Influenza hemagglutinin protein stability, activation, and pandemic risk
Identifieur interne : 000185 ( Main/Exploration ); précédent : 000184; suivant : 000186Influenza hemagglutinin protein stability, activation, and pandemic risk
Auteurs : Charles J. Russell [États-Unis] ; Meng Hu [États-Unis] ; Faten A. Okda [États-Unis]Source :
- Trends in microbiology [ 0966-842X ] ; 2018.
Abstract
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, infectivity, transmissibility, and human pandemic potential. Here, we review HA protein structure, assays to measure its stability, measured HA stability values, residues and mutations that regulate its stability, the effect of HA stability on interspecies adaptation and transmissibility, and mechanistic insights into this process. Most importantly, HA stabilization appears to be necessary for adapting emerging influenza viruses to humans.
Url:
DOI: 10.1016/j.tim.2018.03.005
PubMed: 29681430
PubMed Central: 6150828
Affiliations:
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Okda</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Infectious Diseases, St. Jude Children’s Research Hospital, 262 Danny Thomas Place, Memphis, Tennessee 38105-3678</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Tennessee</region></placeName><wicri:cityArea>Department of Infectious Diseases, St. Jude Children’s Research Hospital, 262 Danny Thomas Place, Memphis</wicri:cityArea></affiliation></author></analytic><series><title level="j">Trends in microbiology</title><idno type="ISSN">0966-842X</idno><idno type="eISSN">1878-4380</idno><imprint><date when="2018">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P2">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, infectivity, transmissibility, and human pandemic potential. Here, we review HA protein structure, assays to measure its stability, measured HA stability values, residues and mutations that regulate its stability, the effect of HA stability on interspecies adaptation and transmissibility, and mechanistic insights into this process. 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