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

被引：30

作者：

Konecsni, T

Kremser, L

Snyers, L

Rankl, C

Kilár, F

Kenndler, E

Blaas, D

机构：

[1] Univ Vienna, Bioctr, Dept Med Biochem, Max F Perutz Labs, A-1030 Vienna, Austria

[2] Univ Vienna, Inst Analyt Chem, A-1010 Vienna, Austria

[3] Univ Pecs, Fac Med, Inst Bioanal, H-7624 Pecs, Hungary

[4] Johannes Kepler Univ, Inst Biophys, A-4040 Linz, Austria

来源：

FEBS LETTERS | 2004年 / 568卷 / 1-3期

基金：

奥地利科学基金会;

关键词：

capillary electrophoresis; human rhinovirus; picornavirus; receptor; low-density lipoprotein; very low-density lipoprotein; structure;

D O I：

10.1016/j.febslet.2004.05.015

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：

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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：99 / 104

页数：6

共 22 条

[1] Charge-reduced nano electrospray ionization combined with differential mobility analysis of peptides, proteins, glycoproteins, noncovalent protein complexes and viruses [J].