Cryo-electron microscopy reconstructions of triatoma virus particles: a clue to unravel genome delivery and capsid disassembly

Triatoma virus (TrV) is a member of the insect virus family Dicistroviridae and consists of a small, non-enveloped capsid that encloses its positive-sense ssRNA genome. Using cryo-transmission electron microscopy and three-dimensional reconstruction techniques combined with fitting of the available...

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Bibliographic Details
Published in:	Journal of general virology 2013-05, Vol.94 (Pt 5), p.1058-1068
Main Authors:	Agirre, J, Goret, G, LeGoff, M, Sánchez-Eugenia, R, Marti, G A, Navaza, J, Guérin, D M A, Neumann, E
Format:	Article
Language:	eng
Subjects:	Animals Biochemistry, Molecular Biology Capsid Capsid - metabolism Cryoelectron Microscopy Cryoelectron Microscopy - methods Crystallography Dicistroviridae Dicistroviridae - isolation & purification Dicistroviridae - physiology Dicistroviridae - ultrastructure Genome, Viral Genome, Viral - genetics Hydrogen-Ion Concentration Imaging, Three-Dimensional Insect Vectors Insect Vectors - virology Life Sciences Microscopy, Electron, Transmission Microscopy, Electron, Transmission - methods Models, Molecular Protein Stability RNA, Viral RNA, Viral - genetics Structural Biology Triatoma Triatoma - virology triatoma virus Virion Virion - ultrastructure Virus Assembly
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Summary:	Triatoma virus (TrV) is a member of the insect virus family Dicistroviridae and consists of a small, non-enveloped capsid that encloses its positive-sense ssRNA genome. Using cryo-transmission electron microscopy and three-dimensional reconstruction techniques combined with fitting of the available crystallographic models, this study analysed the capsids corresponding to mature and several RNA-empty TrV particles. After genome release, the resulting reconstruction of the empty capsids displayed no prominent conformational changes with respect to the full virion capsid. The results showed that RNA delivery led to empty capsids with an apparent overall intact protein shell and suggested that, in a subsequent step, empty capsids disassemble into small symmetrical particles. Contrary to what is observed upon genome release in mammalian picornaviruses, the empty TrV capsid maintained a protein shell thickness and size identical to that in full virions.
ISSN:	0022-1317 1465-2099 1465-2099