title: Molecular tectonic model of virus structural transitions: the putative cell entry states of poliovirus.
abstract: Upon interacting with its receptor, poliovirus undergoes conformational changes that are implicated in cell entry, including the externalization of the viral protein VP4 and the N terminus of VP1. We have determined the structures of native virions and of two putative cell entry intermediates, the 135S and 80S particles, at approximately 22-A resolution by cryo-electron microscopy. The 135S and 80S particles are both approximately 4% larger than the virion. Pseudoatomic models were constructed by adjusting the beta-barrel domains of the three capsid proteins VP1, VP2, and VP3 from their known positions in the virion to fit the 135S and 80S reconstructions. Domain movements of up to 9 A were detected, analogous to the shifting of tectonic plates. These movements create gaps between adjacent subunits. The gaps at the sites where VP1, VP2, and VP3 subunits meet are plausible candidates for the emergence of VP4 and the N terminus of VP1. The implications of these observations are discussed for models in which the externalized components form a transmembrane pore through which viral RNA enters the infected cell.
authors.affiliation: Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
authors.forename: D M
authors.initials: DM
authors.lastname: Belnap
authors.forename: D J
authors.initials: DJ
authors.lastname: Filman
authors.forename: B L
authors.initials: BL
authors.lastname: Trus
authors.forename: N
authors.initials: N
authors.lastname: Cheng
authors.forename: F P
authors.initials: FP
authors.lastname: Booy
authors.forename: J F
authors.initials: JF
authors.lastname: Conway
authors.forename: S
authors.initials: S
authors.lastname: Curry
authors.forename: C N
authors.initials: CN
authors.lastname: Hiremath
authors.forename: S K
authors.initials: SK
authors.lastname: Tsang
authors.forename: A C
authors.initials: AC
authors.lastname: Steven
authors.forename: J M
authors.initials: JM
authors.lastname: Hogle
mesh_terms: D002213:Capsid / Q000737:chemistry / Q000648:ultrastructure*; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D007091:Image Processing, Computer-Assisted; D008565:Membrane Proteins; D008954:Models, Biological; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D017955:Poliovirus / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D011487:Protein Conformation; D012367:RNA, Viral / Q000737:chemistry / Q000648:ultrastructure; D011991:Receptors, Virus / Q000378:metabolism; D014771:Virion / Q000737:chemistry / Q000648:ultrastructure
chemical_list: D008565:Membrane Proteins; D012367:RNA, Viral; D011991:Receptors, Virus; C066100:poliovirus receptor