What proteomics can reveal about plant–virus interactions? Photosynthesis-related proteins on the spotlight
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Plant viruses are responsible for losses in worldwide production of numerous economically important food and fuel crops. As obligate cellular parasites with very small genomes, viruses rely on their hosts for replication, assembly, intra- and intercellular movement, and attraction of vectors for dispersal. Chloroplasts are photosynthesis and are the site of replication for several viruses. When viruses replicate in chloroplasts, photosynthesis, an essential process in plant physiology, is inhibited. The mechanisms underlying molecular and biochemical changes during compatible and incompatible plants–virus interactions, are only beginning to be elucidated, including changes in proteomic profiles induced by virus infections. In this review, we highlight the importance of proteomic studies to understand plant–virus interactions, especially emphasizing the changes in photosynthesis-related protein accumulation. We focus on: (a) chloroplast proteins that differentially accumulate during viral infection; (b) the significance with respect to chloroplast-virus interaction; and (c) alterations in plant’s energetic metabolism and the subsequently the plant defense mechanisms to overcome viral infection.
KeywordsPlant–virus interactions Virus replication in chloroplasts Proteomics Photosynthesis Proteome
This study was supported by the following Brazilian institutions: CNPq (National Council for Scientific and Technological Development. Process Numbers: 308107/2013-6 and 306202/2017-4); CAPES (Coordination of Improvement of Higher Education. Toxinology Project, Process Number: 431511/2016-0) and Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico (FUNCAP). FELC is supported by FUNCAP/CAPES (Bolsista CAPES/BRASIL – Proc. 88887.162856/2018-00). Research at the Garcia-Ruiz lab is supported by NIH grant R01GM120108 to Hernan Garcia-Ruiz and by the Nebraska Agricultural Experiment Station with funding from the Hatch Act (Accession Number 1007272) through the USDA National Institute of Food and Agriculture.
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Conflict of interest
The authors declare that they have no conflict of interest.
- Cueto-Ginzo AI, Serrano L, Bostock RM, Ferrio JP, Rodríguez R, Arcal L, Achon MÁ, Falcioni T, Luzuriaga WP, Medina V (2016) Salicylic acid mitigates physiological and proteomic changes induced by the SPCP1 strain of Potato virus X in tomato plants. Physiol Mol Plant Pathol 93:1–11CrossRefGoogle Scholar
- de Torres Zabala M, Littlejohn G, Jayaraman S, Studholme D, Bailey T, Lawson T, Tillich M, Licht D, Bölter B, Delfino L, Truman W, Mansfield J, Smirnoff N, Grant M (2015) Chloroplasts play a central role in plant defence and are targeted by pathogen effectors. Nat Plant 1:15074CrossRefGoogle Scholar
- Garcia-Ruiz H, Takeda A, Chapman EJ, Sullivan CM, Fahlgren N, Brempelis KJ, Carrington JC (2010) Arabidopsis RNA-dependent RNA polymerases and dicer-like proteins in antiviral defense and small interfering RNA biogenesis during turnip mosaic virus infection. Plant Cell 22:481–496CrossRefPubMedPubMedCentralGoogle Scholar
- Garcia-Ruiz H, Garcia Ruiz MT, Peralta G, Manuel S, Gabriel M, Betzabeth C, El-Mounadi K (2016) Mecanismos, aplicaciones y perspectivas del silenciamiento génico de virus en plantas. Rev Mex Fitopatol 34:286–307Google Scholar
- Garcia-Ruiz H, Peralta GSM, Harte-Maxwell PA (2018) Tomato spotted wilt virus NSs protein supports infection and systemic movement of a potyviruses and is a symptom determinant. Viruses 10:1–21Google Scholar
- Kozuleva M, Goss T, Twachtmann M, Rudi K, Trapka J, Selinski J, Ivanov B, Garapati P, Steinhoff HJ, Hase T, Scheibe R, Klare JP, Hanke GT (2016) Ferredoxin:NADP(H) oxidoreductase abundance and location influences redox poise and stress tolerance. Plant Physiol 172:1480–1493CrossRefPubMedPubMedCentralGoogle Scholar
- Lundin B, Thuswaldner S, Shutova T, Eshaghi S, Samuelsson G, Barber J, Andersson B, Spetea C (2007) Subsequent events to GTP binding by the plant PsbO protein: structural changes, GTP hydrolysis and dissociation from the photosystem II complex. Biochim Biophys Acta 1767:500–508CrossRefPubMedGoogle Scholar
- Montasser M, Al-Ajmy A (2015) Histopathology for the influence of CMV infection on tomato cellular structures. FASEB J 29:887Google Scholar
- Paiva AL, Oliveira JT, de Souza GA, Vasconcelos IM (2016) Label-free proteomic reveals that Cowpea Severe Mosaic Virus transiently suppresses the host leaf protein accumulation during the compatible interaction with cowpea (Vigna unguiculata [L.] Walp.). J Proteome Res 15:4208–4220CrossRefPubMedGoogle Scholar
- Shimura H, Pantaleo V, Ishihara T, Myojo N, Inaba J-I, Sueda K, Burgyán J, Masuta C (2011) A viral satellite RNA induces yellow symptoms on tobacco by targeting a gene involved in chlorophyll biosynthesis using the RNA silencing machinery. PLoS Pathog 7:e1002021CrossRefPubMedPubMedCentralGoogle Scholar
- Varela ALN, Komatsu S, Wang X, Silva RGG, Souza PFN, Lobo AKM, Vasconcelos IM, Silveira JAG, Oliveira JTA (2017) Gel-free/label-free proteomic, photosynthetic, and biochemical analysis of cowpea (Vigna unguiculata [L.] Walp.) resistance against Cowpea severe mosaic virus (CPSMV). J Proteom 163:76–91CrossRefGoogle Scholar
- Ventelon-Debout M, Delalande F, Brizard JP, Diemer H, Van Dorsselaer A, Brugidou C (2004) Proteome analysis of cultivar-specific deregulations of Oryza sativa indica and O. sativa japonica cellular suspensions undergoing Rice yellow mottle virus infection. Proteomics 4:216–225CrossRefPubMedGoogle Scholar
- Yang A, Yu L, Chen Z, Zhang S, Shi J, Zhao X, Yang Y, Hu D, Song B (2017) Label-free quantitative proteomic analysis of chitosan oligosaccharide-treated rice infected with southern rice black-streaked dwarf virus. Viruses 115:1–16Google Scholar