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Viral protein suppresses oxidative burst and salicylic acid-dependent autophagy and facilitates bacterial growth on virus-infected plants
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 3676127
Author(s) Zvereva, Anna S.; Golyaev, Victor; Turco, Silvia; Gubaeva, Ekaterina G.; Rajeswaran, Rajendran; Schepetilnikov, Mikhail V.; Srour, Ola; Ryabova, Lyubov A.; Boller, Thomas; Pooggin, Mikhail M.
Author(s) at UniBasel Boller, Thomas
Turco, Silvia
Golyaev, Victor
Year 2016
Title Viral protein suppresses oxidative burst and salicylic acid-dependent autophagy and facilitates bacterial growth on virus-infected plants
Journal New Phytologis
Volume 211
Number 3
Pages / Article-Number 1020-34
Abstract Virus interactions with plant silencing and innate immunity pathways can potentially alter the susceptibility of virus-infected plants to secondary infections with nonviral pathogens. We found that Arabidopsis plants infected with Cauliflower mosaic virus (CaMV) or transgenic for CaMV silencing suppressor P6 exhibit increased susceptibility to Pseudomonas syringae pv. tomato (Pst) and allow robust growth of the Pst mutant hrcC-, which cannot deploy effectors to suppress innate immunity. The impaired antibacterial defense correlated with the suppressed oxidative burst, reduced accumulation of the defense hormone salicylic acid (SA) and diminished SA-dependent autophagy. The viral protein domain required for suppression of these plant defense responses is dispensable for silencing suppression but essential for binding and activation of the plant target-of-rapamycin (TOR) kinase which, in its active state, blocks cellular autophagy and promotes CaMV translation. Our findings imply that CaMV P6 is a versatile viral effector suppressing both silencing and innate immunity. P6-mediated suppression of oxidative burst and SA-dependent autophagy may predispose CaMV-infected plants to bacterial infection.
Publisher Wiley-Blackwell Publishing
ISSN/ISBN 0028-646X ; 1469-8137
edoc-URL http://edoc.unibas.ch/45193/
Full Text on edoc No
Digital Object Identifier DOI 10.1111/nph.13967
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/27120694
ISI-Number WOS:000379937200023
Document type (ISI) Journal Article
 
   

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