CaltechAUTHORS
  A Caltech Library Service

Aura alphavirus subgenomic RNA is packaged into virions of two sizes

Rümenapf, Tillmann and Brown, Dennis T. and Strauss, Ellen G. and König, Matthias and Ramirez-Mitchell, Ruben and Strauss, James H. (1995) Aura alphavirus subgenomic RNA is packaged into virions of two sizes. Journal of Virology, 69 (3). pp. 1741-1746. ISSN 0022-538X. PMCID PMC188778. https://resolver.caltech.edu/CaltechAUTHORS:RUMjvir95

[img]
Preview
PDF - Published Version
See Usage Policy.

581kB

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:RUMjvir95

Abstract

The alphavirus genome is 11.8 kb in size. During infection, a 4.2-kb subgenomic RNA is also produced. Most alphaviruses package only the genomic RNA into virions, which are enveloped particles with icosahedral symmetry, having a triangulation number (T) = 4. Aura virus, however, packages both the genomic RNA and the subgenomic RNA into virions. The genomic RNA is primarily packaged into a virion that has a diameter of 72 nm and which appears to be identical to the virions produced by other alphaviruses. The subgenomic RNA is packaged into two major, regular particles with diameters of 72 and 62 nm. The 72-nm-diameter particle appears to be identical in construction to virions containing genomic RNA. The 62-nm-diameter particle probably has T = 3. The large and small Aura virions can be partially separated in sucrose gradients. In addition to these two major classes of particles, there are other particles produced that appear to arise from abortive assembly. From these results and from previous studies of alphavirus assembly, we suggest that during assembly of alphavirus nucleocapsids in the infected cell there is a specific initiation event followed by recruitment of additional capsid subunits into the complex, that the triangulation number of the complex is not predetermined but depends upon the size of the RNA and interactions that occur during assembly, and that budding of assembled nucleocapsids results in the acquisition of an envelope containing glycoproteins arranged in a manner determined by the nucleocapsid.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC188778/PubMed CentralArticle
http://jvi.asm.org/cgi/content/abstract/69/3/1741OtherUNSPECIFIED
http://jvi.asm.org/cgi/content/abstract/69/3/1741OtherUNSPECIFIED
ORCID:
AuthorORCID
König, Matthias0000-0003-1725-179X
Additional Information:Copyright © 1995 by the American Society for Microbiology. Received 25 August 1994/Accepted 7 December 1994 We are grateful to F. Weiland for his interest in the project and help with electron microscopy. T.R. was supported by a fellowship from the Deutsche Forschungsgemeinschaft during a postdoctoral stay in Pasadena, Calif. This work was supported by grants AI 20612, AI 10793, and AI 14710 from NIH.
Funders:
Funding AgencyGrant Number
Deutsche Forschungsgemeinschaft (DFG)UNSPECIFIED
NIHAI 20612
NIHAI 10793
NIHAI 14710
Issue or Number:3
PubMed Central ID:PMC188778
Record Number:CaltechAUTHORS:RUMjvir95
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:RUMjvir95
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:2736
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:24 Apr 2006
Last Modified:09 Mar 2020 13:18

Repository Staff Only: item control page