Zhang, Wei and Fisher, Bonnie R. and Olson, Norman H. and Strauss, James H. and Kuhn, Richard J. and Baker, Timothy S. (2002) Aura Virus Structure Suggests that the T=4 Organization Is a Fundamental Property of Viral Structural Proteins. Journal of Virology, 76 (14). pp. 7239-7246. ISSN 0022-538X. PMCID PMC136343. http://resolver.caltech.edu/CaltechAUTHORS:ZHAjvir02
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Aura and Sindbis viruses are closely related alphaviruses. Unlike other alphaviruses, Aura virus efficiently encapsidates both genomic RNA (11.8 kb) and subgenomic RNA (4.2 kb) to form virus particles. Previous studies on negatively stained Aura virus particles predicted that there were two major size classes with potential T=3 and T=4 capsid structures. We have used cryoelectron microscopy and three-dimensional image reconstruction techniques to examine the native morphology of different classes of Aura virus particles produced in BHK cells. Purified particles separated into two components in a sucrose gradient. Reconstructions of particles in the top and bottom components were computed to resolutions of 17 and 21 Å, respectively, and compared with reconstructions of Sindbis virus and Ross River virus particles. Aura virus particles of both top and bottom components have similar, T=4 structures that resemble those of other alphaviruses. The morphology of Aura virus glycoprotein spikes closely resembles that of Sindbis virus spikes and is detectably different from that of Ross River virus spikes. Thus, some aspects of the surface structure of members of the Sindbis virus lineage have been conserved, but other aspects have diverged from the Semliki Forest/Ross River virus lineage.
|Additional Information:||Copyright © 2002, American Society for Microbiology. Received 26 December 2001/ Accepted 15 April 2002 We thank Michael Rossmann, Ellen Strauss, and Rushika Perera for useful discussions. This work was supported in part by NIH grants to T.S.B. (AI45976), R.J.K. (GM56279), and J.H.S. (AI20612) and an NSF shared instrumentation grant (BIR-9112921) to T.S.B. We also thank Purdue University for an instrumentation reinvestment grant to the Purdue Structural Biology Group.|
|PubMed Central ID:||PMC136343|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Archive Administrator|
|Deposited On:||15 Mar 2006|
|Last Modified:||15 Dec 2015 20:35|
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