ArticleEuropean biophysics journal : EBJ2007
Conformational change of influenza virus hemagglutinin is sensitive to ionic concentration.
Article in European biophysics journal : EBJ, 2007. 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, 18 citations in OpenAlex.
- Influenza Hemagglutinin Structures and Antibody Recognition.Cold Spring Harbor perspectives in medicine · 2020Review
- Identification of a pH sensor in Influenza hemagglutinin using X-ray crystallography.Journal of structural biology · 2020Article
- Inhibition of influenza virus activity by the bovine seminal plasma protein PDC-109.European biophysics journal : EBJ · 2019Article
- Phosphatidylserine Lateral Organization Influences the Interaction of Influenza Virus Matrix Protein 1 with Lipid Membranes.Journal of virology · 2017Article
- Modulation of the pH Stability of Influenza Virus Hemagglutinin: A Host Cell Adaptation Strategy.Biophysical journal · 2016Review
- Article
- Role of electrostatic repulsion in controlling pH-dependent conformational changes of viral fusion proteins.Structure (London, England : 1993) · 2013Review
- Article
- Influenza virus-membrane fusion triggered by proton uncaging for single particle studies of fusion kinetics.Analytical chemistry · 2012Article
- Bending and puncturing the influenza lipid envelope.Biophysical journal · 2011Article
- Development of stable influenza vaccine powder formulations: challenges and possibilities.Pharmaceutical research · 2008Review
- Crystal structure of unliganded influenza B virus hemagglutinin.Journal of virology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The homotrimeric spike glycoprotein hemagglutinin (HA) of influenza virus undergoes a low pH-mediated conformational change which mediates the fusion of the viral envelope with the target membrane. Previous approaches predict that the interplay of electrostatic interactions between and within HA subunits, HA 1 and HA2, are essential for the metastability of the HA ectodomain. Here, we show that suspension media of low ionic concentration promote fusion of fluorescent labelled influenza virus X31 with erythrocyte ghosts and with ganglioside containing liposomes. By measuring the low pH mediated inactivation of the fusion competence of HA and the Proteinase K sensitivity of low pH incubated HA we show that the conformational change is promoted by low ionic concentration. We surmise that electrostatic attraction within the HA ectodomain is weakened by lowering the ionic concentration facilitating the conformational change at low pH.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.