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Title: Three-dimensional structure and stoichiometry of Helmintosporium victoriae190S totivirus

Abstract

Most double-stranded RNA viruses have a characteristic capsid consisting of 60 asymmetric coat protein dimers in a so-called T = 2 organization, a feature probably related to their unique life cycle. These capsids organize the replicative complex(es) that is actively involved in genome transcription and replication. Available structural data indicate that their RNA-dependent RNA polymerase (RDRP) is packaged as an integral capsid component, either as a replicative complex at the pentameric vertex (as in reovirus capsids) or as a fusion protein with the coat protein (as in some totivirus). In contrast with members of the family Reoviridae, there are two well-established capsid arrangements for dsRNA fungal viruses, exemplified by the totiviruses L-A and UmV and the chrysovirus PcV. Whereas L-A and UmV have a canonical T = 2 capsid, the PcV capsid is based on a T = 1 lattice composed of 60 capsid proteins. We used cryo-electron microscopy combined with three-dimensional reconstruction techniques and hydrodynamic analysis to determine the structure at 13.8 A resolution of Helminthosporium victoriae 190S virus (Hv190SV), a totivirus isolated from a filamentous fungus. The Hv190SV capsid has a smooth surface and is based on a T = 2 lattice with 60 equivalent dimers. Unlike themore » RDRP of some other totiviruses, which are expressed as a capsid protein-RDRP fusion protein, the Hv190SV RDRP is incorporated into the capsid as a separate, nonfused protein, free or non-covalently associated to the capsid interior.« less

Authors:
 [1];  [2];  [3];  [4];  [5];  [5];  [2];  [2];  [6];  [6]
  1. Department of Estructura de Macromoleculas, Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma de Madrid, Darwin no 3, Cantoblanco, E-28049 Madrid (Spain). E-mail: jrcaston@cnb.uam.es
  2. Department of Estructura de Macromoleculas, Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma de Madrid, Darwin no 3, Cantoblanco, E-28049 Madrid (Spain)
  3. Imaging Sciences Laboratory, CIT, NIAMS, NIH, DHHS, Bethesda, MD 20892-5624 (United States)
  4. (United States)
  5. Centro de Investigaciones Biologicas, CSIC, 28006 Madrid (Spain)
  6. Department of Plant Pathology, University of Kentucky, Lexington, KY 40546 (United States)
Publication Date:
OSTI Identifier:
20779479
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 347; Journal Issue: 2; Other Information: DOI: 10.1016/j.virol.2005.11.038; PII: S0042-6822(05)00781-6; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ASYMMETRY; DIMERS; ELECTRON MICROSCOPY; FUNGI; LIFE CYCLE; PROTEINS; RNA; STOICHIOMETRY; TRANSCRIPTION; VIRUSES

Citation Formats

Caston, Jose R., Luque, Daniel, Trus, Benes L., Laboratory of Structural Biology Research, NIAMS, NIH, DHHS, Bethesda, MD 20892-5624, Rivas, German, Alfonso, Carlos, Gonzalez, Jose M., Carrascosa, Jose L., Annamalai, Padmanaban, and Ghabrial, Said A. Three-dimensional structure and stoichiometry of Helmintosporium victoriae190S totivirus. United States: N. p., 2006. Web. doi:10.1016/J.VIROL.2005.1.
Caston, Jose R., Luque, Daniel, Trus, Benes L., Laboratory of Structural Biology Research, NIAMS, NIH, DHHS, Bethesda, MD 20892-5624, Rivas, German, Alfonso, Carlos, Gonzalez, Jose M., Carrascosa, Jose L., Annamalai, Padmanaban, & Ghabrial, Said A. Three-dimensional structure and stoichiometry of Helmintosporium victoriae190S totivirus. United States. doi:10.1016/J.VIROL.2005.1.
Caston, Jose R., Luque, Daniel, Trus, Benes L., Laboratory of Structural Biology Research, NIAMS, NIH, DHHS, Bethesda, MD 20892-5624, Rivas, German, Alfonso, Carlos, Gonzalez, Jose M., Carrascosa, Jose L., Annamalai, Padmanaban, and Ghabrial, Said A. Mon . "Three-dimensional structure and stoichiometry of Helmintosporium victoriae190S totivirus". United States. doi:10.1016/J.VIROL.2005.1.
@article{osti_20779479,
title = {Three-dimensional structure and stoichiometry of Helmintosporium victoriae190S totivirus},
author = {Caston, Jose R. and Luque, Daniel and Trus, Benes L. and Laboratory of Structural Biology Research, NIAMS, NIH, DHHS, Bethesda, MD 20892-5624 and Rivas, German and Alfonso, Carlos and Gonzalez, Jose M. and Carrascosa, Jose L. and Annamalai, Padmanaban and Ghabrial, Said A.},
abstractNote = {Most double-stranded RNA viruses have a characteristic capsid consisting of 60 asymmetric coat protein dimers in a so-called T = 2 organization, a feature probably related to their unique life cycle. These capsids organize the replicative complex(es) that is actively involved in genome transcription and replication. Available structural data indicate that their RNA-dependent RNA polymerase (RDRP) is packaged as an integral capsid component, either as a replicative complex at the pentameric vertex (as in reovirus capsids) or as a fusion protein with the coat protein (as in some totivirus). In contrast with members of the family Reoviridae, there are two well-established capsid arrangements for dsRNA fungal viruses, exemplified by the totiviruses L-A and UmV and the chrysovirus PcV. Whereas L-A and UmV have a canonical T = 2 capsid, the PcV capsid is based on a T = 1 lattice composed of 60 capsid proteins. We used cryo-electron microscopy combined with three-dimensional reconstruction techniques and hydrodynamic analysis to determine the structure at 13.8 A resolution of Helminthosporium victoriae 190S virus (Hv190SV), a totivirus isolated from a filamentous fungus. The Hv190SV capsid has a smooth surface and is based on a T = 2 lattice with 60 equivalent dimers. Unlike the RDRP of some other totiviruses, which are expressed as a capsid protein-RDRP fusion protein, the Hv190SV RDRP is incorporated into the capsid as a separate, nonfused protein, free or non-covalently associated to the capsid interior.},
doi = {10.1016/J.VIROL.2005.1},
journal = {Virology},
number = 2,
volume = 347,
place = {United States},
year = {Mon Apr 10 00:00:00 EDT 2006},
month = {Mon Apr 10 00:00:00 EDT 2006}
}
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