ArticleVirology2019
A conserved histidine in Group-1 influenza subtype hemagglutinin proteins is essential for membrane fusion activity.
Article in Virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Molecular Dynamics Investigation of the Influenza Hemagglutinin Conformational Changes in Acidic pH.The journal of physical chemistry. B · 2024Article
- Article
- Viral Membrane Fusion: A Dance Between Proteins and Lipids.Annual review of virology · 2023Review
- Epistasis reduces fitness costs of influenza A virus escape from stem-binding antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- pH-dependent endocytosis mechanisms for influenza A and SARS-coronavirus.Frontiers in microbiology · 2023Review
- Universal stabilization of the influenza hemagglutinin by structure-based redesign of the pH switch regions.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Univ-flu: A structure-based model of influenza A virus hemagglutinin for universal antigenic prediction.Computational and structural biotechnology journal · 2022Article
- Protein-sol pKa: prediction of electrostatic frustration, with application to coronaviruses.Bioinformatics (Oxford, England) · 2020Article
- Energy Landscape for the Membrane Fusion Pathway in Influenza A Hemagglutinin From Discrete Path Sampling.Frontiers in chemistry · 2020Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Influenza A viruses enter host cells through the endocytic pathway, where acidification triggers conformational changes of the viral hemagglutinin (HA) to drive membrane fusion. During this process, the HA fusion peptide is extruded from its buried position in the neutral pH structure and targeted to the endosomal membrane. Conserved ionizable residues near the fusion peptide may play a role in initiating these structural rearrangements. We targeted highly conserved histidine residues in this region, at HA1 position 17 of Group-2 HA subtypes and HA2 position 111 of Group-1 HA subtypes, to determine their role in fusion activity. WT and mutant HA proteins representing several subtypes were expressed and characterized, revealing that His 111 is essential for HA functional activity of Group-1 subtypes, supporting continued efforts to target this region of the HA structure for vaccination strategies and the design of antiviral compounds.
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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.