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.
journal_name
Trends Microbioljournal_title
Trends in microbiologyauthors
Russell CJ,Hu M,Okda FAdoi
10.1016/j.tim.2018.03.005subject
Has Abstractpub_date
2018-10-01 00:00:00pages
841-853issue
10eissn
0966-842Xissn
1878-4380pii
S0966-842X(18)30068-4journal_volume
26pub_type
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