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Pathogen protein modularity enables elaborate mimicry of a host phosphatase

ABSTRACT: Pathogens produce diverse effector proteins to manipulate host cellular processes. However, how functional diversity is generated in an effector repertoire is poorly understood. Many effectors in the devastating plant pathogen Phytophthora contain tandem repeats of the “(L)WY” motif, which are structurally conserved but variable in sequences. Here, we discovered a functional module formed by a specific (L)WY-LWY combination in multiple Phytophthora effectors, which efficiently recruit the Serine/Threonine protein phosphatase 2A (PP2A) core enzyme in plant hosts. Crystal structure of an effector-PP2A complex shows that the (L)WY-LWY module enables hijacking of the host PP2A core enzyme to form functional holoenzymes. While sharing the PP2A-interacting module at the amino terminus, these effectors possess divergent C-terminal LWY units and regulate distinct sets of phosphoproteins in the host. Our results highlight the appropriation of an essential host phosphatase through molecular mimicry by pathogens and diversification promoted by protein modularity in an effector repertoire.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Leaf

SUBMITTER: FRank Menke

LAB HEAD: FRank Menke

PROVIDER: PXD042330 | Pride | 2023-06-26

REPOSITORIES: Pride

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			Action	DRS
	HLI210928_10F.raw	Raw
	HLI210928_11F.raw	Raw
	HLI210928_12F.msf	Msf
	HLI210928_12F.raw	Raw
	HLI210928_1F.raw	Raw

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Pathogen protein modularity enables mimicry of a host phosphatase

Project description:Pathogens rely on a diverse complement of effector proteins to manipulate host cellular processes. The devastating plant pathogen Phytophthora produces numerous effectors that consist of tandem repeats of the “(L)WY” motif. Here, we discovered a specific (L)WY-LWY combination that enables efficient recruitment of the Serine/Threonine protein phosphatase 2A (PP2A) core enzyme in plant hosts. Structural characterization of an effector-PP2A complex and biochemical analyses demonstrate multiple effectors adopt this module at the amino terminus to form functional PP2A holoenzymes but have divergent C-terminal LWY units. Our results discovered a virulence strategy widely employed by Phytophthora in which an essential phosphatase complex of the host is appropriated to promote disease and highlight how diversification in an effector repertoire is promoted by protein modularity.

2024-10-01 | PXD034179 | Pride

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Project description:Phytophthora species are a destructive group of filamentous plant pathogens, which have a global distribution and devastating effect on a wide range of plants important to agriculture and natural ecosystems. Throughout the infection cycle, Phytophthora secrete an effector repertoire into its host to inhibit or counter defence associated compounds, lytic enzymes and intracellular processes required for immunity. Despite the advent of genome sequences of both host and microbe however, little is known about the signal interplay between host and pathogen during infection. Here we explore and report on the association between the hemi-biotrophic broad host range pathogen Phytophthora capsici and tomato. Infection assays reveal a distinct hemi-biotrophic infection cycle, featuring haustoria formation early in infection, followed by necrotrophy in the lateinfection stages. We assessed gene expression changes during infection in both P. capsici and tomato and unveil distinct changes in both host and pathogen transcriptomes, associated with biotrophy and the subsequent switch to necrotrophy. These results suggest dynamic but highly regulated transcriptional programmes that underpin P. capsici hemi-biotrophy. Our results provide new detail on coordinate transcriptional reprogramming during infection and sheds light on the basic processes that accompany hemibiotrophy. Please note the timepoint is hours post inoculation (hpi) of P capsici zoospores on detached tomato leaves. Where it is na (not applicable), these are in vitro cultures of P capsici only.

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