Dichorhaviruses Movement Protein and Nucleoprotein Form a Protein Complex That May Be Required for Virus Spread and Interacts in vivo With Viral Movement-Related Cilevirus Proteins

Vista sencilla de ítem
dc.contributor.affiliationInstituto Universitario Mixto de Biología Molecular y Celular de Plantas
dc.contributor.authorLeastro, Mikhail Oliveiraes_ES
dc.contributor.authorFreitas-Astúa, Julianaes_ES
dc.contributor.authorKitajima, Elliot Watanabees_ES
dc.contributor.authorPallás Benet, Vicente
dc.contributor.authorSánchez-Navarro, Jesús-Ángel
dc.contributor.funderGeneralitat Valencianaes_ES
dc.contributor.funderFundação de Amparo à Pesquisa do Estado de São Pauloes_ES
dc.contributor.funderAgencia Estatal de Investigaciónes_ES
dc.date.accessioned2021-05-08T03:31:27Z
dc.date.available2021-05-08T03:31:27Z
dc.date.issued2020-11-04es_ES
dc.description.abstract[EN] Brevipalpus-transmitted viruses (BTVs) belong to the genera Dichorhavirus and Cilevirus and are the main causal agents of the citrus leprosis (CL) disease. In this report, we explored aspects related to the movement mechanism mediated by dichorhaviruses movement proteins (MPs) and the homologous and heterologous interactions among viral proteins related to the movement of citrus leprosis-associated viruses. The membrane-spanning property and topology analysis of the nucleocapsid (N) and MP proteins from two dichorhaviruses revealed that the MPs are proteins tightly associated with the cell membrane, exposing their N- and C-termini to the cytoplasm and the inner part of the nucleus, whereas the N proteins are not membrane-associated. Subcellular localization analysis revealed the presence of dichorhavirus MPs at the cell surface and in the nucleus, while the phosphoproteins (P) were located exclusively in the nucleus and the N proteins in both the cytoplasm and the nucleus. Co-expression analysis with the MP, P, and N proteins showed an interaction network formed between them. We highlight the MP capability to partially redistribute the previously reported N-P core complex, redirecting a portion of the N from the nucleus to the plasmodesmata at the cell periphery, which indicates not only that the MP might guide the intracellular trafficking of the viral infective complex but also that the N protein may be associated with the cell-to-cell movement mechanism of dichorhaviruses. The movement functionality of these MPs was analyzed by using three movement-defective infectious systems. Also, the MP capacity to generate tubular structures on the protoplast surface by ectopic expression was analyzed. Finally, we evaluated the in vivo protein-protein interaction networks between the dichorhavirus MP and/or N proteins with the heterologous cilevirus movement components, which suggest a broad spectrum of interactions, highlighting those among capsid proteins (CP), MPs, and Ns from citrus leprosis-associated viruses. These data may aid in understanding the mixed infection process naturally observed in the field caused by distinct BTVs.en_EN
dc.description.accrualMethodSes_ES
dc.description.bibliographicCitationLeastro, MO.; Freitas-Astúa, J.; Kitajima, EW.; Pallás Benet, V.; Sanchez Navarro, JA. (2020). Dichorhaviruses Movement Protein and Nucleoprotein Form a Protein Complex That May Be Required for Virus Spread and Interacts in vivo With Viral Movement-Related Cilevirus Proteins. Frontiers in Microbiology. 11:1-22. https://doi.org/10.3389/fmicb.2020.571807es_ES
dc.description.referencesAparicio, F., Pallas, V., & Sanchez-Navarro, J. (2010). Implication of the C terminus of the Prunus necrotic ringspot virus movement protein in cell-to-cell transport and in its interaction with the coat protein. Journal of General Virology, 91(7), 1865-1870. doi:10.1099/vir.0.019950-0es_ES
dc.description.referencesAparicio, F., Sánchez-Navarro, J. A., & Pallás, V. (2006). In vitro and in vivo mapping of the Prunus necrotic ringspot virus coat protein C-terminal dimerization domain by bimolecular fluorescence complementation. Journal of General Virology, 87(6), 1745-1750. doi:10.1099/vir.0.81696-0es_ES
