Virion-associated influenza hemagglutinin clusters upon sialic acid binding visualized by cryoelectron tomography.

ABSTRACT: Influenza viruses are enveloped, negative-sense single-stranded RNA viruses covered in a dense layer of glycoproteins. Hemagglutinin (HA) accounts for 80 to 90% of influenza glycoprotein and plays a role in host cell binding and membrane fusion. While previous studies have characterized structures of purified receptor-free and receptor-bound HA, the effect of receptor binding on HA organization and structure on virions remains unknown. Here, we used cryoelectron tomography to visualize influenza virions bound to a sialic acid receptor mimic. Overall, receptor binding did not result in significant changes in viral morphology; however, we observed rearrangements of HA trimer organization and orientation. Compared to the even interglycoprotein spacing of unliganded HA trimers, receptor bindin

SUBMITTER: Huang QJ 

PROVIDER: S-EPMC12037027 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature