Ruonan Liang

This study examines the evolution of H1N1 influenza viruses over five decades, revealing conserved glycan receptor specificity despite amino acid changes in the hemagglutinin.

This study investigates how amino acid substitutions in H3N2 influenza A virus subclade K affect hemagglutination and glycan binding, showing a preference for elongated glycans not present on turkey erythrocytes.

This study characterizes the emergence and antigenic properties of influenza A(H3N2) viruses with N158K and K189R substitutions, showing they are antigenically distinct from vaccine strains and may reduce vaccine effectiveness.

The paper describes a chemoenzymatic method to synthesize O-acetylated GD3 gangliosides and uses them to study viral receptor specificities in a cellular context.

This study identifies epistatic interactions in H3N2 influenza viruses that enable reversion to bind sialylated diLacNAc glycans, impacting receptor specificity and vaccine strain selection.

The paper shows that a single Q226L mutation in the HA protein of a 2.3.4.4e H5 virus allows it to bind human-type receptors, unlike a modified 2.3.4.4b virus.