dc.description.referencesBastianel, M., Novelli, V. M., Kitajima, E. W., Kubo, K. S., Bassanezi, R. B., Machado, M. A., & Freitas-Astúa, J. (2010). Citrus Leprosis: Centennial of an Unusual Mite–Virus Pathosystem. Plant Disease, 94(3), 284-292. doi:10.1094/pdis-94-3-0284es_ES
dc.description.referencesBejerman, N., Giolitti, F., de Breuil, S., Trucco, V., Nome, C., Lenardon, S., & Dietzgen, R. G. (2015). Complete genome sequence and integrated protein localization and interaction map for alfalfa dwarf virus, which combines properties of both cytoplasmic and nuclear plant rhabdoviruses. Virology, 483, 275-283. doi:10.1016/j.virol.2015.05.001es_ES
dc.description.referencesBeltran-Beltran, A. K., Santillán-Galicia, M. T., Guzmán-Franco, A. W., Teliz-Ortiz, D., Gutiérrez-Espinoza, M. A., Romero-Rosales, F., & Robles-García, P. L. (2020). Incidence of Citrus leprosis virus C and Orchid fleck dichorhavirus Citrus Strain in Mites of the Genus Brevipalpus in Mexico. Journal of Economic Entomology, 113(3), 1576-1581. doi:10.1093/jee/toaa007es_ES
dc.description.referencesBordier, C. (1981). Phase separation of integral membrane proteins in Triton X-114 solution. Journal of Biological Chemistry, 256(4), 1604-1607. doi:10.1016/s0021-9258(19)69848-0es_ES
dc.description.referencesBrown, J. K., Idris, A. M., Alteri, C., & Stenger, D. C. (2002). Emergence of a New Cucurbit-Infecting Begomovirus Species Capable of Forming Viable Reassortants with Related Viruses in theSquash leaf curl virusCluster. Phytopathology®, 92(7), 734-742. doi:10.1094/phyto.2002.92.7.734es_ES
dc.description.referencesCanto, T., & Palukaitis, P. (2002). Novel N Gene-Associated, Temperature-Independent Resistance to the Movement of Tobacco Mosaic Virus Vectors Neutralized by a Cucumber Mosaic Virus RNA1 Transgene. Journal of Virology, 76(24), 12908-12916. doi:10.1128/jvi.76.24.12908-12916.2002es_ES
dc.description.referencesChabi-Jesus, C., Ramos-González, P. L., Tassi, A. D., Guerra-Peraza, O., Kitajima, E. W., Harakava, R., … Freitas-Astúa, J. (2018). Identification and Characterization of Citrus Chlorotic Spot Virus, a New Dichorhavirus Associated with Citrus Leprosis-Like Symptoms. Plant Disease, 102(8), 1588-1598. doi:10.1094/pdis-09-17-1425-rees_ES
dc.description.referencesChapman, S., Hills, G., Watts, J., & Baulcombe, D. (1992). Mutational analysis of the coat protein gene of potato virus X: Effects on virion morphology and viral pathogenicity. Virology, 191(1), 223-230. doi:10.1016/0042-6822(92)90183-pes_ES
dc.description.referencesCook, G., Kirkman, W., Clase, R., Steyn, C., Basson, E., Fourie, P. H., … Hattingh, V. (2019). Orchid fleck virus associated with the first case of citrus leprosis-N in South Africa. European Journal of Plant Pathology, 155(4), 1373-1379. doi:10.1007/s10658-019-01854-4es_ES
dc.description.referencesCruz-Jaramillo, J., Ruiz-Medrano, R., Rojas-Morales, L., López-Buenfil, J., Morales-Galván, O., Chavarín-Palacio, C., … Xoconostle-Cázares, B. (2014). Characterization of a Proposed Dichorhavirus Associated with the Citrus Leprosis Disease and Analysis of the Host Response. Viruses, 6(7), 2602-2622. doi:10.3390/v6072602es_ES
dc.description.referencesDeng, M., Bragg, J. N., Ruzin, S., Schichnes, D., King, D., Goodin, M. M., & Jackson, A. O. (2007). Role of the Sonchus Yellow Net Virus N Protein in Formation of Nuclear Viroplasms. Journal of Virology, 81(10), 5362-5374. doi:10.1128/jvi.02349-06es_ES
dc.description.referencesDietzgen, R. G., Bejerman, N. E., Goodin, M. M., Higgins, C. M., Huot, O. B., Kondo, H., … Whitfield, A. E. (2020). Diversity and epidemiology of plant rhabdoviruses. Virus Research, 281, 197942. doi:10.1016/j.virusres.2020.197942es_ES
