May 29, 2020

LtEPG1, a secretory endopolygalacturonase protein, regulates the virulence of Lasiodiplodia theobromae in Vitis vinifera and is recognized as an MAMP

Thilini Chethana Kandawatte WedaralalageJiye Yan


The Lasiodiplodia theobromae genome encodes numerous glycoside hydrolases involved in organic matter degradation and conducive to pathogen infection, whereas their molecular mechanisms are still largely unknown. Here, we identified the glycoside hydrolase family 28 endopolygalacturonase LtEPG1 in L. theobromae and characterized its function in detail. LtEPG1 acts as a virulence factor during L. theobromae infection. Over-expression and silencing of LtEPG1 in L. theobromae led to significantly increased and decreased lesion areas, respectively. Further, the high transcript level of LtEPG1 during the infection process supported its virulence function. Polygalacturonase activity of LtEPG1 was substantiated by detecting its ability to degrade pectin. Furthermore, LtEPG1 functioned as microbe-associated molecular patterns during the infection process. Both transient expression of LtEPG1 in planta and infiltration of purified LtEPG1 triggered cell death in Nicotiana benthamiana. Site-directed mutation of LtEPG1 indicated that the enzymatic activity of LtEPG1 is independent from its elicitor activity. A protein kinase, KINβ1, was shown to interact in the yeast two-hybrid system with LtEPG1. This interaction was further confirmed in vi...Continue Reading

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Mentioned in this Paper

Protein KINASE
Vitis vinifera
Purified Protein Derivative of Tuberculin

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