期刊
CELL
卷 174, 期 4, 页码 926-+出版社
CELL PRESS
DOI: 10.1016/j.cell.2018.05.050
关键词
-
资金
- NIH [DP2 AI124384, K22 AI116262]
- Gilead Sciences Research Scholars Program
- NIAID Centers for Excellence in Influenza Virus Research and Surveillance program (CEIRS) [HHSN272201400008C]
Influenza hemagglutinin (HA) is the canonical type I viral envelope glycoprotein and provides a template for the membrane-fusion mechanisms of numerous viruses. The current model of HA-mediated membrane fusion describes a static spring-loaded fusion domain (HA2) at neutral pH. Acidic pH triggers a singular irreversible conformational rearrangement in HA2 that fuses viral and cellular membranes. Here, pH-triggered conformational changes of HA trimers on the viral surface. Our analyses reveal reversible exchange between the pre-fusion and two intermediate conformations of HA2. Acidification of pH and receptor binding shifts the dynamic equilibrium of HA2 in favor of forward progression along the membrane-fusion reaction coordinate. Interaction with the target membrane promotes irreversible transition of HA2 to the post-fusion state. The reversibility of HA2 conformation may protect against transition to the post-fusion state prior to arrival at the target membrane.
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