dc.description.referencesDietzgen, R. G., Freitas-Astúa, J., Chabi-Jesus, C., Ramos-González, P. L., Goodin, M. M., Kondo, H., … Kitajima, E. W. (2018). Dichorhaviruses in their Host Plants and Mite Vectors. Advances in Virus Research, 119-148. doi:10.1016/bs.aivir.2018.06.001es_ES
dc.description.referencesForster, R. L. S., Beck, D. L., Guilford, P. J., Voot, D. M., Van Dolleweerd, C. J., & Andersen, M. T. (1992). Thecoat protein of white clover mosaic potexvirus has a role in facilitating cell-to-cell transport in plants. Virology, 191(1), 480-484. doi:10.1016/0042-6822(92)90215-bes_ES
dc.description.referencesFreitas-Astúa, J., Moreira, L., Rivera, C., Rodríguez, C. M., & Kitajima, E. W. (2002). First Report of Orchid fleck virus in Costa Rica. Plant Disease, 86(12), 1402-1402. doi:10.1094/pdis.2002.86.12.1402des_ES
dc.description.referencesFreitas-Astúa, J., Ramos-González, P. L., Arena, G. D., Tassi, A. D., & Kitajima, E. W. (2018). Brevipalpus-transmitted viruses: parallelism beyond a common vector or convergent evolution of distantly related pathogens? Current Opinion in Virology, 33, 66-73. doi:10.1016/j.coviro.2018.07.010es_ES
dc.description.referencesGenovés, A., Pallás, V., & Navarro, J. A. (2011). Contribution of Topology Determinants of a Viral Movement Protein to Its Membrane Association, Intracellular Traffic, and Viral Cell-to-Cell Movement. Journal of Virology, 85(15), 7797-7809. doi:10.1128/jvi.02465-10es_ES
dc.description.referencesGhosh, D., Brooks, R. E., Wang, R., Lesnaw, J., & Goodin, M. M. (2008). Cloning and subcellular localization of the phosphoprotein and nucleocapsid proteins of Potato yellow dwarf virus, type species of the genus Nucleorhabdovirus. Virus Research, 135(1), 26-35. doi:10.1016/j.virusres.2008.02.003es_ES
dc.description.referencesGoodin, M. M., Austin, J., Tobias, R., Fujita, M., Morales, C., & Jackson, A. O. (2001). Interactions and Nuclear Import of the N and P Proteins of Sonchus Yellow Net Virus, a Plant Nucleorhabdovirus. Journal of Virology, 75(19), 9393-9406. doi:10.1128/jvi.75.19.9393-9406.2001es_ES
dc.description.referencesGoodin, M. M., Chakrabarty, R., Yelton, S., Martin, K., Clark, A., & Brooks, R. (2007). Membrane and protein dynamics in live plant nuclei infected with Sonchus yellow net virus, a plant-adapted rhabdovirus. Journal of General Virology, 88(6), 1810-1820. doi:10.1099/vir.0.82698-0es_ES
dc.description.referencesGoodin, M. M., Dietzgen, R. G., Schichnes, D., Ruzin, S., & Jackson, A. O. (2002). pGD vectors: versatile tools for the expression of green and red fluorescent protein fusions in agroinfiltrated plant leaves. The Plant Journal, 31(3), 375-383. doi:10.1046/j.1365-313x.2002.01360.xes_ES
dc.description.referencesHofmann, C., Niehl, A., Sambade, A., Steinmetz, A., & Heinlein, M. (2009). Inhibition of Tobacco Mosaic Virus Movement by Expression of an Actin-Binding Protein. Plant Physiology, 149(4), 1810-1823. doi:10.1104/pp.108.133827es_ES
dc.description.referencesHuang, Y.-W., Geng, Y.-F., Ying, X.-B., Chen, X.-Y., & Fang, R.-X. (2005). Identification of a Movement Protein of Rice Yellow Stunt Rhabdovirus. Journal of Virology, 79(4), 2108-2114. doi:10.1128/jvi.79.4.2108-2114.2005es_ES
dc.description.referencesIdris, A. M., & Brown, J. K. (2004). Cotton leaf crumple virus Is a Distinct Western Hemisphere Begomovirus Species with Complex Evolutionary Relationships Indicative of Recombination and Reassortment. Phytopathology®, 94(10), 1068-1074. doi:10.1094/phyto.2004.94.10.1068es_ES
dc.description.referencesIdris, A. M., Mills-Lujan, K., Martin, K., & Brown, J. K. (2008). Melon Chlorotic Leaf Curl Virus  : Characterization and Differential Reassortment with Closest Relatives Reveal Adaptive Virulence in the Squash Leaf Curl Virus Clade and Host Shifting by the Host-Restricted Bean Calico Mosaic Virus. Journal of Virology, 82(4), 1959-1967. doi:10.1128/jvi.01992-07es_ES
dc.description.referencesKang, S.-H., Bak, A., Kim, O.-K., & Folimonova, S. Y. (2015). Membrane association of a nonconserved viral protein confers virus ability to extend its host range. Virology, 482, 208-217. doi:10.1016/j.virol.2015.03.047es_ES
