RESOLVING EXTENDED N‐GLYCANS BY NMR: NEW INSIGHTS INTO INFLUENZA HEMAGGLUTININ N‐GLYCAN INTERACTIONS

Abstract

Seasonal flu (influenza virus infection) is one of the major threats to human health, causing of up to 500 thousands deaths worldwide annually.1,2 Hemagglutinin, a glycoprotein presented in the surface of the influenza virus, binds sialylated N‐glycans located on the surface of host epithelial cells.The structural elucidation and the conformational studies of N‐glycans remain a challenge due to the complexity, heterogeneity and flexibility of carbohydrates. Moreover, the isochronous chemical shifts presented for the same units located at different branches make impossible the distinction of their signals in the NMR spectra.Taking advantage of the lanthanide approach, an unambiguous assignment of each carbohydrate unit has been reached for bianntenary N‐glycans containing one and two LacNAc units, permitting their conformational elucidation and the recognition study of these N‐glycans by the HK/68 hemagglutinin strain.Support or Funding InformationThis research was financially supported by funding from Spanish government, MINECO, projects: CTQ2016‐76263‐P, CTQ2015‐64597‐C2‐1‐P and CTQ2015‐64597‐C2‐2‐P and FPI fellowship.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.