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dc.contributor.authorStrauss, Mike
dc.contributor.authorLevy, Hazel C.
dc.contributor.authorBostina, Mihnea
dc.contributor.authorFilman, David J.
dc.contributor.authorHogle, James M.
dc.date.accessioned2019-10-05T09:46:33Z
dc.date.issued2013
dc.identifier.citationStrauss, M., H. C. Levy, M. Bostina, D. J. Filman, and J. M. Hogle. 2013. “RNA Transfer from Poliovirus 135S Particles across Membranes Is Mediated by Long Umbilical Connectors.” Journal of Virology 87 (7): 3903–14. https://doi.org/10.1128/jvi.03209-12.
dc.identifier.issn0022-538X
dc.identifier.issn1070-6321
dc.identifier.issn1098-5514
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41483143*
dc.description.abstractDuring infection, the binding of poliovirus to its cell surface receptor at 37 degrees C triggers an expansion of the virus in which internal polypeptides that bind to membranes are externalized. Subsequently, in a poorly understood process, the viral RNA genome is transferred directly across an endosomal membrane, and into the host cell cytoplasm, to initiate infection. Here, cryoelectron tomography demonstrates the results of 37 degrees C warming of a poliovirus-receptor-liposome model complex that was produced using Ni-nitrilotriacetic acid lipids and His-tagged receptor ectodomains. In total, 651 subtomographic volumes were aligned, classified, and averaged to obtain detailed pictures, showing both the conversion of virus into its expanded form and the passage of RNA into intact liposomes. Unexpectedly, the virus and membrane surfaces were located similar to 50 angstrom apart, with the 5-fold axis tilted away from the perpendicular, and the solvent spaces between them were spanned by either one or two long "umbilical" density features that lie at an angle to the virus and membrane. The thinner connector, which sometimes appears alone, is 28 to 30 angstrom in diameter and has a footprint on the virus surface located close to either a 5-fold or a 3-fold axis. The broader connector has a footprint near the quasi-3-fold hole that opens upon virus expansion and is hypothesized to include RNA, shielded from enzymatic degradation by polypeptides that include the N-terminal extension of VP1 and capsid protein VP4. The implications of these observations for the mechanism of RNase-protected RNA transfer in picornaviruses are discussed.
dc.language.isoen_US
dc.publisherAmerican Society for Microbiology
dash.licenseLAA
dc.titleRNA Transfer from Poliovirus 135S Particles across Membranes Is Mediated by Long Umbilical Connectors
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalJournal of Virology
dash.depositing.authorHogle, James M.::b88a5e6fc972147844be38cdc64c65b7::600
dc.date.available2019-10-05T09:46:33Z
dash.workflow.comments1Science Serial ID 63239
dc.identifier.doi10.1128/JVI.03209-12
dash.source.volume87;7
dash.source.page3903


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