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dc.contributor.authorMathioudakis, Matthaios M.
dc.contributor.authorKhechmar, Souheyla
dc.contributor.authorOwen, Carolyn A.
dc.contributor.authorMedina Piles, Vicente
dc.contributor.authorMansour, Karima Ben
dc.contributor.authorTomaszewska, Weronika
dc.contributor.authorSpanos, Theodore
dc.contributor.authorSarris, Panagiotis F.
dc.contributor.authorLivieratos, Ioannis C.
dc.date.accessioned2019-01-22T10:50:06Z
dc.date.available2019-01-22T10:50:06Z
dc.date.issued2018
dc.identifier.issn1422-0067
dc.identifier.urihttp://hdl.handle.net/10459.1/65597
dc.description.abstractPepino mosaic virus (PepMV) is a mechanically-transmitted tomato pathogen of importance worldwide. Interactions between the PepMV coat protein and triple gene block protein (TGBp1) with the host heat shock cognate protein 70 and catalase 1 (CAT1), respectively, have been previously reported by our lab. In this study, a novel tomato interactor (SlTXND9) was shown to bind the PepMV TGBp1 in yeast-two-hybrid screening, in vitro pull-down and bimolecular fluorescent complementation (BiFC) assays. SlTXND9 possesses part of the conserved thioredoxin (TRX) active site sequence (W__PC vs. WCXPC), and TXND9 orthologues cluster within the TRX phylogenetic superfamilyclosesttophosducin-likeprotein-3. InPepMV-infectedandhealthyNicotianabenthamiana plants,NbTXND9mRNAlevelswerecomparable,andexpressionlevelsremainedstableinbothlocal and systemic leaves for 10 days post inoculation (dpi), as was also the case for catalase 1 (CAT1). To localize the TXND9 in plant cells, a polyclonal antiserum was produced. Purified α-SlTXND9 immunoglobulin (IgG) consistently detected a set of three protein bands in the range of 27–35 kDa, in the 1000 and 30,000 g pellets, and the soluble fraction of extracts of healthy and PepMV-infected N. benthamiana leaves, but not in the cell wall. These bands likely consist of the homologous protein NbTXND9 and its post-translationally modified derivatives. On electron microscopy, immuno-gold labellingofultrathinsectionsofPepMV-infectedN.benthamianaleavesusingα-SlTXND9IgGrevealed particle accumulation close to plasmodesmata, suggesting a role in virus movement. Taken together, this study highlights a novel tomato-PepMV protein interaction and provides data on its localization in planta. Currently, studies focusing on the biological function of this interaction during PepMV infection are in progress.ca_ES
dc.language.isoengca_ES
dc.publisherMDPIca_ES
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.3390/ijms19123747ca_ES
dc.relation.ispartofInternational Journal of Molecular Sciences, 2018, vol. 19, núm. 12, 3747ca_ES
dc.rightscc-by (c) Matthaios M. Mathioudakis et al., 2018ca_ES
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectPotexvirusesca_ES
dc.subjectPepinomosaicvirusca_ES
dc.subjectHost-pathogeninteractionsca_ES
dc.subjectThioredoxinsca_ES
dc.titleA Thioredoxin Domain-Containing Protein Interacts with Pepino mosaic virus Triple Gene Block Protein 1ca_ES
dc.typeinfo:eu-repo/semantics/articleca_ES
dc.identifier.idgrec027893
dc.type.versioninfo:eu-repo/semantics/publishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES
dc.identifier.doihttps://doi.org/10.3390/ijms19123747


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cc-by (c) Matthaios M. Mathioudakis et al., 2018
Except where otherwise noted, this item's license is described as cc-by (c) Matthaios M. Mathioudakis et al., 2018