Cholesterol enhances influenza binding avidity by controlling nanoscale receptor clustering.

ABSTRACT: Influenza virus infects cells by binding to sialylated glycans on the cell surface. While the chemical structure of these glycans determines hemagglutinin-glycan binding affinity, bimolecular affinities are weak, so binding is avidity-dominated and driven by multivalent interactions. Here, we show that membrane spatial organization can control viral binding. Using single-virus fluorescence microscopy, we demonstrate that the sterol composition of the target membrane enhances viral binding avidity in a dose-dependent manner. Binding shows a cooperative dependence on concentration of receptors for influenza virus, as would be expected for a multivalent interaction. Surprisingly, the ability of sterols to promote viral binding is independent of their ability to support liquid-liquid phase sep

SUBMITTER: Goronzy IN 

PROVIDER: S-EPMC5839467 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature