tetano
Editor, Senior Moderator
Glycobiology. 2017 Oct 26. doi: 10.1093/glycob/cwx092. [Epub ahead of print]
[h=1]NMR interaction studies of Neu5Ac-α-(2,6)-Gal-β-(1-4)-GlcNAc with influenza-virus Hemagglutinin expressed in transfected human cells.[/h] Vasile F[SUP]1[/SUP], Gubinelli F[SUP]2[/SUP], Panigada M[SUP]2[/SUP], Soprana E[SUP]2[/SUP], Siccardi A[SUP]2[/SUP], Potenza D[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The emergence of escape-mutants of Influenza Hemagglutinin 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 hemagglutinin 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 hemagglutinins (H1 and H5) from human and avian strains of influenza virus, directly expressed on the surface of stable transfected 293 T human cells. The hemagglutinins 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 hemagglutinin species. The rapid and reliable method for screening sialic acid-related hemagglutinin ligands we have developed could yield useful information for an efficient drug design.
? The Author 2017. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.
[h=4]KEYWORDS:[/h] STD-NMR spectroscopy; antiviral drug discovery; influenza-virus Hemagglutinin; ligand-protein interaction; transfected cells
PMID: 29087468 DOI: 10.1093/glycob/cwx092
[h=1]NMR interaction studies of Neu5Ac-α-(2,6)-Gal-β-(1-4)-GlcNAc with influenza-virus Hemagglutinin expressed in transfected human cells.[/h] Vasile F[SUP]1[/SUP], Gubinelli F[SUP]2[/SUP], Panigada M[SUP]2[/SUP], Soprana E[SUP]2[/SUP], Siccardi A[SUP]2[/SUP], Potenza D[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The emergence of escape-mutants of Influenza Hemagglutinin 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 hemagglutinin 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 hemagglutinins (H1 and H5) from human and avian strains of influenza virus, directly expressed on the surface of stable transfected 293 T human cells. The hemagglutinins 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 hemagglutinin species. The rapid and reliable method for screening sialic acid-related hemagglutinin ligands we have developed could yield useful information for an efficient drug design.
? The Author 2017. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.
[h=4]KEYWORDS:[/h] STD-NMR spectroscopy; antiviral drug discovery; influenza-virus Hemagglutinin; ligand-protein interaction; transfected cells
PMID: 29087468 DOI: 10.1093/glycob/cwx092