title: Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses.
abstract: When poliovirus (PV) recognizes its receptor, CD155, the virus changes from a 160S to a 135S particle before releasing its genome into the cytoplasm. CD155 is a transmembrane protein with 3 Ig-like extracellular domains, D1-D3, where D1 is recognized by the virus. The crystal structure of D1D2 has been determined to 3.5-A resolution and fitted into approximately 8.5-A resolution cryoelectron microscopy reconstructions of the virus-receptor complexes for the 3 PV serotypes. These structures show that, compared with human rhinoviruses, the virus-receptor interactions for PVs have a greater dependence on hydrophobic interactions, as might be required for a virus that can inhabit environments of different pH. The pocket factor was shown to remain in the virus during the first recognition stage. The present structures, when combined with earlier mutational investigations, show that in the subsequent entry stage the receptor moves further into the canyon when at a physiological temperature, thereby expelling the pocket factor and separating the viral subunits to form 135S particles. These results provide a detailed analysis of how a nonenveloped virus can enter its host cell.
authors.affiliation: Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907-2054, USA.
authors.forename: Ping
authors.initials: P
authors.lastname: Zhang
authors.forename: Steffen
authors.initials: S
authors.lastname: Mueller
authors.forename: Marc C
authors.initials: MC
authors.lastname: Morais
authors.forename: Carol M
authors.initials: CM
authors.lastname: Bator
authors.forename: Valorie D
authors.initials: VD
authors.lastname: Bowman
authors.forename: Susan
authors.initials: S
authors.lastname: Hafenstein
authors.forename: Eckard
authors.initials: E
authors.lastname: Wimmer
authors.forename: Michael G
authors.initials: MG
authors.lastname: Rossmann
mesh_terms: D000595:Amino Acid Sequence; D002459:Cell Fusion; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D006367:HeLa Cells; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D017955:Poliovirus / Q000502:physiology*; D011487:Protein Conformation; D011991:Receptors, Virus / Q000737:chemistry* / Q000235:genetics / Q000502:physiology / Q000648:ultrastructure
chemical_list: D011991:Receptors, Virus; C066100:poliovirus receptor