Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk.

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 Microbiol

journal_title

Trends in microbiology

authors

Russell CJ,Hu M,Okda FA

doi

10.1016/j.tim.2018.03.005

subject

Has Abstract

pub_date

2018-10-01 00:00:00

pages

841-853

issue

10

eissn

0966-842X

issn

1878-4380

pii

S0966-842X(18)30068-4

journal_volume

26

pub_type

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