Recognition of the GM3 Ganglioside Glycan by Rhesus Rotavirus Particles

被引：37

作者：

Haselhorst, Thomas ^{[1
]}

Fiebig, Timm ^{[1
]}

Dyason, Jeffrey C. ^{[1
]}

Fleming, Fiona E. ^{[2
]}

Blanchard, Helen ^{[1
]}

Coulson, Barbara S. ^{[2
]}

von Itzstein, Mark ^{[1
]}

机构：

[1] Griffith Univ, Inst Glyc, Nathan, Qld 4222, Australia

[2] Univ Melbourne, Dept Microbiol & Immunol, Parkville, Vic 3010, Australia

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2011年 / 50卷 / 05期

基金：

英国医学研究理事会; 澳大利亚研究理事会;

关键词：

gangliosides; rotaviruses; sialic acids; STD NMR spectroscopy; STD NMR-SPECTROSCOPY; SIALIC-ACID BINDING; LIGAND-BINDING; VIRUS; VP4; VP8-ASTERISK-CORE; ALPHA-2-BETA-1; SPECIFICITY; PROTEIN; DOMAIN;

D O I：

10.1002/anie.201004116

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The tie that binds: Rotaviruses bind to their host cells through the interaction of the virion outer capsid and spike proteins with receptors including sialic acid containing glycoconjugates. Intact rotavirus particles interact with the glycan of the GM3 ganglioside (see picture) primarily through the N-acetylneuraminic acid, but the penultimate galactose residue also contributes. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：1055 / 1058

页数：4

共 22 条

[1] Virus-ligand interactions:: Identification and characterization of ligand binding by NMR spectroscopy [J].