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Research
Nature Biotechnology 26, 107–113 (1 January 2008) | doi:10.1038/nbt1375
Glycan topology determines human adaptation of avian H5N1 virus hemagglutinin
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Abstract
A switch in specificity of avian influenza A viruses' hemagglutinin (HA) from avian-like (α2-3 sialylated glycans) to human-like (α2-6 sialylated glycans) receptors is believed to be associated with their adaptation to infect humans. We show that a characteristic structural topology—and not the α2-6 linkage itself—enables specific binding of HA to α2-6 sialylated glycans and that recognition of this topology may be critical for adaptation of HA to bind glycans in the upper respiratory tract of humans.
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