dc.description.referencesKawakami, S., Watanabe, Y., & Beachy, R. N. (2004). Tobacco mosaic virus infection spreads cell to cell as intact replication complexes. Proceedings of the National Academy of Sciences, 101(16), 6291-6296. doi:10.1073/pnas.0401221101es_ES
dc.description.referencesKondo, H., Chiba, S., Andika, I. B., Maruyama, K., Tamada, T., & Suzuki, N. (2013). Orchid Fleck Virus Structural Proteins N and P Form Intranuclear Viroplasm-Like Structures in the Absence of Viral Infection. Journal of Virology, 87(13), 7423-7434. doi:10.1128/jvi.00270-13es_ES
dc.description.referencesKondo, H., Maeda, T., & Tamada, T. (2003). Orchid Fleck Virus: Brevipalpus californicus Mite Transmission, Biological Properties and Genome Structure. Experimental and Applied Acarology, 30(1-3), 215-223. doi:10.1023/b:appa.0000006550.88615.10es_ES
dc.description.referencesKondo, H., Maruyama, K., Chiba, S., Andika, I. B., & Suzuki, N. (2014). Transcriptional mapping of the messenger and leader RNAs of orchid fleck virus, a bisegmented negative-strand RNA virus. Virology, 452-453, 166-174. doi:10.1016/j.virol.2014.01.007es_ES
dc.description.referencesLeastro, M. O., Castro, D. Y. O., Freitas-Astúa, J., Kitajima, E. W., Pallás, V., & Sánchez-Navarro, J. Á. (2020). Citrus Leprosis Virus C Encodes Three Proteins With Gene Silencing Suppression Activity. Frontiers in Microbiology, 11. doi:10.3389/fmicb.2020.01231es_ES
dc.description.referencesLeastro, M. O., De Oliveira, A. S., Pallás, V., Sánchez-Navarro, J. A., Kormelink, R., & Resende, R. O. (2017). The NSm proteins of phylogenetically related tospoviruses trigger Sw-5b–mediated resistance dissociated of their cell-to-cell movement function. Virus Research, 240, 25-34. doi:10.1016/j.virusres.2017.07.019es_ES
dc.description.referencesLeastro, M. O., Pallás, V., Resende, R. O., & Sánchez-Navarro, J. A. (2017). The functional analysis of distinct tospovirus movement proteins (NS M ) reveals different capabilities in tubule formation, cell-to-cell and systemic virus movement among the tospovirus species. Virus Research, 227, 57-68. doi:10.1016/j.virusres.2016.09.023es_ES
dc.description.referencesLeastro, M. O., Kitajima, E. W., Silva, M. S., Resende, R. O., & Freitas-Astúa, J. (2018). Dissecting the Subcellular Localization, Intracellular Trafficking, Interactions, Membrane Association, and Topology of Citrus Leprosis Virus C Proteins. Frontiers in Plant Science, 9. doi:10.3389/fpls.2018.01299es_ES
dc.description.referencesLeastro, M. O., Pallás, V., Resende, R. O., & Sánchez-Navarro, J. A. (2015). The movement proteins (NSm) of distinct tospoviruses peripherally associate with cellular membranes and interact with homologous and heterologous NSm and nucleocapsid proteins. Virology, 478, 39-49. doi:10.1016/j.virol.2015.01.031es_ES
dc.description.referencesSue Loesch-Fries, L., Halk, E. L., Nelson, S. E., & Krahn, K. J. (1985). Human leukocyte interferon does not inhibit alfalfa mosaic virus in protoplasts or tobacco tissue. Virology, 143(2), 626-629. doi:10.1016/0042-6822(85)90402-7es_ES
dc.description.referencesMann, K. S., Bejerman, N., Johnson, K. N., & Dietzgen, R. G. (2016). Cytorhabdovirus P3 genes encode 30K-like cell-to-cell movement proteins. Virology, 489, 20-33. doi:10.1016/j.virol.2015.11.028es_ES
dc.description.referencesMartin, K. M., Dietzgen, R. G., Wang, R., & Goodin, M. M. (2012). Lettuce necrotic yellows cytorhabdovirus protein localization and interaction map, and comparison with nucleorhabdoviruses. Journal of General Virology, 93(4), 906-914. doi:10.1099/vir.0.038034-0es_ES
dc.description.referencesMartínez-Gil, L., Sánchez-Navarro, J. A., Cruz, A., Pallás, V., Pérez-Gil, J., & Mingarro, I. (2009). Plant Virus Cell-to-Cell Movement Is Not Dependent on the Transmembrane Disposition of Its Movement Protein. Journal of Virology, 83(11), 5535-5543. doi:10.1128/jvi.00393-09es_ES
dc.description.referencesMartínez-Pérez, M., Navarro, J. A., Pallás, V., & Sánchez-Navarro, J. A. (2019). A sensitive and rapid RNA silencing suppressor activity assay based on alfalfa mosaic virus expression vector. Virus Research, 272, 197733. doi:10.1016/j.virusres.2019.197733es_ES
dc.description.referencesMelcher, U. (2000). The ‘30K’ superfamily of viral movement proteins. Microbiology, 81(1), 257-266. doi:10.1099/0022-1317-81-1-257es_ES
dc.description.referencesMoreno, A. B., & López-Moya, J. J. (2020). When Viruses Play Team Sports: Mixed Infections in Plants. Phytopathology®, 110(1), 29-48. doi:10.1094/phyto-07-19-0250-fies_ES
dc.description.referencesNagano, H., Mise, K., Furusawa, I., & Okuno, T. (2001). Conversion in the Requirement of Coat Protein in Cell-to-Cell Movement Mediated by the Cucumber Mosaic Virus Movement Protein. Journal of Virology, 75(17), 8045-8053. doi:10.1128/jvi.75.17.8045-8053.2001es_ES
dc.description.referencesNagano, H., Okuno, T., Mise, K., & Furusawa, I. (1997). Deletion of the C-terminal 33 amino acids of cucumber mosaic virus movement protein enables a chimeric brome mosaic virus to move from cell to cell. Journal of Virology, 71(3), 2270-2276. doi:10.1128/jvi.71.3.2270-2276.1997es_ES
dc.description.referencesNavarro, J. A., Sanchez-Navarro, J. A., & Pallas, V. (2019). Key checkpoints in the movement of plant viruses through the host. Advances in Virus Research, 1-64. doi:10.1016/bs.aivir.2019.05.001es_ES
dc.description.referencesPeiró, A., Cañizares, M. C., Rubio, L., López, C., Moriones, E., Aramburu, J., & Sánchez-Navarro, J. (2014). The movement protein (NSm) ofTomato spotted wilt virusis the avirulence determinant in the tomatoSw-5gene-based resistance. Molecular Plant Pathology, 15(8), 802-813. doi:10.1111/mpp.12142es_ES
dc.description.referencesPeiro, A., Martinez-Gil, L., Tamborero, S., Pallas, V., Sanchez-Navarro, J. A., Mingarro, I., & Simon, A. (2013). The Tobacco mosaic virus Movement Protein Associates with but Does Not Integrate into Biological Membranes. Journal of Virology, 88(5), 3016-3026. doi:10.1128/jvi.03648-13es_ES
dc.description.referencesPeremyslov, V. V., Pan, Y.-W., & Dolja, V. V. (2004). Movement Protein of a Closterovirus Is a Type III Integral Transmembrane Protein Localized to the EndoplasmicReticulum. Journal of Virology, 78(7), 3704-3709. doi:10.1128/jvi.78.7.3704-3709.2004es_ES
dc.description.referencesEdgerton, B. (1996). A new bacilliform virus in Australian Cherax destructor (Decapoda:Parastacidae) with notes on Cherax quadricarinatus bacilliform virus (= Cherax baculovirus). Diseases of Aquatic Organisms, 27, 43-52. doi:10.3354/dao027043es_ES
dc.description.referencesPitzalis, N., & Heinlein, M. (2017). The roles of membranes and associated cytoskeleton in plant virus replication and cell-to-cell movement. Journal of Experimental Botany, 69(1), 117-132. doi:10.1093/jxb/erx334es_ES
dc.description.referencesPowers, J. G., Sit, T. L., Qu, F., Morris, T. J., Kim, K.-H., & Lommel, S. A. (2008). A Versatile Assay for the Identification of RNA Silencing Suppressors Based on Complementation of Viral Movement. Molecular Plant-Microbe Interactions®, 21(7), 879-890. doi:10.1094/mpmi-21-7-0879es_ES
dc.description.referencesShankhwar, N., Singh, R. K., Kothiyal, G. P., Perumal, A., & Srinivasan, A. (2014). Evolution of Magnetic Properties of ${\hbox{CaO}}\hbox{-}{\hbox{P}}_{2}{\hbox{O}}_{5}\hbox{-}{\hbox{Na}}_{2}{\hbox{O}}\hbox{-}{\hbox{Fe}}_{2}{\hbox{O}}_{3}\hbox{-}{\hbox{SiO}}_{2}$ Glass Upon Heat Treatment. IEEE Transactions on Magnetics, 50(1), 1-4. doi:10.1109/tmag.2013.2278570es_ES
dc.description.referencesRamalho, T. O., Figueira, A. R., Sotero, A. J., Wang, R., Geraldino Duarte, P. S., Farman, M., & Goodin, M. M. (2014). Characterization of Coffee ringspot virus-Lavras: A model for an emerging threat to coffee production and quality. Virology, 464-465, 385-396. doi:10.1016/j.virol.2014.07.031es_ES
