Virus-cell and cell-cell fusion
- PMID: 8970739
- DOI: 10.1146/annurev.cellbio.12.1.627
Virus-cell and cell-cell fusion
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
-
Entry of rhabdoviruses into animal cells.Adv Exp Med Biol. 2013;790:167-77. doi: 10.1007/978-1-4614-7651-1_9. Adv Exp Med Biol. 2013. PMID: 23884591 Free PMC article. Review.
-
Inhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: role of a conserved hydrophobic cavity in membrane fusion.J Virol. 1999 Oct;73(10):8578-86. doi: 10.1128/JVI.73.10.8578-8586.1999. J Virol. 1999. PMID: 10482611 Free PMC article.
-
Analysis of the pH requirement for membrane fusion of different isolates of the paramyxovirus parainfluenza virus 5.J Virol. 2006 Mar;80(6):3071-7. doi: 10.1128/JVI.80.6.3071-3077.2006. J Virol. 2006. PMID: 16501116 Free PMC article.
-
Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core.J Biol Chem. 2004 Nov 19;279(47):49414-9. doi: 10.1074/jbc.M408782200. Epub 2004 Sep 1. J Biol Chem. 2004. PMID: 15345712 Free PMC article.
-
HIV-1 membrane fusion: targets of opportunity.J Cell Biol. 2000 Oct 16;151(2):F9-14. doi: 10.1083/jcb.151.2.f9. J Cell Biol. 2000. PMID: 11038194 Free PMC article. No abstract available.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources