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Journal of Virology, November 2008, p. 11208-11216, Vol. 82, No. 22
0022-538X/08/$08.00+0     doi:10.1128/JVI.00733-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Crystal Structure of the Avian Reovirus Inner Capsid Protein {sigma}A{triangledown}

Pablo Guardado-Calvo,1 Lorena Vazquez-Iglesias,1 José Martinez-Costas,1 Antonio L. Llamas-Saiz,2 Guy Schoehn,3,4 Gavin C. Fox,5 X. Lois Hermo-Parrado,1 Javier Benavente,1 and Mark J. van Raaij1,6*

Departamento de Bioquímica e Bioloxía Molecular, Facultade de Farmacia,1 Unidade de Difracción de Raios X, Laboratorio Integral de Dinámica y Estructura de Biomoléculas José R. Carracido, Edificio CACTUS, Universidade de Santiago de Compostela, E-15782 Santiago de Compostela, Spain,2 Unit for Virus Host Cell Interaction, UMR 5233, Université Joseph Fourier, EMBL, CNRS,3 Institut de Biologie Structurale Jean-Pierre Ebel, UMR5075 CEA-CNRS-UJF, Grenoble, France,4 Spanish CRG Beam-Line BM16, European Synchrotron Radiation Facility (ESRF), 6 rue Jules Horowitz, BP 220, F-38043 Grenoble, France,5 Instituto de Biologia Molecular de Barcelona (CSIC-Parc Cientific), c/Josep-Samitier 1-5, E-08028 Barcelona, Spain6

Received 3 April 2008/ Accepted 3 September 2008

Avian reovirus, an important avian pathogen, expresses eight structural and four nonstructural proteins. The structural {sigma}A protein is a major component of the inner capsid, clamping together {lambda}A building blocks. {sigma}A has also been implicated in the resistance of avian reovirus to the antiviral action of interferon by strongly binding double-stranded RNA in the host cell cytoplasm and thus inhibiting activation of the double-stranded RNA-dependent protein kinase. We have solved the structure of bacterially expressed {sigma}A by molecular replacement and refined it using data to 2.3-Å resolution. Twelve {sigma}A molecules are present in the P1 unit cell, arranged as two short double helical hexamers. A positively charged patch is apparent on the surface of {sigma}A on the inside of this helix and mutation of either of two key arginine residues (Arg155 and Arg273) within this patch abolishes double-stranded RNA binding. The structural data, together with gel shift assay, electron microscopy, and sedimentation velocity centrifugation results, provide evidence for cooperative binding of {sigma}A to double-stranded RNA. The minimal length of double-stranded RNA required for {sigma}A binding was observed to be 14 to 18 bp.

* Corresponding author. Mailing address: Departamento de Bioquímica e Bioloxía Molecular, Facultade de Farmacia, Universidade de Santiago de Compostela, E-15782 Santiago de Compostela, Spain. Phone and fax: 34 981 599157. E-mail: mark.vanraaij{at}usc.es

{triangledown} Published ahead of print on 17 September 2008.

Journal of Virology, November 2008, p. 11208-11216, Vol. 82, No. 22
0022-538X/08/$08.00+0     doi:10.1128/JVI.00733-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Vazquez-Iglesias, L., Lostale-Seijo, I., Martinez-Costas, J., Benavente, J. (2009). Avian Reovirus SigmaA Localizes to the Nucleolus and Enters the Nucleus by a Nonclassical Energy- and Carrier-Independent Pathway. J. Virol. 83: 10163-10175 [Abstract] [Full Text]  
  • Guu, T. S. Y., Liu, Z., Ye, Q., Mata, D. A., Li, K., Yin, C., Zhang, J., Tao, Y. J. (2009). Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding. Proc. Natl. Acad. Sci. USA 106: 12992-12997 [Abstract] [Full Text]  


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