Literature DB >> 24559987

Stochastic fusion simulations and experiments suggest passive and active roles of hemagglutinin during membrane fusion.

Donald W Lee1, Vikram Thapar1, Paulette Clancy1, Susan Daniel2.   

Abstract

Influenza enters the host cell cytoplasm by fusing the viral and host membrane together. Fusion is mediated by hemagglutinin (HA) trimers that undergo conformational change when acidified in the endosome. It is currently debated how many HA trimers, w, and how many conformationally changed HA trimers, q, are minimally required for fusion. Conclusions vary because there are three common approaches for determining w and q from fusion data. One approach correlates the fusion rate with the fraction of fusogenic HA trimers and leads to the conclusion that one HA trimer is required for fusion. A second approach correlates the fusion rate with the total concentration of fusogenic HA trimers and indicates that more than one HA trimer is required. A third approach applies statistical models to fusion rate data obtained at a single HA density to establish w or q and suggests that more than one HA trimer is required. In this work, all three approaches are investigated through stochastic fusion simulations and experiments to elucidate the roles of HA and its ability to bend the target membrane during fusion. We find that the apparent discrepancies among the results from the various approaches may be resolved if nonfusogenic HA participates in fusion through interactions with a fusogenic HA. Our results, based on H3 and H1 serotypes, suggest that three adjacent HA trimers and one conformationally changed HA trimer are minimally required to induce membrane fusion (w = 3 and q = 1).
Copyright © 2014 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2014        PMID: 24559987      PMCID: PMC3944606          DOI: 10.1016/j.bpj.2013.12.048

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  57 in total

1.  A quantitative model for membrane fusion based on low-energy intermediates.

Authors:  P I Kuzmin; J Zimmerberg; Y A Chizmadzhev; F S Cohen
Journal:  Proc Natl Acad Sci U S A       Date:  2001-06-12       Impact factor: 11.205

2.  Estimation by radiation inactivation of the size of functional units governing Sendai and influenza virus fusion.

Authors:  K Bundo-Morita; S Gibson; J Lenard
Journal:  Biochemistry       Date:  1987-09-22       Impact factor: 3.162

3.  How many trimers? Modeling influenza virus fusion yields a minimum aggregate size of six trimers, three of which are fusogenic.

Authors:  Maria Pamela Dobay; Akos Dobay; Johnrob Bantang; Eduardo Mendoza
Journal:  Mol Biosyst       Date:  2011-07-08

4.  Radiation inactivation analysis of influenza virus reveals different target sizes for fusion, leakage, and neuraminidase activities.

Authors:  S Gibson; C Y Jung; M Takahashi; J Lenard
Journal:  Biochemistry       Date:  1986-10-07       Impact factor: 3.162

Review 5.  The structure and function of the hemagglutinin membrane glycoprotein of influenza virus.

Authors:  D C Wiley; J J Skehel
Journal:  Annu Rev Biochem       Date:  1987       Impact factor: 23.643

6.  Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus.

Authors:  M J Gething; R W Doms; D York; J White
Journal:  J Cell Biol       Date:  1986-01       Impact factor: 10.539

7.  An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids.

Authors:  L V Chernomordik; E Leikina; V Frolov; P Bronk; J Zimmerberg
Journal:  J Cell Biol       Date:  1997-01-13       Impact factor: 10.539

8.  Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.

Authors:  T Danieli; S L Pelletier; Y I Henis; J M White
Journal:  J Cell Biol       Date:  1996-05       Impact factor: 10.539

9.  Cryotomography of budding influenza A virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal end.

Authors:  Swetha Vijayakrishnan; Colin Loney; David Jackson; Worawit Suphamungmee; Frazer J Rixon; David Bhella
Journal:  PLoS Pathog       Date:  2013-06-06       Impact factor: 6.823

10.  Effects of spontaneous bilayer curvature on influenza virus-mediated fusion pores.

Authors:  V I Razinkov; G B Melikyan; R M Epand; R F Epand; F S Cohen
Journal:  J Gen Physiol       Date:  1998-10       Impact factor: 4.086

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Journal:  Adv Exp Med Biol       Date:  2019       Impact factor: 2.622

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Authors:  Donald W Lee; Hung-Lun Hsu; Kaitlyn B Bacon; Susan Daniel
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6.  Viral fusion efficacy of specific H3N2 influenza virus reassortant combinations at single-particle level.

Authors:  Hung-Lun Hsu; Jean K Millet; Deirdre A Costello; Gary R Whittaker; Susan Daniel
Journal:  Sci Rep       Date:  2016-10-18       Impact factor: 4.379

  6 in total

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