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Crystal structure of a poxvirus-like zalpha domain from cyprinid herpesvirus 3

2013-04Journal article Open access
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dc.contributor.authorTomé, Ana Rita
dc.contributor.authorKuś, Krzysztof
dc.contributor.authorCorreia, Silvia
dc.contributor.authorPaulo, Lara Martins
dc.contributor.authorZacarias, Sónia
dc.contributor.authorde Rosa, Matteo
dc.contributor.authorFigueiredo, Delio
dc.contributor.authorParkhouse, R Michael E
dc.contributor.authorAthanasiadis, Alekos
dc.date.accessioned2015-11-10T11:06:38Z
dc.date.available2015-11-10T11:06:38Z
dc.date.issued2013-04
dc.description.abstractZalpha domains are a subfamily of the winged helix-turn-helix domains sharing the unique ability to recognize CpG repeats in the left-handed Z-DNA conformation. In vertebrates, domains of this family are found exclusively in proteins that detect foreign nucleic acids and activate components of the antiviral interferon response. Moreover, poxviruses encode the Zalpha domain-containing protein E3L, a well-studied and potent inhibitor of interferon response. Here we describe a herpesvirus Zalpha-domain-containing protein (ORF112) from cyprinid herpesvirus 3. We demonstrate that ORF112 also binds CpG repeats in the left-handed conformation, and moreover, its structure at 1.75 Å reveals the Zalpha fold found in ADAR1, DAI, PKZ, and E3L. Unlike other Zalpha domains, however, ORF112 forms a dimer through a unique domain-swapping mechanism. Thus, ORF112 may be considered a new member of the Z-domain family having DNA binding properties similar to those of the poxvirus E3L inhibitor of interferon response.pt_PT
dc.description.sponsorshipFCT PhD fellowships: (SFRH/BPD/71629/2010, SFRH/BD/51626/2011), MX-1428 BAG program.pt_PT
dc.identifier10.1128/JVI.03116-12
dc.identifier.citationCrystal Structure of a Poxvirus-Like Zalpha Domain from Cyprinid Herpesvirus 3 Ana Rita Tomé, Krzysztof Kuś, Silvia Correia, Lara Martins Paulo, Sónia Zacarias, Matteo de Rosa, Delio Figueiredo, R. Michael E. Parkhouse, and Alekos Athanasiadis J. Virol. April 2013 87:7 3998-4004; Accepted manuscript posted online 30 January 2013, doi:10.1128/JVI.03116-12pt_PT
dc.identifier.doi10.1128/JVI.03116-12
dc.identifier.urihttp://hdl.handle.net/10400.7/484
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherAmerican Society for Microbiologypt_PT
dc.relationMolecular basis of the recognition of foreign nucleic acids in innate immunity
dc.relationRecognition of Pathogen Nucleic Acids by Innate Immunity: Structure-Function Studies of the Cytoplasmic DNA Receptor DAI Pathway
dc.relation.publisherversionhttp://jvi.asm.org/content/87/7/3998.longpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectChromatography, Gelpt_PT
dc.subjectCloning, Molecularpt_PT
dc.subjectCpG Islandspt_PT
dc.subjectCrystallographypt_PT
dc.subjectDNA Virusespt_PT
dc.subjectDimerizationpt_PT
dc.subjectOpen Reading Framespt_PT
dc.subjectProtein Foldingpt_PT
dc.subjectViral Proteinspt_PT
dc.subjectModels, Molecularpt_PT
dc.subjectProtein Conformationpt_PT
dc.titleCrystal structure of a poxvirus-like zalpha domain from cyprinid herpesvirus 3pt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleMolecular basis of the recognition of foreign nucleic acids in innate immunity
oaire.awardTitleRecognition of Pathogen Nucleic Acids by Innate Immunity: Structure-Function Studies of the Cytoplasmic DNA Receptor DAI Pathway
oaire.awardURIinfo:eu-repo/grantAgreement/EC/FP7/231000/EU
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-PRO%2F112962%2F2009/PT
oaire.citation.endPage4004pt_PT
oaire.citation.issue7pt_PT
oaire.citation.startPage3998pt_PT
oaire.citation.titleJournal of Virologypt_PT
oaire.citation.volume87pt_PT
oaire.fundingStreamFP7
oaire.fundingStream3599-PPCDT
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameEuropean Commission
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublication26aa4b1c-7402-432d-8bc2-bc68664311c3
relation.isProjectOfPublicationb6213c74-475a-49d7-8f04-445bf4da83fa
relation.isProjectOfPublication.latestForDiscovery26aa4b1c-7402-432d-8bc2-bc68664311c3

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