| Literature DB >> 26780420 |
Yiming Wang1,2, Jingni Wu2,3, Sang Gon Kim1, Kenichi Tsuda2, Ravi Gupta4, Sook-Young Park5, Sun Tae Kim4, Kyu Young Kang1,3.
Abstract
The Magnaporthe oryzae snodprot1 homolog (MSP1), secreted by M. oryzae, is a cerato-platanin family protein. msp1-knockout mutants have reduced virulence on barley leaves, indicating that MSP1 is required for the pathogenicity of rice blast fungus. To investigate the functional roles of MSP1 and its downstream signaling in rice, recombinant MSP1 was produced in Escherichia coli and was assayed for its functionality. Application of MSP1 triggered cell death and elicited defense responses in rice. MSP1 also induced H2O2 production and autophagic cell death in both suspension-cultured cells and rice leaves. One or more protein kinases triggered cell death, jasmonic acid and abscisic acid enhanced cell death, while salicylic acid suppressed it. We demonstrated that the secretion of MSP1 into the apoplast is a prerequisite for triggering cell death and activating defense-related gene expression. Furthermore, pretreatment of rice with a sublethal MSP1 concentration potentiated resistance to the pathogen. Taken together, our results showed that MSP1 induces a high degree of cell death in plants, which might be essential for its virulence. Moreover, rice can recognize MSP1, resulting in the induction of pathogen-associated molecular pattern-triggered immunity.Entities:
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Year: 2016 PMID: 26780420 DOI: 10.1094/MPMI-12-15-0266-R
Source DB: PubMed Journal: Mol Plant Microbe Interact ISSN: 0894-0282 Impact factor: 4.171