Glycan topology determines human adaptation of avian H5N1 virus hemagglutinin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2008-01

AUTHORS

Aarthi Chandrasekaran, Aravind Srinivasan, Rahul Raman, Karthik Viswanathan, S Raguram, Terrence M Tumpey, V Sasisekharan, Ram Sasisekharan

ABSTRACT

A switch in specificity of avian influenza A viruses' hemagglutinin (HA) from avian-like (alpha2-3 sialylated glycans) to human-like (alpha2-6 sialylated glycans) receptors is believed to be associated with their adaptation to infect humans. We show that a characteristic structural topology--and not the alpha2-6 linkage itself--enables specific binding of HA to alpha2-6 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. An integrated biochemical, analytical and data mining approach demonstrates that HAs from the human-adapted H1N1 and H3N2 viruses, but not H5N1 (bird flu) viruses, specifically bind to long alpha2-6 sialylated glycans with this topology. This could explain why H5N1 viruses have not yet gained a foothold in the human population. Our findings will enable the development of additional strategies for effective surveillance and potential therapeutic interventions for H5N1 and possibly other influenza A viruses. More... »

PAGES

107-113

Journal

TITLE

Nature Biotechnology

ISSUE

1

VOLUME

26

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nbt1375

DOI

http://dx.doi.org/10.1038/nbt1375

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1018691185

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/18176555


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