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Direct and Indirect Targeting of PP2A by Conserved Bacterial Type-III Effector Proteins
Jin, Lin,Ham, Jong Hyun,Hage, Rosemary,Zhao, Wanying,Soto-Herná,ndez, Jaricelis,Lee, Sang Yeol,Paek, Seung-Mann,Kim, Min Gab,Boone, Charles,Coplin, David L.,Mackey, David Public Library of Science 2016 PLoS pathogens Vol.12 No.5
<▼1><P>Bacterial AvrE-family Type-III effector proteins (T3Es) contribute significantly to the virulence of plant-pathogenic species of <I>Pseudomonas</I>, <I>Pantoea</I>, <I>Ralstonia</I>, <I>Erwinia</I>, <I>Dickeya</I> and <I>Pectobacterium</I>, with hosts ranging from monocots to dicots. However, the mode of action of AvrE-family T3Es remains enigmatic, due in large part to their toxicity when expressed in plant or yeast cells. To search for targets of WtsE, an AvrE-family T3E from the maize pathogen <I>Pantoea stewartii</I> subsp. <I>stewartii</I>, we employed a yeast-two-hybrid screen with non-lethal fragments of WtsE and a synthetic genetic array with full-length WtsE. Together these screens indicate that WtsE targets maize protein phosphatase 2A (PP2A) heterotrimeric enzyme complexes via direct interaction with B’ regulatory subunits. AvrE1, another AvrE-family T3E from <I>Pseudomonas syringae</I> pv. tomato strain DC3000 (<I>Pto</I> DC3000), associates with specific PP2A B’ subunit proteins from its susceptible host Arabidopsis that are homologous to the maize B’ subunits shown to interact with WtsE. Additionally, AvrE1 was observed to associate with the WtsE-interacting maize proteins, indicating that PP2A B’ subunits are likely conserved targets of AvrE-family T3Es. Notably, the ability of AvrE1 to promote bacterial growth and/or suppress callose deposition was compromised in Arabidopsis plants with mutations of PP2A genes. Also, chemical inhibition of PP2A activity blocked the virulence activity of both WtsE and AvrE1 <I>in planta</I>. The function of HopM1, a <I>Pto</I> DC3000 T3E that is functionally redundant to AvrE1, was also impaired in specific PP2A mutant lines, although no direct interaction with B’ subunits was observed. These results indicate that sub-component specific PP2A complexes are targeted by bacterial T3Es, including direct targeting by members of the widely conserved AvrE-family.</P></▼1><▼2><P><B>Author Summary</B></P><P>Gram-negative bacterial pathogens employ type-III effector (T3E) proteins to suppress host immunity and promote disease symptoms. AvrE-family T3Es, which are widely distributed among plant-pathogenic bacteria, suppress host defense responses and also contribute to water-soaking, which is perhaps the most common symptom of bacterial diseases and likely results in the release of nutrients from host cells to promote pathogen growth. Despite the central virulence functions of AvrE-family T3Es, their mode of action remains enigmatic largely due to their cell toxicity. We report here that two AvrE-family T3Es, WtsE from the maize pathogen <I>Pantoea stewartii</I> subsp. <I>stewartii</I> and AvrE1 from the tomato and Arabidopsis pathogen <I>Pseudomonas syringae</I> pv. tomato, each target protein phosphatase 2A (PP2A) complexes in susceptible hosts via direct interaction/association with specific B’ regulatory subunits. Chemical inhibitors were used to demonstrate that PP2A activity is required for the virulence functions of WtsE and AvrE1. PP2A isoform specificity was also tested using mutants of Arabidopsis. More generally, PP2A subunits regulate, both positively and negatively, rapid pattern-triggered immune responses in Arabidopsis. Thus, bacterial T3Es target sub-component specific PP2A complexes to manipulate host immunity and cause disease symptoms during infection.</P></▼2>
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