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Updated: Jul 20, 2026

Averaging of Viral Envelope Glycoprotein Spikes from Electron Cryotomography Reconstructions using Jsubtomo
Published on: October 21, 2014
Molecular tectonic model of virus structural transitions: the putative cell entry states of poliovirus
D M Belnap1, D J Filman, B L Trus
1Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
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.
Insights
Poliovirus entry involves significant structural changes, revealing gaps in the capsid that allow viral proteins to emerge. These structural shifts are crucial for viral RNA entry into host cells.
Area of Science:
- Structural biology
- Virology
- Molecular biology
Background:
- Poliovirus entry into host cells is a complex process involving conformational changes.
- Externalization of viral proteins VP4 and VP1 N-terminus is critical for cell entry.
Purpose of the Study:
- To determine the structures of poliovirus native virions and cell entry intermediates.
- To elucidate the structural basis of poliovirus cell entry mechanisms.
Main Methods:
- Cryo-electron microscopy was used to determine structures at approximately 22-Å resolution.
- Pseudoatomic models were constructed by fitting known protein structures into the reconstructions.
- Analysis of domain movements within the viral capsid.
Main Results:
- Structures of native virions, 135S, and 80S particles were resolved.
- 135S and 80S particles showed a 4% increase in size compared to the virion.
- Domain movements up to 9 Å were observed, creating inter-subunit gaps.
Conclusions:
- The observed structural changes and gaps provide plausible mechanisms for VP4 and VP1 N-terminus externalization.
- These findings support models of viral RNA translocation through a transmembrane pore.
- Structural insights advance understanding of poliovirus infection and potential therapeutic targets.
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