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Multifaceted Capsid Proteins: Multiple Interactions Suggest Multiple Roles for Pepino mosaic virus Capsid Protein

December 2014 , Volume 27 , Number  12
Pages  1,356 - 1,369

Matthaios M. Mathioudakis,1,2 Luis Rodríguez-Moreno,3 Raquel Navarro Sempere,3 Miguel A. Aranda,3 and Ioannis Livieratos1

1Mediterranean Agronomic Institute of Chania, Department of Sustainable Agriculture, Alsylio Agrokepio, Chania 73100, Greece; 2Plant Pathology Laboratory, Faculty of Agriculture, Aristotle University of Thessaloniki, P.O.B. 269, Thessaloniki 54124, Greece; 3Departamento de Biología del Estrés y Patología Vegetal, Centro de Edafología y Biología Aplicada del Segura (CEBAS)-CSIC, PO Box 164, 30100 Espinardo, Murcia, Spain

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Accepted 14 August 2014.

Pepino mosaic virus (PepMV) (family Alphaflexiviridae, genus Potexvirus) is a mechanically transmitted tomato pathogen that, over the last decade, has evolved from emerging to endemic worldwide. Here, two heat-shock cognate (Hsc70) isoforms were identified as part of the coat protein (CP)/Hsc70 complex in vivo, following full-length PepMV and CP agroinoculation. PepMV accumulation was severely reduced in Hsp70 virus-induced gene silenced and in quercetin-treated Nicotiana benthamiana plants. Similarly, in vitro–transcribed as well as virion RNA input levels were reduced in quercetin-treated protoplasts, suggesting an essential role for Hsp70 in PepMV replication. As for Potato virus X, the PepMV CP and triple gene-block protein 1 (TGBp1) self-associate and interact with each other in vitro but, unlike in the prototype, both PepMV proteins represent suppressors of transgene-induced RNA silencing with different modes of action; CP is a more efficient suppressor of RNA silencing, sequesters the silencing signal by preventing its spread to neighboring cells and its systemic movement. Here, we provide evidence for additional roles of the PepMV CP and host-encoded Hsp70 in viral infection, the first as a truly multifunctional protein able to specifically bind to a host chaperone and to counterattack an RNA-based defense mechanism, and the latter as an essential factor for PepMV infection.

© 2014 The American Phytopathological Society