Membrane fusion activity of influenza virus
- PMID: 7188182
- PMCID: PMC553023
- DOI: 10.1002/j.1460-2075.1982.tb01150.x
Membrane fusion activity of influenza virus
Abstract
A simple assay is described to monitor fusion between fowl plague virus (FPV, an avian influenza A virus) and liposomes which allows the simultaneous quantitation of both lytic and non-lytic fusion events. As in fusion between viruses and the plasma membrane and in FPV-induced cell-cell fusion, the reaction only occurs at pH 5.5 or below, and it is fast, highly efficient, and essentially non-lytic when fresh virus and liposomes are used. The fusion occurs over a broad temperature range, and has no requirement for divalent cations. The fusion factor of influenza virus is a hemagglutinin (HA) spike which protrudes from the virus membrane and which is also responsible for virus binding to the host cell. The finding that fusion occurs as efficiently with liposomes containing or lacking virus receptor structures, further emphasizes the remarkable division of labor in the HA molecule: the receptor-binding sites are located in the globular HA1 domains and the fusion activation peptide is found at the N-terminal of HA2 in the stem region of the protein. The mechanism of fusion is discussed in terms of the three-dimensional structure of the HA and the conformational change which the protein undergoes at the fusion pH optimum.
Similar articles
-
Membrane fusion activity of the influenza virus hemagglutinin. The low pH-induced conformational change.J Biol Chem. 1985 Mar 10;260(5):2973-81. J Biol Chem. 1985. PMID: 3972812
-
Fusion activity of influenza virus PR8/34 correlates with a temperature-induced conformational change within the hemagglutinin ectodomain detected by photochemical labeling.Biochemistry. 1991 Mar 5;30(9):2432-8. doi: 10.1021/bi00223a019. Biochemistry. 1991. PMID: 2001371
-
Evidence for H(+)-induced insertion of influenza hemagglutinin HA2 N-terminal segment into viral membrane.J Biol Chem. 1994 Jul 15;269(28):18353-8. J Biol Chem. 1994. PMID: 8034580
-
Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin.Annu Rev Biochem. 2000;69:531-69. doi: 10.1146/annurev.biochem.69.1.531. Annu Rev Biochem. 2000. PMID: 10966468 Review.
-
Receptor binding and pH stability - how influenza A virus hemagglutinin affects host-specific virus infection.Biochim Biophys Acta. 2014 Apr;1838(4):1153-68. doi: 10.1016/j.bbamem.2013.10.004. Epub 2013 Oct 24. Biochim Biophys Acta. 2014. PMID: 24161712 Review.
Cited by
-
Interplay between H1N1 influenza a virus infection, extracellular and intracellular respiratory tract pH, and host responses in a mouse model.PLoS One. 2021 May 12;16(5):e0251473. doi: 10.1371/journal.pone.0251473. eCollection 2021. PLoS One. 2021. PMID: 33979408 Free PMC article.
-
Host cell factors in filovirus entry: novel players, new insights.Viruses. 2012 Dec;4(12):3336-62. doi: 10.3390/v4123336. Viruses. 2012. PMID: 23342362 Free PMC article. Review.
-
Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis.J Virol. 2002 Oct;76(20):10455-64. doi: 10.1128/jvi.76.20.10455-10464.2002. J Virol. 2002. PMID: 12239322 Free PMC article.
-
Morphological changes and fusogenic activity of influenza virus hemagglutinin.Biophys J. 1998 Jan;74(1):54-62. doi: 10.1016/S0006-3495(98)77766-5. Biophys J. 1998. PMID: 9449309 Free PMC article.
-
Influenza virus-mediated membrane fusion: Structural insights from electron microscopy.Arch Biochem Biophys. 2015 Sep 1;581:86-97. doi: 10.1016/j.abb.2015.04.011. Epub 2015 May 6. Arch Biochem Biophys. 2015. PMID: 25958107 Free PMC article. Review.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous