BATTISTI, Anthony J., Joshua D. YODER, Pavel PLEVKA, Dennis C. WINKLER, Vidya Mangala PRASAD, Richard J. KUHN, Teryl K. FREY, Alasdair C. STEVEN and Michael G. ROSSMANN. Cryo-Electron Tomography of Rubella Virus. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2012, vol. 86, No 20, p. 11078-11085. ISSN 0022-538X. Available from: https://dx.doi.org/10.1128/JVI.01390-12.
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Basic information
Original name Cryo-Electron Tomography of Rubella Virus
Authors BATTISTI, Anthony J., Joshua D. YODER, Pavel PLEVKA, Dennis C. WINKLER, Vidya Mangala PRASAD, Richard J. KUHN, Teryl K. FREY, Alasdair C. STEVEN and Michael G. ROSSMANN.
Edition JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2012, 0022-538X.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 5.076
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1128/JVI.01390-12
UT WoS 000309114900015
Keywords in English CAPSID PROTEIN; ELECTRON-MICROSCOPY; SINDBIS VIRUS; NONSTRUCTURAL POLYPROTEIN; 3-DIMENSIONAL STRUCTURE; GLYCOPROTEIN; SEQUENCE; PARTICLES; E2; ALPHAVIRUSES
Tags neMU
Changed by Changed by: Mgr. Eva Špillingová, učo 110713. Changed: 29/3/2017 14:27.
Abstract
Rubella virus is the only member of the Rubivirus genus within the Togaviridae family and is the causative agent of the childhood disease known as rubella or German measles. Here, we report the use of cryo-electron tomography to examine the three-dimensional structure of rubella virions and compare their structure to that of Ross River virus, a togavirus belonging the genus Alphavirus. The ectodomains of the rubella virus glycoproteins, E1 and E2, are shown to be organized into extended rows of density, separated by 9 nm on the viral surface. We also show that the rubella virus nucleocapsid structure often forms a roughly spherical shell which lacks high density at its center. While many rubella virions are approximately spherical and have dimensions similar to that of the icosahedral Ross River virus, the present results indicate that rubella exhibits a large degree of pleo-morphy. In addition, we used rotation function calculations and other analyses to show that approximately spherical rubella virions lack the icosahedral organization which characterizes Ross River and other alphaviruses. The present results indicate that the assembly mechanism of rubella virus, which has previously been shown to differ from that of the alphavirus assembly pathway, leads to an organization of the rubella virus structural proteins that is different from that of alphaviruses.
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