John J. Skehel

TL;DR: X-ray diffraction studies yielded 3 A resolution crystal structures of hemagglutinin in complex with four of the synthetic analogs and with the naturally occurring cell-surface saccharide (alpha 2-3)sialyllactose, which could lead to the design of tight binding inhibitors of possible therapeutic value.

TL;DR: It is indicated that the HA2 conformation in viral HA before low pH activation of its fusion potential is metastable and suggested that removal of the receptor-binding chain (HA1) is enough to allow HA2 to adopt the stable state.

TL;DR: Three series of compounds are synthesized, each containing two sialic acid residues separated by spacers of different length, and tested as ligands for influenza hemagglutinin, showing 100-fold increased affinity for whole virus over the paradigm monovalent ligand, Neu5Ac alpha 2Me.

TL;DR: X-ray crystal structures have been determined for several complexes between influenza virus hemagglutinin and derivatives of its cell-surface receptor, sialic acid, and establish the existence of a second binding site in addition to the primary site characterized previously.

TL;DR: The neutral pH crystal structure of one such mutant HAs from mutant viruses with raised fusion pH optima is determined, and it appears that four intra‐chain hydrogen bonds that stabilize the location of the N‐terminus of HA2 are lost in the mutant, resulting in a local destabilization that facilitates the extrusion of theN‐ terminus at higher pH.