人鼻病毒2型的每个病毒颗粒通过多个模块附着12个受体分子。

Twelve receptor molecules attach per viral particle of human rhinovirus serotype 2 via multiple modules.

作者信息

Konecsni Tünde, Kremser Leopold, Snyers Luc, Rankl Christian, Kilár Ferenc, Kenndler Ernst, Blaas Dieter

机构信息

Institute for Analytical Chemistry, University of Vienna, Währingerstr. 38, A 1090 Vienna, Austria.

出版信息

FEBS Lett. 2004 Jun 18;568(1-3):99-104. doi: 10.1016/j.febslet.2004.05.015.

DOI:10.1016/j.febslet.2004.05.015

PMID:15196928

Abstract

The crystallographic T = 1 (pseudo T = 3) icosahedral symmetry of the human rhinovirus capsid dictates the presence of 60 identical, symmetry related surface structures that are available for antibody and receptor binding. X-ray crystallography has shown that 60 individual very-low density lipoprotein receptor (VLDLR) modules bind to HRV2. Their arrangement around the fivefold axes of the virion suggested that tandem oligomers of such modules could attach simultaneously to symmetry-related sites. By resolving virus particles carrying various numbers of artificial recombinant concatemers of VLDLR repeat 3 (V33333) by capillary electrophoresis and extrapolation of the measured mobilities to that at saturation of all binding sites, we present evidence for up to 12 molecules of the concatemer to bind one single virion.

摘要

人鼻病毒衣壳的晶体学T = 1（假T = 3）二十面体对称性决定了存在60个相同的、与对称性相关的表面结构，这些结构可用于抗体和受体结合。X射线晶体学表明，60个单独的极低密度脂蛋白受体（VLDLR）模块与HRV2结合。它们围绕病毒粒子五重轴的排列表明，这种模块的串联寡聚体可以同时附着到与对称性相关的位点。通过毛细管电泳解析携带不同数量VLDLR重复3（V33333）人工重组串联体的病毒颗粒，并将测量的迁移率外推至所有结合位点饱和时的迁移率，我们提供了证据表明多达12个串联体分子可结合单个病毒粒子。