NMR interaction studies of Neu5Ac-α-(2,6)-Gal-β-(1-4)-GlcNAc with influenza-virus hemagglutinin expressed in transfected human cells

Glycobiology
Francesca VasileDonatella Potenza

Abstract

The emergence of escape-mutants of influenza hemagglutinin (HA) following vaccination compels the yearly re-formulation of flu vaccines. Since binding the sialic acid receptor remains in all cases essential for infection, small-molecule inhibitors of HA binding to sialic acid could be interesting therapeutic complements or alternatives to immuno-prophylaxis in the control of flu epidemics. In this work, we made use of NMR spectroscopy to study the interaction between a derivative of sialic acid (the Neu5Ac-α-(2,6)-Gal-β-(1-4)-GlcNAc trisaccharide) and HAs (H1 and H5) from human and avian strains of influenza virus, directly expressed on the surface of stable transfected 293 T human cells. The HAs were shown to retain their native trimeric conformation and binding properties. Exploiting the magnetization transfer between the proteins and the ligand, we obtained evidence of the binding event and mapped the (non-identical) sugar epitopes recognized by the two HA species. The rapid and reliable method for screening sialic acid-related HA ligands we have developed could yield useful information for an efficient drug design.

References

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Citations

Jun 4, 2019·PLoS Computational Biology·Monica CiveraLaura Belvisi
Jul 6, 2021·Journal of Medicinal Chemistry·Francesca Alessandra AmbrosioSimona Collina
Apr 19, 2019·ACS Medicinal Chemistry Letters·Serena Della VolpeSimona Collina
May 5, 2021·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Trần Thanh Tâm Phạm, Jan K Rainey

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