Picornavirus-receptor interactions.
Many picornaviruses use cell-surface molecules belonging to the immunoglobulin superfamily (IgSF) as their cellular receptors. These molecules usually consist of tandem repeats of between two and five Ig-like domains whose amino-terminal domains (D1) interact with invading viruses, with their carboxy-terminal sections comprising a transmembrane and a short cytoplasmic region. Most rhino- and enteroviruses, belonging to the Picornavirus family, use a canyon-like feature on their surface to attach to cellular receptors. Binding into the canyon destabilizes the virus and thus initiates the uncoating process. By contrast, non-IgSF molecules, when used by picornaviruses as receptors, bind outside the canyon and do not cause viral instability.
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392, USA. mgr@indiana.bio.purdue.edu
Michael G
MG
Rossmann
Yongning
Y
He
Richard J
RJ
Kuhn
D000818:Animals; D062727:Coxsackie and Adenovirus Receptor-Like Membrane Protein; D029822:Enterovirus B, Human / Q000378:metabolism; D006801:Humans; D007136:Immunoglobulins / Q000378:metabolism; D018799:Intercellular Adhesion Molecule-1 / Q000378:metabolism; D010849:Picornaviridae / Q000378:metabolism*; D011991:Receptors, Virus / Q000378:metabolism*
C568771:CLMP protein, human; D062727:Coxsackie and Adenovirus Receptor-Like Membrane Protein; D007136:Immunoglobulins; D011991:Receptors, Virus; C105941:coxsackievirus B receptor; D018799:Intercellular Adhesion Molecule-1