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Characterization of Ovine A3Z1 Restriction Properties against Small Ruminant Lentiviruses (SRLVs)

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dc.contributor Háskóli Íslands
dc.contributor University of Iceland
dc.contributor.author de Pablo-Maiso, Lorena
dc.contributor.author Glaria, Idoia
dc.contributor.author Crespo, Helena
dc.contributor.author Nistal-Villán, Estanislao
dc.contributor.author Andrésdóttir, Valgerður
dc.contributor.author de Andrés, Damián
dc.contributor.author Amorena, Beatriz
dc.contributor.author Reina, Ramsés
dc.date.accessioned 2017-12-21T11:12:30Z
dc.date.available 2017-12-21T11:12:30Z
dc.date.issued 2017-11-17
dc.identifier.citation de Pablo-Maiso, L.; Glaria, I.; Crespo, H.; Nistal-Villán, E.; Andrésdóttir, V.; de Andrés, D.; Amorena, B.; Reina, R. Characterization of Ovine A3Z1 Restriction Properties against Small Ruminant Lentiviruses (SRLVs). Viruses 2017, 9, 345. doi:10.3390/v9110345
dc.identifier.issn 1999-4915
dc.identifier.uri https://hdl.handle.net/20.500.11815/491
dc.description.abstract Intrinsic factors of the innate immune system include the apolipoprotein B editing enzyme catalytic polypeptide-like 3 (APOBEC3) protein family. APOBEC3 inhibits replication of different virus families by cytosine deamination of viral DNA and a not fully characterized cytosine deamination-independent mechanism. Sheep are susceptible to small ruminant lentivirus (SRLVs) infection and contain three APOBEC3 genes encoding four proteins (A3Z1, Z2, Z3 and Z2-Z3) with yet not deeply described antiviral properties. Using sheep blood monocytes and in vitro-derived macrophages, we found that A3Z1 expression is associated with lower viral replication in this cellular type. A3Z1 transcripts may also contain spliced variants (A3Z1Tr) lacking the cytidine deaminase motif. A3Z1 exogenous expression in fully permissive fibroblast-like cells restricted SRLVs infection while A3Z1Tr allowed infection. A3Z1Tr was induced after SRLVs infection or stimulation of blood-derived macrophages with interferon gamma (IFN-γ). Interaction between truncated isoform and native A3Z1 protein was detected as well as incorporation of both proteins into virions. A3Z1 and A3Z1Tr interacted with SRLVs Vif, but this interaction was not associated with degradative properties. Similar A3Z1 truncated isoforms were also present in human and monkey cells suggesting a conserved alternative splicing regulation in primates. A3Z1-mediated retroviral restriction could be constrained by different means, including gene expression and specific alternative splicing regulation, leading to truncated protein isoforms lacking a cytidine-deaminase motif
dc.description.sponsorship We sincerely acknowledge Sandra Hervás-Stubbs from CIMA for her fruitful help. We also acknowledge Greg Towers, University College London for plasmids and protocols. Funded by CICYT (AGL2010-22341-C04-01) and Navarra’s Government (IIQ010449.RI1, IIQ14064.RI1 and PI042-LENTIMOL). Ramsés Reina was supported by the Spanish Ministry of Science and Innovation “Ramón y Cajal” contract. We acknowledge support of the publication fee by the Public University of Navarra and CSIC Open Access Publication Support Initiative through its Unit of Information Resources for Research (URICI).
dc.format.extent 345
dc.language.iso en
dc.publisher MDPI AG
dc.relation.ispartofseries Viruses;9(11)
dc.rights info:eu-repo/semantics/openAccess
dc.subject APOBEC3
dc.subject Small ruminant lentiviruses
dc.subject Restriction factors
dc.subject Deaminase domain
dc.subject Alternative splicing
dc.subject Ónæmiskerfi
dc.subject Veirur
dc.subject Prótín
dc.title Characterization of Ovine A3Z1 Restriction Properties against Small Ruminant Lentiviruses (SRLVs)
dc.type info:eu-repo/semantics/article
dcterms.license This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
dc.description.version Peer Reviewed
dc.identifier.journal Viruses
dc.identifier.doi 10.3390/v9110345
dc.relation.url http://www.mdpi.com/1999-4915/9/11/345/pdf
dc.contributor.department Tilraunastöð í meinafræði að Keldum (HÍ)
dc.contributor.department Institute for Experimental Pathology, Keldur (UI)

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