Structural dynamics reveal subtype-specific activation and inhibition of influenza virus hemagglutinin.

ABSTRACT: Influenza hemagglutinin (HA) is a prototypical class 1 viral entry glycoprotein, responsible for mediating receptor binding and membrane fusion. Structures of its prefusion and postfusion forms, embodying the beginning and endpoints of the fusion pathway, have been extensively characterized. Studies probing HA dynamics during fusion have begun to identify intermediate states along the pathway, enhancing our understanding of how HA becomes activated and traverses its conformational pathway to complete fusion. HA is also the most variable, rapidly evolving part of influenza virus, and it is not known whether mechanisms of its activation and fusion are conserved across divergent viral subtypes. Here, we apply hydrogen-deuterium exchange mass spectrometry to compare fusion activation in two su

SUBMITTER: Garcia NK 

PROVIDER: S-EPMC10220487 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature