Review
doi: 10.1146/annurev.cellbio.12.1.627.
Virus-cell and cell-cell fusion
Affiliations
- PMID: 8970739
- DOI: 10.1146/annurev.cellbio.12.1.627
Item in Clipboard
Review
Virus-cell and cell-cell fusion
Annu Rev Cell Dev Biol.
1996.
Abstract
Significant progress has been made in elucidating the mechanisms of viral membrane fusion proteins; both those that function at low, as well as those that function at neutral, pH. For many viral fusion proteins evidence now suggests that a triggered conformational change that exposes a previously cryptic fusion peptide, along with a rearrangement of the fusion protein oligomer, allows the fusion peptide to gain access to the target bilayer and thus initiate the fusion reaction. Although the topologically equivalent process of cell-cell fusion is less well understood, several cell surface proteins, including members of the newly described ADAM gene family, have emerged as candidate adhesion/fusion proteins.
Similar articles
-
Peptide models for the membrane destabilizing actions of viral fusion proteins.Biopolymers. 1992 Apr;32(4):309-14. doi: 10.1002/bip.360320403. Biopolymers. 1992. PMID: 1623124
-
Attenuation of recombinant vesicular stomatitis viruses encoding mutant glycoproteins demonstrate a critical role for maintaining a high pH threshold for membrane fusion in viral fitness.Virology. 1998 Jan 20;240(2):349-58. doi: 10.1006/viro.1997.8921. Virology. 1998. PMID: 9454708
-
The Role of histidine residues in low-pH-mediated viral membrane fusion.Structure. 2006 Oct;14(10):1481-7. doi: 10.1016/j.str.2006.07.011. Structure. 2006. PMID: 17027497 Review.
-
Conformational changes in Sindbis virions resulting from exposure to low pH and interactions with cells suggest that cell penetration may occur at the cell surface in the absence of membrane fusion.Virology. 2004 Jul 1;324(2):373-86. doi: 10.1016/j.virol.2004.03.046. Virology. 2004. PMID: 15207623
-
The mechanisms of lipid-protein rearrangements during viral infection.Bioelectrochemistry. 2004 Jun;63(1-2):129-36. doi: 10.1016/j.bioelechem.2003.10.016. Bioelectrochemistry. 2004. PMID: 15110263 Review.
Cited by
-
The receptor attachment function of measles virus hemagglutinin can be replaced with an autonomous protein that binds Her2/neu while maintaining its fusion-helper function.J Virol. 2013 Jun;87(11):6246-56. doi: 10.1128/JVI.03298-12. Epub 2013 Mar 27. J Virol. 2013. PMID: 23536664 Free PMC article.
-
pH-Dependent lytic peptides discovered by phage display.Biochemistry. 2006 May 23;45(20):6476-87. doi: 10.1021/bi052488s. Biochemistry. 2006. PMID: 16700558 Free PMC article.
-
Ultrastructural characterization of peptide-induced membrane fusion and peptide self-assembly in the lipid bilayer.Biophys J. 1999 Aug;77(2):829-41. doi: 10.1016/S0006-3495(99)76935-3. Biophys J. 1999. PMID: 10423429 Free PMC article.
-
Identification of linear heparin-binding peptides derived from human respiratory syncytial virus fusion glycoprotein that inhibit infectivity.J Virol. 2007 Jan;81(1):261-71. doi: 10.1128/JVI.01226-06. Epub 2006 Oct 18. J Virol. 2007. PMID: 17050595 Free PMC article.
-
A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3.Nat Med. 2000 Jan;6(1):35-40. doi: 10.1038/71503. Nat Med. 2000. PMID: 10613821 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
