Ruonan Liang

Five decades of human H1N1 evolution reveal conserved glycan receptor specificity

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

Loss of hemagglutination ability by H3N2 influenza A virus, subclade K.

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.

Emergence and antigenic characterisation of influenza A(H3N2) viruses with hemagglutinin substitutions N158K and K189R during the 2024/25 influenza season

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.

Chemoenzymatically Synthesized O-Acetylated GD3 Gangliosides to Examine Viral Receptor Specificities in a Cellular Context

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

Epistasis in the receptor binding domain of contemporary H3N2 viruses that reverted to bind sialylated diLacNAc repeats

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 Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors

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.

The HCoV-HKU1 N-terminal domain binds a wide range of 9-O-acetylated sialic acids presented on different glycan cores