Document Detail

Molecular tectonic model of virus structural transitions: the putative cell entry states of poliovirus.
MedLine Citation:
PMID:  10627545     Owner:  NLM     Status:  MEDLINE    
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.
D M Belnap; D J Filman; B L Trus; N Cheng; F P Booy; J F Conway; S Curry; C N Hiremath; S K Tsang; A C Steven; J M Hogle
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of virology     Volume:  74     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  2000 Feb 
Date Detail:
Created Date:  2000-02-07     Completed Date:  2000-02-07     Revised Date:  2014-11-07    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1342-54     Citation Subset:  IM    
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MeSH Terms
Capsid / chemistry,  ultrastructure*
Cryoelectron Microscopy
Crystallography, X-Ray
Image Processing, Computer-Assisted
Membrane Proteins*
Models, Biological
Models, Molecular
Nucleic Acid Conformation
Poliovirus / chemistry*,  metabolism,  ultrastructure*
Protein Conformation
RNA, Viral / chemistry,  ultrastructure
Receptors, Virus / metabolism
Virion / chemistry,  ultrastructure
Grant Support
Reg. No./Substance:
0/Membrane Proteins; 0/RNA, Viral; 0/Receptors, Virus; 0/poliovirus receptor

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