Structure and Receptor Complexes of the Hemagglutinin from a Highly Pathogenic H7N7 Influenza Virus

Yang, H., et al., 86(16), 8645-52, Journal of Virology, 2012

A H7N7 Influenza virus isolated from a fatal case (NL219) caused a lethal infection in mouse models. A mutation which introduces a potential glycosylation site in the NL219 hemagglutinin was postulated to contribute to its pathogenicity. Kinetic analysis were performed using Octet RED system to compare the receptor binding profiles of the wild-type recombinant NL219 hemagglutinin to a variant with a threonine-to-alanine mutation at position 125, resulting in loss of the glycosylation site. The results suggest that the additional glycosylation sequon increased binding affinity relative to avian-type a2-3-linked sialosides and not to human type a2-6-linked sialosides. The binding affinity was measured by immobilizing biotinylated glycans onto the Streptavidin Biosensor, and then dipping into recombinant hemagglutinin (WT and mutant versions).

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