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

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

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31 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)99-104
Number of pages6
JournalFEBS letters
Issue number1-3
Publication statusPublished - Jun 18 2004



  • Capillary electrophoresis
  • Human rhinovirus
  • Low-density lipoprotein
  • Picornavirus
  • Receptor
  • Structure
  • Very low-density lipoprotein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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