ArticleBiophysical journal2000
Delay of influenza hemagglutinin refolding into a fusion-competent conformation by receptor binding: a hypothesis.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- CD4 Incorporation into HIV-1 Viral Particles Exposes Envelope Epitopes Recognized by CD4-Induced Antibodies.Journal of virology · 2019Article
- A "building block" approach to the new influenza A virus entry inhibitors with reduced cellular toxicities.Scientific reports · 2016Article
- Wild-type and mutant hemagglutinin fusion peptides alter bilayer structure as well as kinetics and activation thermodynamics of stalk and pore formation differently: mechanistic implications.Biophysical journal · 2013Article
- Influenza virus entry.Advances in experimental medicine and biology · 2012Review
- Hemagglutinin fusion peptide mutants in model membranes: structural properties, membrane physical properties, and PEG-mediated fusion.Biophysical journal · 2011Article
- Heterogeneity of early intermediates in cell-liposome fusion mediated by influenza hemagglutinin.Biophysical journal · 2006Article
- Properties and structures of the influenza and HIV fusion peptides on lipid membranes: implications for a role in fusion.Biophysical journal · 2005Article
- Measuring pKa of activation and pKi of inactivation for influenza hemagglutinin from kinetics of membrane fusion of virions and of HA expressing cells.Biophysical journal · 2002Article
- Functional motions of influenza virus hemagglutinin: a structure-based analytical approach.Biophysical journal · 2002Article
- Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machines.The Journal of cell biology · 2001Article
- Stochastic simulation of hemagglutinin-mediated fusion pore formation.Biophysical journal · 2001Article
- Comprehensive kinetic analysis of influenza hemagglutinin-mediated membrane fusion: role of sialate binding.Biophysical journal · 2001Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two subunits of influenza hemagglutinin (HA), HA1 and HA2, represent one of the best-characterized membrane fusion machines. While a low pH conformation of HA2 mediates the actual fusion, HA1 establishes a specific connection between the viral and cell membranes via binding to the sialic acid-containing receptors. Here we propose that HA1 may also be involved in modulating the kinetics of HA refolding. We hypothesized that binding of the HA1 subunit to its receptor restricts the major refolding of the low pH-activated HA to a fusion-competent conformation and, in the absence of fusion, to an HA-inactivated state. Dissociation of the HA1-receptor connection was considered to be a slow kinetic step. To verify this hypothesis, we first analyzed a simple kinetic scheme accounting for the stages of dissociation of the HA1/receptor bonds, inactivation and fusion, and formulated experimentally testable predictions. Second, we verified these predictions by measuring the extent of fusion between HA-expressing cells and red blood cells. Three experimental approaches based on 1) the temporal inhibition of fusion by lysophosphatidylcholine, 2) rapid dissociation of the HA1-receptor connections by neuraminidase treatment, and 3) substitution of membrane-anchored receptors by a water-soluble sialyllactose all provided support for the proposed role of the release of HA1-receptor connections. Possible biological implications of this stage in HA refolding and membrane fusion are being discussed.
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