, and R. G. Miller Stress Renders T Cell Blasts Sensitive to Killing by Activated Syngeneic NK Cells J. Immunol., September 1, 2000; 165(5): 2390 - 2397. [Abstract] [Full Text] [PDF]

				S. B. Tencza, D. J. Creighton, T. Yuan, H. J. Vogel, R. C. Montelaro, and T. A. Mietzner Lentivirus-derived antimicrobial peptides: increased potency by sequence engineering and dimerization J. Antimicrob. Chemother., July 1, 1999; 44(1): 33 - 41. [Abstract] [Full Text] [PDF]

				S.-F. Lee, C.-T. Wang, J. Y.-P. Liang, S.-L. Hong, C.-C. Huang, and S. S.-L. Chen Multimerization Potential of the Cytoplasmic Domain of the Human Immunodeficiency Virus Type 1 Transmembrane Glycoprotein gp41 J. Biol. Chem., May 19, 2000; 275(21): 15809 - 15819. [Abstract] [Full Text] [PDF]

				Y. Kliger, S. A. Gallo, S. G. Peisajovich, I. Munoz-Barroso, S. Avkin, R. Blumenthal, and Y. Shai Mode of Action of an Antiviral Peptide from HIV-1. INHIBITION AT A POST-LIPID MIXING STAGE J. Biol. Chem., January 5, 2001; 276(2): 1391 - 1397. [Abstract] [Full Text] [PDF]