Robert P. de Vries

This paper synthesizes 6-sulfo sialyl Lewisx glycans to identify MERS-CoV's preferred receptor and develops a multivalent inhibitor.

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 uses self-assembling nanoparticles to investigate how multivalent HA binding affects influenza virus interaction with glycan surfaces, finding that valency and receptor density significantly influence binding strength and mode.

This study compares the pathogenicity and transmissibility of two H5N1 genotypes in ferrets, finding B3.13 is more pathogenic and transmissible than D1.1, while D1.1 acquires adaptive mutations rapidly.

This study shows that multiple mutations, not just Q226L, are required for H5N1 hemagglutinin to bind human respiratory tract tissue, highlighting the complexity of receptor specificity evolution.

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.

The paper shows that E190D and Q226H mutations in H5N1 HA reduce sialic acid binding across multiple H5 backgrounds.

This study shows avian IAVs preferentially bind ciliated cells but replicate similarly in secretory and ciliated cells, while human IAVs bind ciliated cells but replicate more efficiently in secretory cells due to ANP32 usage.

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.

This study identifies that H5Nx influenza A viruses bind promiscuously to avian-type mucin-like O-glycans, enhancing their zoonotic potential by binding human tracheal tissues.

This study examines how glycan evolution in H3 hemagglutinin affects antigenicity and immunogenicity, showing reduced antibody binding and shifted immune response.

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 a monoclonal antibody that neutralizes HCoV-HKU1 by mimicking sialic acid binding to block receptor engagement.

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

This study identifies sialic acid-containing glycolipids as novel receptors for EV-D68 and shows that different strains prefer distinct sialic acid linkages.

The paper characterizes glycoproteins of novel fish influenza B-like viruses, revealing differences in receptor binding and antigenic conservation compared to influenza B viruses.

The paper examines the receptor-binding specificity of a bovine HPAI H5N1 virus using multiple assays and finds it preferentially binds avian-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 study identifies receptor distribution in cow and goat mammary and respiratory tracts for avian H5 influenza viruses, showing H5 proteins from cow isolates bind mammary glands while classical H5 proteins do not.

This paper introduces GLOVID, a biosensor platform that detects intact respiratory viruses by reconstituting split luciferase, achieving ultrasensitive detection of influenza A and RSV.

The paper develops fluorescent protein fusions to study receptor binding of viral envelope proteins in cells.

This study shows that NeuGc-adapted H7 IAVs can bind sialyl-LewisX, enabling replication in chickens and ducks despite lacking NeuGc receptors.

This paper identifies 9-O-acetylated sialic acids as a ligand for the SARS-CoV-2 NTD, revealing a dual-receptor functionality in the S1 domain that was rapidly selected against.

The paper investigates how avian H7 influenza A viruses can bind NeuGc through specific mutations, revealing insights into viral adaptation to NeuGc receptors.

The paper demonstrates that fully glycosylated trimeric RBD proteins of SARS-CoV-2 bind more effectively to ACE2 compared to monomeric or immaturely glycosylated variants.