Adenovirus interaction with its cellular receptor CAR.
Representative adenoviruses from four of the five major virus subgroups have been shown to interact with the 46-kDa coxsackievirus and adenovirus receptor (CAR) that is widely expressed on many human cell types, suggesting that the ability to bind CAR may be a conserved feature of many of the approximately 50 known adenovirus serotypes. Receptor binding is a function of the distal 'knob' domain of the trimeric viral fiber protein. Here we review recent structural characterizations of knob, CAR and knob-CAR complexes, and we discuss how knob architecture may have evolved to accommodate opposing selective pressures to vary antigenic structure while conserving receptor binding specificity. In contrast to the hypervariability of the solvent-exposed surface of knob, the CAR receptor was found to be non-polymorphic.
Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
J
J
Howitt
C W
CW
Anderson
P
P
Freimuth
D000260:Adenoviruses, Human / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002213:Capsid / Q000737:chemistry / Q000378:metabolism; D062727:Coxsackie and Adenovirus Receptor-Like Membrane Protein; D005822:Genetic Vectors / Q000235:genetics; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011991:Receptors, Virus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
C568771:CLMP protein, human; D062727:Coxsackie and Adenovirus Receptor-Like Membrane Protein; D011991:Receptors, Virus