dc.description.referencesRamos-González, P. L., Chabi-Jesus, C., Guerra-Peraza, O., Tassi, A. D., Kitajima, E. W., Harakava, R., … Freitas-Astúa, J. (2017). Citrus leprosis virus N: A New Dichorhavirus Causing Citrus Leprosis Disease. Phytopathology®, 107(8), 963-976. doi:10.1094/phyto-02-17-0042-res_ES
dc.description.referencesRitzenthaler, C., & Hofmann, C. (s. f.). Tubule-Guided Movement of Plant Viruses. Plant Cell Monographs, 63-83. doi:10.1007/7089_2006_105es_ES
dc.description.referencesRoossinck, M. J. (1997). MECHANISMS OF PLANTVIRUS EVOLUTION. Annual Review of Phytopathology, 35(1), 191-209. doi:10.1146/annurev.phyto.35.1.191es_ES
dc.description.referencesRoy, A., Hartung, J. S., Schneider, W. L., Shao, J., Leon, G., Melzer, M. J., … Brlansky, R. H. (2015). Role Bending: Complex Relationships Between Viruses, Hosts, and Vectors Related to Citrus Leprosis, an Emerging Disease. Phytopathology®, 105(7), 1013-1025. doi:10.1094/phyto-12-14-0375-fies_ES
dc.description.referencesRoy, A., Stone, A. L., Shao, J., Otero-Colina, G., Wei, G., Choudhary, N., … Brlansky, R. H. (2015). Identification and Molecular Characterization of Nuclear Citrus leprosis virus, a Member of the Proposed Dichorhavirus Genus Infecting Multiple Citrus Species in Mexico. Phytopathology®, 105(4), 564-575. doi:10.1094/phyto-09-14-0245-res_ES
dc.description.referencesSambade, A., & Heinlein, M. (2009). Approaching the cellular mechanism that supports the intercellular spread ofTobacco mosaic virus. Plant Signaling & Behavior, 4(1), 35-38. doi:10.4161/psb.4.1.7253es_ES
dc.description.referencesSanchez-Navarro, J., Miglino, R., Ragozzino, A., & Bol, J. F. (2001). Engineering of Alfalfa mosaic virus RNA 3 into an expression vector. Archives of Virology, 146(5), 923-939. doi:10.1007/s007050170125es_ES
dc.description.referencesSánchez-Navarro, J. A., & Bol, J. F. (2001). Role of the Alfalfa mosaic virus Movement Protein and Coat Protein in Virus Transport. Molecular Plant-Microbe Interactions®, 14(9), 1051-1062. doi:10.1094/mpmi.2001.14.9.1051es_ES
dc.description.referencesSánchez-Navarro, J. A., Carmen Herranz, M., & Pallás, V. (2006). Cell-to-cell movement of Alfalfa mosaic virus can be mediated by the movement proteins of Ilar-, bromo-, cucumo-, tobamo- and comoviruses and does not require virion formation. Virology, 346(1), 66-73. doi:10.1016/j.virol.2005.10.024es_ES
dc.description.referencesSánchez-Velázquez, E. J., Santillán-Galicia, M. T., Novelli, V. M., Nunes, M. A., Mora-Aguilera, G., Valdez-Carrasco, J. M., … Freitas-Astúa, J. (2015). Diversity and Genetic Variation among Brevipalpus Populations from Brazil and Mexico. PLOS ONE, 10(7), e0133861. doi:10.1371/journal.pone.0133861es_ES
dc.description.referencesSauvêtre, P., Veniant, E., Croq, G., Tassi, A. D., Kitajima, E. W., Chabi-Jesus, C., … Navia, D. (2018). First Report of Orchid Fleck Virus in the Orchid Collection of Jardin du Luxembourg, Paris, France. Plant Disease, 102(12), 2670-2670. doi:10.1094/pdis-02-18-0371-pdnes_ES
dc.description.referencesTakeda, A., Kaido, M., Okuno, T., & Mise, K. (2004). The C terminus of the movement protein of Brome mosaic virus controls the requirement for coat protein in cell-to-cell movement and plays a role in long-distance movement. Journal of General Virology, 85(6), 1751-1761. doi:10.1099/vir.0.79976-0es_ES
dc.description.referencesTaschner, P. E. M., Van Der Kuyl, A. C., Neeleman, L., & Bol, J. F. (1991). Replication of an incomplete alfalfa mosaic virus genome in plants transformed with viral replicase genes. Virology, 181(2), 445-450. doi:10.1016/0042-6822(91)90876-des_ES
dc.description.referencesTsai, C.-W., Redinbaugh, M. G., Willie, K. J., Reed, S., Goodin, M., & Hogenhout, S. A. (2005). Complete Genome Sequence and In Planta Subcellular Localization of Maize Fine Streak Virus Proteins. Journal of Virology, 79(9), 5304-5314. doi:10.1128/jvi.79.9.5304-5314.2005es_ES
dc.description.referencesVan Dun, C. M. P., Van Vloten-Doting, L., & Bol, J. F. (1988). Expression of alfalfa mosaic virus cDNA1 and 2 in transgenic Tobacco plants. Virology, 163(2), 572-578. doi:10.1016/0042-6822(88)90298-xes_ES
dc.description.referencesWolf, S., Lucas, W. J., Deom, C. M., & Beachy, R. N. (1989). Movement Protein of Tobacco Mosaic Virus Modifies Plasmodesmatal Size Exclusion Limit. Science, 246(4928), 377-379. doi:10.1126/science.246.4928.377es_ES
dc.description.referencesZamyatnin, A. A., Solovyev, A. G., Bozhkov, P. V., Valkonen, J. P. T., Morozov, S. Y., & Savenkov, E. I. (2006). Assessment of the integral membrane protein topology in living cells. The Plant Journal, 46(1), 145-154. doi:10.1111/j.1365-313x.2006.02674.xes_ES
dc.description.sponsorshipThis work was supported by the Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP), proc. 2014/08459, 2015/10249-1, 2017/50222-0, and 2017/19898-8. This work was also supported by grant BIO2017-88321-R from the Spanish Direccion General de Investigacion Cientifica y Tecnica (DGICYT) and the Prometeo Program GV2015/010 from the Generalitat Valenciana.es_ES
dc.description.upvformatpfin22es_ES
dc.description.upvformatpinicio1es_ES
dc.description.volume11es_ES
dc.identifier.doi10.3389/fmicb.2020.571807es_ES
dc.identifier.issn1664-302Xes_ES
dc.identifier.pmcidPMC7672204es_ES
dc.identifier.pmid33250868es_ES
dc.identifier.urihttps://riunet.upv.es/handle/10251/166081
dc.languageIngléses_ES
dc.publisherFrontiers Media SAes_ES
dc.relation.ispartofFrontiers in Microbiologyes_ES
dc.relation.pasarelaS\433224es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/GVA//PROMETEO%2F2015%2F010/ES/Interacciones RNA-proteína y proteína-proteína en procesos de desarrollo y patogénesis mediados por virus y agentes subvirales en cultivos de interés Agronómico (RNAPROT)/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/FAPESP//2017%2F50222-0/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/FAPESP//2017%2F19898-8/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/FAPESP//2015%2F10249-1/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/FAPESP//2014%2F08459/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2017-88321-R/ES/DESCRIFRANDO INTERACCIONES VIRUS-PLANTA ESENCIALES PARA LA SUSCEPTIBILIDAD Y%2FO RESISTENCIA EN DOS PATOSISTEMAS AGRONOMICAMENTE RELEVANTES/es_ES
dc.relation.publisherversionhttps://doi.org/10.3389/fmicb.2020.571807es_ES
dc.relation.references10.1099/vir.0.019950-0es_ES
dc.relation.references10.1099/vir.0.81696-0es_ES
dc.relation.references10.1094/pdis-94-3-0284es_ES
dc.relation.references10.1016/j.virol.2015.05.001es_ES
dc.relation.references10.1093/jee/toaa007es_ES
dc.relation.references10.1016/S0021-9258(19)69848-0es_ES
dc.relation.references10.1094/phyto.2002.92.7.734es_ES
dc.relation.references10.1128/jvi.76.24.12908-12916.2002es_ES
dc.relation.references10.1094/pdis-09-17-1425-rees_ES
dc.relation.references10.1016/0042-6822(92)90183-pes_ES
dc.relation.references10.1007/s10658-019-01854-4es_ES
dc.relation.references10.3390/v6072602es_ES
dc.relation.references10.1128/jvi.02349-06es_ES
dc.relation.references10.1016/j.virusres.2020.197942es_ES
dc.relation.references10.1016/bs.aivir.2018.06.001es_ES
dc.relation.references10.1016/0042-6822(92)90215-bes_ES
dc.relation.references10.1094/pdis.2002.86.12.1402des_ES
dc.relation.references10.1016/j.coviro.2018.07.010es_ES
dc.relation.references10.1128/jvi.02465-10es_ES
dc.relation.references10.1016/j.virusres.2008.02.003es_ES
dc.relation.references10.1128/jvi.75.19.9393-9406.2001es_ES
dc.relation.references10.1099/vir.0.82698-0es_ES
dc.relation.references10.1046/j.1365-313x.2002.01360.xes_ES
dc.relation.references10.1104/pp.108.133827es_ES
dc.relation.references10.1128/jvi.79.4.2108-2114.2005es_ES
dc.relation.references10.1094/phyto.2004.94.10.1068es_ES
dc.relation.references10.1128/jvi.01992-07es_ES
dc.relation.references10.1016/j.virol.2015.03.047es_ES
dc.relation.references10.1073/pnas.0401221101es_ES
dc.relation.references10.1128/jvi.00270-13es_ES
