Virus-Induced Necrosis Is a Consequence of Direct Protein-Protein Interaction between a Viral RNA-Silencing Suppressor and a Host Catalase

DOI PDF PubMed 被引用文献12件 オープンアクセス
  • Jun-ichi Inaba
    Research Faculty of Agriculture, Hokkaido University, Sapporo 060–8589, Japan
  • Bo Min Kim
    Research Faculty of Agriculture, Hokkaido University, Sapporo 060–8589, Japan
  • Hanako Shimura
    Research Faculty of Agriculture, Hokkaido University, Sapporo 060–8589, Japan
  • Chikara Masuta
    Research Faculty of Agriculture, Hokkaido University, Sapporo 060–8589, Japan

書誌事項

公開日
2011-08-01
権利情報
  • https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model
DOI
  • 10.1104/pp.111.180042
公開者
Oxford University Press (OUP)

説明

<jats:title>Abstract</jats:title><jats:p>Many plant host factors are known to interact with viral proteins during pathogenesis, but how a plant virus induces a specific disease symptom still needs further research. A lily strain of Cucumber mosaic virus (CMV-HL) can induce discrete necrotic spots on infected Arabidopsis (Arabidopsis thaliana) plants; other CMV strains can induce similar spots, but they are not as distinct as those induced by CMV-HL. The CMV 2b protein (2b), a known RNA-silencing suppressor, is involved in viral movement and symptom induction. Using in situ proximity ligation assay immunostaining and the protoplast assays, we report here that CMV 2b interacts directly with Catalase3 (CAT3) in infected tissues, a key enzyme in the breakdown of toxic hydrogen peroxide. Interestingly, CAT3, normally localized in the cytoplasm (glyoxysome), was recruited to the nucleus by an interaction between 2b and CAT3. Although overexpression of CAT3 in transgenic plants decreased the accumulation of CMV and delayed viral symptom development to some extent, 2b seems to neutralize the cellular catalase contributing to the host defense response, thus favoring viral infection. Our results thus provide evidence that, in addition to altering the type of symptom by disturbing microRNA pathways, 2b can directly bind to a host factor that is important in scavenging cellular hydrogen peroxide and thus interfere specifically with that host factor, leading to the induction of a specific necrosis.</jats:p>

収録刊行物

  • Plant Physiology

    Plant Physiology 156 (4), 2026-2036, 2011-08-01

    Oxford University Press (OUP)

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