Molecular plant-microbe interactions : MPMI · 2015
Cell Death Triggered by a Putative Amphipathic Helix of Radish mosaic virus Helicase Protein Is Tightly Correlated With Host Membrane Modification.
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Hashimoto Masayoshi, Komatsu Ken, Iwai Ryo, Keima Takuya, Maejima Kensaku, Shiraishi Takuya, Ishikawa Kazuya, Yoshida Tetsuya, Kitazawa Yugo, Okano Yukari, Yamaji Yasuyuki, Namba Shigetou
Аннотация
Systemic necrosis is one of the most severe symptoms caused by plant RNA viruses. Recently, systemic necrosis has been suggested to have similar features to a defense response referred to as the hypersensitive response (HR), a form of programmed cell death. In virus-infected plant cells, host intracellular membrane structures are changed dramatically for more efficient viral replication. However, little is known about whether this replication-associated membrane modification is the cause of the symptoms. In this study, we identified an amino-terminal amphipathic helix of the helicase encoded by Radish mosaic virus (RaMV) (genus Comovirus) as an elicitor of cell death in RaMV-infected plants. Cell death caused by the amphipathic helix had features similar to HR, such as SGT1-dependence. Mutational analyses and inhibitor assays using cerulenin demonstrated that the amphipathic helix-induced cell death was tightly correlated with dramatic alterations in endoplasmic reticulum (ER) membrane structures. Furthermore, the cell death-inducing activity of the amphipathic helix was conserved in Cowpea mosaic virus (genus Comovirus) and Tobacco ringspot virus (genus Nepovirus), both of which are classified in the family Secoviridae. Together, these results indicate that ER membrane modification associated with viral intracellular replication may be recognized to prime defense responses against plant viruses.
Предметные рубрики MeSH
Amino Acid SequenceCell DeathCeruleninComovirusDNA HelicasesEndoplasmic ReticulumGenes, ReporterIntracellular MembranesMolecular Sequence DataMutagenesis, Site-DirectedNecrosisPlant DiseasesPlant LeavesProtein Structure, SecondaryRaphanusRecombinant Fusion ProteinsSequence AlignmentNicotianaViral ProteinsVirus Replication