title: Distinct cellular receptor interactions in poliovirus and rhinoviruses.
abstract: Receptor binding to human poliovirus type 1 (PV1/M) and the major group of human rhinoviruses (HRV) was studied comparatively to uncover the evolution of receptor recognition in picornaviruses. Surface plas- mon resonance showed receptor binding to PV1/M with faster association and dissociation rates than to HRV3 and HRV16, two serotypes that have similar binding kinetics. The faster rate for receptor association to PV1/M suggested a relatively more accessible binding site. Thermodynamics for receptor binding to the viruses and assays for receptor-mediated virus uncoating showed a more disruptive receptor interaction with PV1/M than with HRV3 or HRV16. Cryo-electron microscopy and image reconstruction of receptor-PV1/M complexes revealed receptor binding to the 'wall' of surface protrusions surrounding the 'canyon', a depressive surface in the capsid where the rhinovirus receptor binds. These data reveal more exposed receptor-binding sites in poliovirus than rhinoviruses, which are less protected from immune surveillance but more suited for receptor-mediated virus uncoating and entry at the cell surface.
authors.affiliation: Karolinska Institute, Department of Biosciences at NOVUM, Center for Biotechnology, S-141 57 Huddinge, Sweden.
authors.forename: L
authors.initials: L
authors.lastname: Xing
authors.forename: K
authors.initials: K
authors.lastname: Tjarnlund
authors.forename: B
authors.initials: B
authors.lastname: Lindqvist
authors.forename: G G
authors.initials: GG
authors.lastname: Kaplan
authors.forename: D
authors.initials: D
authors.lastname: Feigelstock
authors.forename: R H
authors.initials: RH
authors.lastname: Cheng
authors.forename: J M
authors.initials: JM
authors.lastname: Casasnovas
mesh_terms: D000818:Animals; D001665:Binding Sites; D002213:Capsid / Q000378:metabolism / Q000648:ultrastructure; D002460:Cell Line; D020285:Cryoelectron Microscopy; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D007700:Kinetics; D008565:Membrane Proteins; D008954:Models, Biological; D008958:Models, Molecular; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D017955:Poliovirus / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D011487:Protein Conformation; D011991:Receptors, Virus / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D011994:Recombinant Proteins / Q000378:metabolism / Q000648:ultrastructure; D012229:Rhinovirus / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D012995:Solubility; D013379:Substrate Specificity; D020349:Surface Plasmon Resonance; D013696:Temperature; D013816:Thermodynamics
chemical_list: D008565:Membrane Proteins; D010446:Peptide Fragments; D011991:Receptors, Virus; D011994:Recombinant Proteins; C066100:poliovirus receptor; D018799:Intercellular Adhesion Molecule-1