Main Menu (Mobile)- Block
- Our Research
-
Support Teams
- Overview
- Anatomy and Histology
- Cell and Tissue Culture
- Cryo-Electron Microscopy
- Drosophila Resources
- Electron Microscopy
- Flow Cytometry Shared Resource (FCSR)
- Gene Targeting and Transgenics
- Janelia Experimental Technology
- Light Microscopy
- Media Prep
- Molecular Biology
- Project Pipeline Support
- Project Technical Resources
- Quantitative Genomics
- Scientific Computing Software
- Scientific Computing Systems
- Viral Tools
- Vivarium
- Open Science
- You + Janelia
- About Us
Main Menu - Block
- Overview
- Anatomy and Histology
- Cell and Tissue Culture
- Cryo-Electron Microscopy
- Drosophila Resources
- Electron Microscopy
- Flow Cytometry Shared Resource (FCSR)
- Gene Targeting and Transgenics
- Janelia Experimental Technology
- Light Microscopy
- Media Prep
- Molecular Biology
- Project Pipeline Support
- Project Technical Resources
- Quantitative Genomics
- Scientific Computing Software
- Scientific Computing Systems
- Viral Tools
- Vivarium
Note: Research in this publication was not performed at Janelia.
Abstract
Non-enveloped viruses of different types have evolved distinct mechanisms for penetrating a cellular membrane during infection. Rotavirus penetration appears to occur by a process resembling enveloped-virus fusion: membrane distortion linked to conformational changes in a viral protein. Evidence for such a mechanism comes from crystallographic analyses of fragments of VP4, the rotavirus-penetration protein, and infectivity analyses of structure-based VP4 mutants. We describe here the structure of an infectious rotavirus particle determined by electron cryomicroscopy (cryoEM) and single-particle analysis at about 4.3 Å resolution. The cryoEM image reconstruction permits a nearly complete trace of the VP4 polypeptide chain, including the positions of most side chains. It shows how the two subfragments of VP4 (VP8(*) and VP5(*)) retain their association after proteolytic cleavage, reveals multiple structural roles for the β-barrel domain of VP5(*), and specifies interactions of VP4 with other capsid proteins. The virion model allows us to integrate structural and functional information into a coherent mechanism for rotavirus entry.