Twelve receptor molecules attach per viral particle of human rhinovirus serotype 2 via multiple modules.
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.
Konecsni
Tünde
T
Institute for Analytical Chemistry, University of Vienna, Währingerstr. 38, A 1090 Vienna, Austria.
Kremser
Leopold
L
Snyers
Luc
L
Rankl
Christian
C
Kilár
Ferenc
F
Kenndler
Ernst
E
Blaas
Dieter
D
D019075:Electrophoresis, Capillary; D006801:Humans; D011973:Receptors, LDL / Q000378:metabolism*; D011991:Receptors, Virus / Q000378:metabolism*; D012229:Rhinovirus / Q000378:metabolism*; D014771:Virion / Q000378:metabolism*
D011973:Receptors, LDL; D011991:Receptors, Virus; C036053:VLDL receptor