A Thioredoxin Domain-Containing Protein Interacts with Pepino mosaic virus Triple Gene Block Protein 1
Mathioudakis, Matthaios M.
Owen, Carolyn A.
Mansour, Karima Ben
Sarris, Panagiotis F.
Livieratos, Ioannis C.
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Pepino 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.
Is part ofInternational Journal of Molecular Sciences, 2018, vol. 19, núm. 12, 3747
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Except where otherwise noted, this item's license is described as cc-by (c) Matthaios M. Mathioudakis et al., 2018
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