Virus Membrane Fusion Proteins: Biological Machines that Undergo a Metamorphosis
Authors: Ellis Dutch R.1; Jardetzky T.S.2; Lamb R.A.3
Source: Bioscience Reports, Volume 20, Number 6, December 2000 , pp. 597-612(16)
Publisher: Springer
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Abstract:
Fusion proteins from a group of widely disparate viruses, including the paramyxovirus F protein, the HIV and SIV gp160 proteins, the retroviral Env protein, the Ebola virus Gp, and the influenza virus haemagglutinin, share a number of common features. All contain multiple glycosylation sites, and must be trimeric and undergo proteolytic cleavage to be fusogenically active. Subsequent to proteolytic cleavage, the subunit containing the transmembrane domain in each case has an extremely hydrophobic region, termed the fusion peptide, or at near its newly generated N-terminus. In addition, all of these viral fusion proteins have 4–3 heptad repeat sequences near both the fusion peptide and the transmembrane domain. These regions have been demonstrated from a tight complex, in which the N-terminal heptad repeat forms a trimeric-coiled coil, with the C-terminal heptad repeat forming helical regions that buttress the coiled-coil in an anti-parallel manner. The significance of each of these structural elements in the processing and function of these viral fusion proteins is discussed.
Keywords: membrane fusion; viral glycoprotein; heptad repeats; proteolytic processing; glycosylation; oligomerization; fusion peptides
Language: English
Document Type: Regular paper
Affiliations: 1: Department of Biochemistry, University of Kentucky Medical Center, Lexington, Kentucky, 40536 2: Department of Biochemistry, Molecular Biology and Cell Biology 3: Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois, 60208–3500
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