Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk.

doi:10.1016/j.tim.2018.03.005

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Article

Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk.

Trends in microbiology - 1 Oct 2018

Russell Charles J, Hu Meng, Okda Faten A

Abstract excerpt

For decades, hemagglutinin (HA) protein structure and its refolding mechanism have served as a paradigm for understanding protein-mediated membrane fusion. HA trimers are in a high-energy state and are functionally activated by low pH. Over the past decade, HA stability (or the pH at which irreversible conformational changes are triggered) has emerged as an important determinant in influenza virus host range,...

Topics

Animals
Ferrets
Hemagglutinin Glycoproteins, Influenza Virus
Humans
Hydrogen-Ion Concentration
Influenza A Virus, H1N1 Subtype
Influenza, Human
Membrane Fusion
Mutation
Orthomyxoviridae Infections
Pandemics
Protein Stability
Protein Structure, Tertiary
Virus Internalization

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Identifiers

PMID: 29681430
DOI: 10.1016/j.tim.2018.03.005
PMCID: PMC6150828

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