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Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains.

Identifieur interne : 001621 ( Ncbi/Curation ); précédent : 001620; suivant : 001622

Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains.

Auteurs : Marie-Pierre Egloff [France] ; Hélène Malet ; Akos Putics ; Maarit Heinonen ; Hélène Dutartre ; Antoine Frangeul ; Arnaud Gruez ; Valérie Campanacci ; Christian Cambillau ; John Ziebuhr ; Tero Ahola ; Bruno Canard

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RBID : pubmed:16912299

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English descriptors

Abstract

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-Angstroms 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.

DOI: 10.1128/JVI.00713-06
PubMed: 16912299

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Le document en format XML

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<term>Adenosine Diphosphate Ribose (metabolism)</term>
<term>Amino Acid Sequence</term>
<term>Crystallography</term>
<term>Hepatitis E virus (chemistry)</term>
<term>Hepatitis E virus (metabolism)</term>
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<term>Histones (metabolism)</term>
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<term>Séquence d'acides aminés</term>
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<term>Virus de la forêt de Semliki ()</term>
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<term>Adenosine Diphosphate Ribose</term>
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<term>Histones</term>
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<term>Séquence d'acides aminés</term>
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<div type="abstract" xml:lang="en">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-Angstroms 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.</div>
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