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Journal of Virology, September 2006, p. 8493-8502, Vol. 80, No. 17
0022-538X/06/$08.00+0     doi:10.1128/JVI.00713-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains

Marie-Pierre Egloff,1,{dagger} Hélène Malet,1,{dagger} Ákos Putics,2 Maarit Heinonen,4 Hélène Dutartre,1 Antoine Frangeul,1 Arnaud Gruez,1 Valérie Campanacci,1 Christian Cambillau,1 John Ziebuhr,2,3 Tero Ahola,4 and Bruno Canard1*

Centre National de la Recherche Scientifique and Universités d'Aix-Marseille I et II, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Ecole Supérieure d'Ingénieurs de Luminy-Case 925, 163 Ave. de Luminy, 13288 Marseille Cedex 9, France,1 Institute of Virology and Immunology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany,2 Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, The Queen's University of Belfast, 97 Lisburn Rd., Belfast BT9 7BL, United Kingdom,3 Program in Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, P.O. Box 56, Viikinkaari 9, 00014 Helsinki, Finland4

Received 23 May 2006/ Accepted 8 June 2006

Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Å resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.

* Corresponding author. Mailing address: Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Université Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex 09, France. Phone: 33 4 91 82 86 44. Fax: 33 4 91 82 86 46. E-mail: Bruno.Canard{at}afmb.univ-mrs.fr.

{dagger} M.-P.E. and H.M. contributed equally to this study.

Journal of Virology, September 2006, p. 8493-8502, Vol. 80, No. 17
0022-538X/06/$08.00+0     doi:10.1128/JVI.00713-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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