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Distinct cellular receptor interactions in poliovirus and rhinoviruses
Author(s) -
Xing Li,
Tjarnlund Karin,
Lindqvist Birgitta,
Kaplan Gerardo G.,
Feigelstock Dino,
Cheng R. Holland,
Casasnovas José M.
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.6.1207
Subject(s) - biology , receptor , rhinovirus , poliovirus , binding site , capsid , biophysics , picornaviridae , viral entry , virology , virus , microbiology and biotechnology , biochemistry , viral replication
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 plasmon 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.