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

被引：11

作者：

Barclay, Wendy S.

Jones, Ian M.

Osborn, Helen M. I. ^{[1
]}

Phillipson, Louisa

Ren, Junyuan

Talevera, Guadalupe A.

Thompson, Catherine I.

机构：

[1] Univ Reading, Sch Pharm, Reading RG6 6AD, Berks, England

[2] Univ Reading, Sch Chem, Reading RG6 6AD, Berks, England

[3] Univ Reading, Sch Biol Sci, Reading RG6 6AJ, Berks, England

来源：

BIOORGANIC & MEDICINAL CHEMISTRY | 2007年 / 15卷 / 12期

基金：

英国医学研究理事会;

关键词：

sialic acid; carbohydrate; influenza; H5N1;

D O I：

10.1016/j.bmc.2007.03.085

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：4038 / 4047

页数：10

共 42 条

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