María Ríos Carrasco

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 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.

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

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.

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 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.