Distinct cellular receptor interactions in poliovirus and rhinoviruses

Li Xing, Karin Tjarnlund, Birgitta Lindqvist, Gerardo G. Kaplan, Dino Feigelstock, R. Holland Cheng, José M. Casasnovas

Research output: Contribution to journalArticlepeer-review

105 Scopus citations


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. Cryoelectron 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.

Original languageEnglish (US)
Pages (from-to)1207-1216
Number of pages10
JournalEMBO Journal
Issue number6
StatePublished - Mar 15 2000
Externally publishedYes


  • Cryo-EM and image reconstruction
  • Picornavirus entry
  • Poliovirus
  • Rhinovirus
  • Virus-recept interaction

ASJC Scopus subject areas

  • Genetics
  • Cell Biology


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