The WY Domain of an RxLr Effector Drives Interactions with a Host Target Phosphatase to Mimic Host Regulatory Proteins and Promote Phytophthora infestans Infection

Molecular Plant-Microbe Interactions, Journal Year: 2023, Volume and Issue: 37(3), P. 239 - 249

Published: Nov. 3, 2023

Plant pathogens manipulate the cellular environment of host to facilitate infection and colonization that often lead plant diseases. To accomplish this, many specialized secrete virulence proteins called effectors into cell, which subvert processes such as immune signaling, gene transcription, metabolism. Phytophthora infestans, causative agent potato late blight, employs an expanded repertoire RxLR with WY domains through direct interaction protein targets. However, our understanding molecular mechanisms underlying interactions between their targets remains limited. In this study, we performed a structural biophysical characterization P. infestans effector Pi04314 in complex Protein Phosphatase 1-c (PP1c). We elucidate how uses domain C-terminal loop carrying KVxF motif interact conserved surfaces on PP1c, known be used by regulatory for guiding function. Through planta analyses, demonstrate or mutants lose ability bind PP1c. The loss PP1c binding correlates changes nucleolar localization decrease lesion size assays. This study provides insights manipulation hosts pathogens, revealing exploit key interfaces modify function disease. [Formula: see text] Copyright © 2024 Author(s). is open access article distributed under CC BY 4.0 International license.

Language: Английский

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“Order from disordered”: Potential role of intrinsically disordered regions in phytopathogenic oomycete intracellular effector proteins

Current Opinion in Plant Biology, Journal Year: 2023, Volume and Issue: 75, P. 102402 - 102402

Published: June 16, 2023

There is a continuous arms race between pathogens and their host plants. However, successful pathogens, such as phytopathogenic oomycetes, secrete effector proteins to manipulate defense responses for disease development. Structural analyses of these reveal the existence regions that fail fold into three-dimensional structures, intrinsically disordered (IDRs). Because flexibility, are involved in important biological functions proteins, effector-host protein interactions perturb immune responses. Despite significance, role IDRs oomycete not clear. This review, therefore, searched literature functionally characterized intracellular effectors with known interactors. We further classify mediate globular or binding sites proteins. To fully appreciate potential IDRs, five encoding were used case studies. also propose pipeline can be identify, well characterize Understanding aid development new disease-control strategies.

Language: Английский

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A pathogen effector co-opts a host RabGAP protein to remodel pathogen interface and subvert defense-related secretion

Science Advances, Journal Year: 2024, Volume and Issue: 10(40)

Published: Oct. 4, 2024

Pathogens have evolved sophisticated mechanisms to manipulate host cell membrane dynamics, a crucial adaptation survive in hostile environments shaped by innate immune responses. Plant-derived interfaces, engulfing invasive hyphal projections of fungal and oomycete pathogens, are prominent junctures dictating infection outcomes. Understanding how pathogens transform these host-pathogen interfaces their advantage remains key biological question. Here, we identified conserved effector, secreted plant pathogenic oomycetes, that co-opts Rab GTPase-activating protein (RabGAP), TOPGAP, remodel the interface. The PiE354, hijacks TOPGAP as susceptibility factor usurp its GAP activity on Rab8a, GTPase for defense-related secretion. By hijacking PiE354 purges Rab8a from plasma membrane, diverting Rab8a-mediated trafficking away pathogen This mechanism signifies an uncanny evolutionary effector co-opting regulatory component subvert secretion, thereby providing unprecedented mechanistic insights into reprogramming dynamics pathogens.

Language: Английский

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Structure determinants of DANGEROUS MIX 3, an alpha/beta hydrolase, for triggering NLR-mediated genetic incompatibility in plants

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Nov. 1, 2024

SUMMARY Genetic incompatibility occurs when a mismatched pair of plant immune components mounts autoimmune responses in hybrids. Highly diversified NLR receptors are main culprits the genetic conflict, recognizing host proteins from different origin as trigger. Here, we report molecular mechanism underlying DANGEROUS MIX (DM) autoimmunity, comprising DM2h/RPP1 and its incompatible partner DM3, an alpha/beta hydrolase. Cryo-electron microscopy reveals oligomeric nature two natural DM3 variants trimer dimer configuration. The polymorphism triggering autoimmunity is located at interface, resulting drastic structural differences such that dimerizing helix loop reinforcing interface lost disordered. Structure-function analysis shows integrity but neither maintenance hexamer nor enzymatic activity, key factor contributing to autoimmunity. Our finding pinpoints checkpoints embedded configuration enzyme controls switching activity.

Language: Английский

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An RXLR effector disrupts vesicle trafficking at ER-Golgi interface for Phytophthora capsici pathogenicity

Molecules and Cells, Journal Year: 2024, Volume and Issue: unknown, P. 100158 - 100158

Published: Nov. 1, 2024

Phytophthora species, an oomycetes plant pathogen, secrete effectors into cell throughout their life cycle for manipulating host immunity to achieve successful colonization. However, the molecular mechanisms underlying effector-triggered necrotic death remain elusive. In this study, we identified RXLR effector (Pc12) from capsici which contributes virulence and induces necrosis by triggering a distinct endoplasmic reticulum (ER) stress response through its interaction with Rab13-2. The induced Pc12 did not exhibit conventional (ETI)-mediated hypersensitive death, including involvement of NLR downstream signaling components transcriptional reprogramming defense-related genes. Instead, it alters localization ER-resident proteins confines secretory within ER. directly interacts Rab13-2, is primarily localized ER Golgi apparatus, resulting in diminished Rab13-2 signal on apparatus. Furthermore, exhibits increased affinity interactor, Rab escort protein 1 (REP1), presence Pc12. Structural predictions revealed that specific residue crucial binding C-terminus Substitution reduced impaired P. infection, while maintaining REP1 prenylated acceptor (PRA1). These findings provide insight how pathogen form facilitate colonization disrupting recycling involved vesicle trafficking at ER-Golgi interface.

Language: Английский

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