Probing the receptor interactions of an H5 avian influenza virus using a baculovirus expression system and functionalised poly(acrylic acid) ligands

Barclay, W.S., Jones, I.M., Osborn, H.M.I. ORCID: https://orcid.org/0000-0002-0683-0457, Phillipson, L., Ren, J.Y., Talevera, G.A. and Thompson, C.I. (2007) Probing the receptor interactions of an H5 avian influenza virus using a baculovirus expression system and functionalised poly(acrylic acid) ligands. Bioorganic & Medicinal Chemistry, 15 (12). pp. 4038-4047. ISSN 0968-0896 doi: 10.1016/j.bmc.2007.03.085

Abstract/Summary

Influenza viruses attach to host cells by binding to terminal sialic acid (Neu5Ac) on glycoproteins or glycolipids. Both the linkage of Neu5Ac and the identity of other carbohydrates within the oligosaccharide are thought to play roles in restricting the host range of the virus. In this study, the receptor specificity of an H5 avian influenza virus haemagglutinin protein that has recently infected man (influenza strain A/Vietnam/1194/04) has been probed using carbohydrate functionalised poly(acrylic acid) polymers. A baculovirus expression system that allows facile and safe analysis of the Neu5Ac binding specificity of mutants of H5 HA engineered at sites that are predicted to effect a switch in host range has also been developed. (C) 2007 Elsevier Ltd. All rights reserved.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/13793
Item Type	Article
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy
Uncontrolled Keywords	sialic acid, carbohydrate, influenza, H5N1, STRONGLY INHIBIT AGGLUTINATION, HIGH BINDING-AFFINITY, SIALIC-ACID, CELLS, POLYACRYLAMIDES, HEMAGGLUTININ, SPECIFICITY, GLYCOCHEMISTRY, ERYTHROCYTES, DERIVATIVES
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