Viral fusion proteins: multiple regions contribute to membrane fusion.
In recent years, the simple picture of a viral fusion protein interacting with the cell and/or viral membranes by means of only two localized segments (i.e. the fusion peptide and the transmembrane domain) has given way to a more complex picture in which multiple regions from the viral proteins interact with membranes. Indeed, possible roles in membrane binding and/or destabilization have been postulated for the N-terminal heptad repeats, pre-transmembrane segments, and other internal regions of fusion proteins from distant viruses (such as orthomyxo-, retro-, paramyxo-, or flaviviruses). This review focuses on the experimental evidence and functional models postulated so far about the role of these regions in the process of virus-induced membrane fusion.
Peisajovich
Sergio G
SG
Department of Biological Chemistry, The Weizmann Institute of Science, 76100, Rehovot, Israel.
Shai
Yechiel
Y
D000595:Amino Acid Sequence; D008561:Membrane Fusion; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D020449:Repetitive Sequences, Amino Acid; D016415:Sequence Alignment; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000378:metabolism*; D014780:Viruses / Q000472:pathogenicity
D014760:Viral Fusion Proteins