| Title | Distinct cellular receptor interactions in poliovirus and rhinoviruses. | ||
| Author | Xing, L; Tjarnlund, K; Lindqvist, B; Kaplan, G G; Feigelstock, D; Cheng, R H; Casasnovas, J M | ||
| Journal | EMBO J | Publication Year/Month | 2000-Mar |
| PMID | 10716921 | PMCID | PMC305662 |
| Affiliation | 1.Karolinska Institute, Department of Biosciences at NOVUM, Center for Biotechnology, S-141 57 Huddinge, Sweden. | ||
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.