Enhanced Human Receptor Binding by H5 Haemagglutinins

Xiong X, et al., 456-7:179-187, Virology, 2014

Structural and biochemical functional studies were performed on the virus membrane glycoprotein, Haemagglutinin (HA) as well as a number of H5 virus mutants isolated from humans in two geographically distinct regions to demonstrate the differences in receptor binding properties. Detailed binding studies were performed on the Octet RED system using Streptavidin biosensors to examine 12 different wildtype and mutant/double H5 mutant variants and further characterized using X-ray crystallography. Three specific substituted residues in the characterized mutants were shown to dramatically change the avidity for the human vs. avian receptor by affecting the receptor binding pocket as oppose to direct interaction with the receptor. These studies provide additional insight into the evolution of HA receptor binding properties during H5 virus infection of humans.

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