Structural Correlates of Rotavirus Cell Entry

DSpace/Manakin Repository

Structural Correlates of Rotavirus Cell Entry

Citable link to this page

 

 
Title: Structural Correlates of Rotavirus Cell Entry
Author: Abdelhakim, Aliaa H.; Salgado, Eric N.; Fu, Xiaofeng; Pasham, Mithun; Nicastro, Daniela; Kirchhausen, Tomas; Harrison, Stephen C.

Note: Order does not necessarily reflect citation order of authors.

Citation: Abdelhakim, Aliaa H., Eric N. Salgado, Xiaofeng Fu, Mithun Pasham, Daniela Nicastro, Tomas Kirchhausen, and Stephen C. Harrison. 2014. “Structural Correlates of Rotavirus Cell Entry.” PLoS Pathogens 10 (9): e1004355. doi:10.1371/journal.ppat.1004355. http://dx.doi.org/10.1371/journal.ppat.1004355.
Full Text & Related Files:
Abstract: Cell entry by non-enveloped viruses requires translocation into the cytosol of a macromolecular complex—for double-strand RNA viruses, a complete subviral particle. We have used live-cell fluorescence imaging to follow rotavirus entry and penetration into the cytosol of its ∼700 Å inner capsid particle (“double-layered particle”, DLP). We label with distinct fluorescent tags the DLP and each of the two outer-layer proteins and track the fates of each species as the particles bind and enter BSC-1 cells. Virions attach to their glycolipid receptors in the host cell membrane and rapidly become inaccessible to externally added agents; most particles that release their DLP into the cytosol have done so by ∼10 minutes, as detected by rapid diffusional motion of the DLP away from residual outer-layer proteins. Electron microscopy shows images of particles at various stages of engulfment into tightly fitting membrane invaginations, consistent with the interpretation that rotavirus particles drive their own uptake. Electron cryotomography of membrane-bound virions also shows closely wrapped membrane. Combined with high resolution structural information about the viral components, these observations suggest a molecular model for membrane disruption and DLP penetration.
Published Version: doi:10.1371/journal.ppat.1004355
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4161437/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:12987223
Downloads of this work:

Show full Dublin Core record

This item appears in the following Collection(s)

 
 

Search DASH


Advanced Search
 
 

Submitters