dc.relation.references10.1023/b:appa.0000006550.88615.10es_ES
dc.relation.references10.1016/j.virol.2014.01.007es_ES
dc.relation.references10.3389/fmicb.2020.01231es_ES
dc.relation.references10.1016/j.virusres.2017.07.019es_ES
dc.relation.references10.1016/j.virusres.2016.09.023es_ES
dc.relation.references10.3389/fpls.2018.01299es_ES
dc.relation.references10.1016/j.virol.2015.01.031es_ES
dc.relation.references10.1006/viro.1998.9125es_ES
dc.relation.references10.1016/0042-6822(85)90402-7es_ES
dc.relation.references10.1016/j.virol.2015.11.028es_ES
dc.relation.references10.1099/vir.0.038034-0es_ES
dc.relation.references10.1128/jvi.00393-09es_ES
dc.relation.references10.1016/j.virusres.2019.197733es_ES
dc.relation.references10.1099/0022-1317-81-1-257es_ES
dc.relation.references10.1094/phyto-07-19-0250-fies_ES
dc.relation.references10.1128/jvi.75.17.8045-8053.2001es_ES
dc.relation.references10.1128/jvi.71.3.2270-2276.1997es_ES
dc.relation.references10.1016/bs.aivir.2019.05.001es_ES
dc.relation.references10.1111/mpp.12142es_ES
dc.relation.references10.1128/jvi.03648-13es_ES
dc.relation.references10.1128/jvi.78.7.3704-3709.2004es_ES
dc.relation.references10.3354/dao027043es_ES
dc.relation.references10.1093/jxb/erx334es_ES
dc.relation.references10.1094/mpmi-21-7-0879es_ES
dc.relation.references10.1109/tmag.2013.2278570es_ES
dc.relation.references10.1016/j.virol.2014.07.031es_ES
dc.relation.references10.1094/phyto-02-17-0042-res_ES
dc.relation.references10.1007/7089_2006_105es_ES
dc.relation.references10.1146/annurev.phyto.35.1.191es_ES
dc.relation.references10.1094/phyto-12-14-0375-fies_ES
dc.relation.references10.1094/phyto-09-14-0245-res_ES
dc.relation.references10.4161/psb.4.1.7253es_ES
dc.relation.references10.1007/s007050170125es_ES
dc.relation.references10.1094/mpmi.2001.14.9.1051es_ES
dc.relation.references10.1016/j.virol.2005.10.024es_ES
dc.relation.references10.1371/journal.pone.0133861es_ES
dc.relation.references10.1094/pdis-02-18-0371-pdnes_ES
dc.relation.references10.1099/vir.0.79976-0es_ES
dc.relation.references10.1016/0042-6822(91)90876-des_ES
dc.relation.references10.1128/jvi.79.9.5304-5314.2005es_ES
dc.relation.references10.1016/0042-6822(88)90298-xes_ES
dc.relation.references10.1016/j.febslet.2007.05.082es_ES
dc.relation.references10.1126/science.246.4928.377es_ES
dc.relation.references10.1111/j.1365-313x.2006.02674.xes_ES
dc.relation.references10.1128/JVI.00296-19es_ES
dc.rightsReconocimiento (by)es_ES
dc.rights.accessRightsAbiertoes_ES
dc.subjectDichorhaviruseses_ES
dc.subjectCileviruseses_ES
dc.subjectCitrus leprosis pathosystemes_ES
dc.subjectVirus movementes_ES
dc.subjectIn vivo protein-protein interactiones_ES
dc.subjectProtein membrane association and topologyes_ES
dc.subjectMixed infectiones_ES
dc.titleDichorhaviruses Movement Protein and Nucleoprotein Form a Protein Complex That May Be Required for Virus Spread and Interacts in vivo With Viral Movement-Related Cilevirus Proteinses_ES
dc.typeArtículoes_ES
dc.type.versioninfo:eu-repo/semantics/publishedVersiones_ES
dspace.entity.typePublication
person.identifier246872
person.identifier251790
person.identifier.orcid0000-0003-4954-989X
person.identifier.orcid0000-0002-3320-2827
relation.isAuthorOfPublication44283853-3ee2-44c0-aff2-eece59521d71
relation.isAuthorOfPublication445f244c-4e98-4753-a819-fcb94ca3569c
relation.isAuthorOfPublication.latestForDiscovery44283853-3ee2-44c0-aff2-eece59521d71
relation.isOrgUnitOfPublicatione7a4640e-8a10-48bc-8661-bb4fb3481bd0
relation.isOrgUnitOfPublication.latestForDiscoverye7a4640e-8a10-48bc-8661-bb4fb3481bd0
upv.uuidc3fe7c1f-ea1f-4d8a-8455-7dfde4dcc57fes_ES

Archivos

Bloque original

Mostrando 1 - 1 de 1
Miniatura
Nombre:
Leastro;Fretas-Astúa;Ktajma - Dchorhavruses Movement Proten and Nucleoproten Form a Proten Comple....pdf
Tamaño:
5.57 MB
Formato:
Adobe Portable Document Format
Descripción:
Versión editorial
[object Object] Descargar

Colecciones

Artículos, conferencias, monografías