Asymmetric binding of transferrin receptor to parvovirus capsids.
Although many viruses are icosahedral when they initially bind to one or more receptor molecules on the cell surface, such an interaction is asymmetric, probably causing a breakdown in the symmetry and conformation of the original infecting virion in preparation for membrane penetration and release of the viral genome. Cryoelectron microscopy and biochemical analyses show that transferrin receptor, the cellular receptor for canine parvovirus, can bind to only one or a few of the 60 icosahedrally equivalent sites on the virion, indicating that either canine parvovirus has inherent asymmetry or binding of receptor induces asymmetry. The asymmetry of receptor binding to canine parvovirus is reminiscent of the special portal in tailed bacteriophages and some large, icosahedral viruses. Asymmetric interactions of icosahedral viruses with their hosts might be a more common phenomenon than previously thought and may have been obscured by averaging in previous crystallographic and electron microscopic structure determinations.
Hafenstein
Susan
S
Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907-2054, USA.
Palermo
Laura M
LM
Kostyuchenko
Victor A
VA
Xiao
Chuan
C
Morais
Marc C
MC
Nelson
Christian D S
CD
Bowman
Valorie D
VD
Battisti
Anthony J
AJ
Chipman
Paul R
PR
Parrish
Colin R
CR
Rossmann
Michael G
MG
D000818:Animals; D001665:Binding Sites; D002213:Capsid / Q000737:chemistry* / Q000378:metabolism*; D002415:Cats; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D004285:Dogs; D028301:Feline Panleukopenia Virus / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D017993:Parvovirus, Canine / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D011990:Receptors, Transferrin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018411:Spodoptera; D014771:Virion / Q000737:chemistry / Q000378:metabolism
D011990:Receptors, Transferrin