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Recognition of Sialylated Poly-N-acetyllactosamine Chains on N- and O-Linked Glycans by Human and Avian Influenza A Virus Hemagglutinins

tetano

Editor, Senior Moderator
Angew Chem Int Ed Engl. 2012 Apr 13. doi: 10.1002/anie.201200596. [Epub ahead of print]
Recognition of Sialylated Poly-N-acetyllactosamine Chains on N- and O-Linked Glycans by Human and Avian Influenza A Virus Hemagglutinins.
Nycholat CM, McBride R, Ekiert DC, Xu R, Rangarajan J, Peng W, Razi N, Gilbert M, Wakarchuk W, Wilson IA, Paulson JC.
Source

Department of Chemical Physiology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037 (USA).
Abstract

Human influenza viruses are proposed to recognize sialic acids (pink diamonds) on glycans extended with poly-LacNAc chains (LacNAc=(yellow circle+blue square)). N- and O-linked glycans were extended with different poly-LacNAc chains with α2-3 and α2-6-linked sialic acids recognized by human and avian influenza viruses, respectively. The specificity of recombinant hemagglutinins (receptors in green) was investigated using glycan microarray technology.

Copyright ? 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

PMID:
22505324
[PubMed - as supplied by publisher]

http://www.ncbi.nlm.nih.gov/pubmed/22505324
 
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