Comparison of COVA1-16 binding mode with CR3022 and ACE2. (A) Crystal structure of COVA1-16/RBD complex with RBD in grey and COVA1-16 Fab in cyan (heavy chain) and greyish blue (light chain).

The study authors focused on altering one of H5N1’s surface proteins, hemagglutinin, which contains the binding site that allows the virus to latch onto host cell receptors and kick-start infection.

G protein-coupled receptors (GPCRs) are intrinsically allosteric proteins. Through spatially distinct, but conformationally linked, binding sites they have evolved to transduce signals from one ...

“Binding to human-type receptors is not the only factor that is required for an avian flu virus to replicate well in humans,” said Kawaoka, a leading influenza virologist at the University of ...