ArticleThe Journal of biological chemistry2011
Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
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Who cites it
105 citing papers in PubMed.
- RXLR effectors of Phytophthora infestans: delivery, host targets and immune suppression.Molecular biology reports · 2026Review
- How to frustrate a plant pathogen.The Plant journal : for cell and molecular biology · 2026Review
- Parallel adaptation and admixture drive the evolution of virulence in the grapevine downy mildew pathogen.PLoS pathogens · 2026Article
- Phylogenomics of Plasmopara halstedii Reveals Genomic Regions Associated With the Breakdown of Sunflower Downy Mildew Resistance Genes.Molecular ecology · 2026Article
- Molecular Interactions Between Soil-Borne Oomycetes and Plants: Infection Mechanisms, Host Resistance, and Implications for Sustainable Agriculture.Plants (Basel, Switzerland) · 2026Review
- Pathogenicity and virulence ofVirulence · 2025Review
- Structural Insights Into the Role of RxLR Effectors in the Arms Race Between Oomycetes and Plants.Molecular plant pathology · 2025Review
- Deciphering the Molecular Interplay Between RXLR-EncodedInternational journal of molecular sciences · 2025Review
- Phytophthora Avr3a-Like Effectors Target and Inhibit Cinnamyl Alcohol Dehydrogenase CAD5 to Suppress Plant Immunity.Molecular plant pathology · 2025Article
- Plasmopara viticola Effector PvRXLR10 Targets a Host Phospholipase VvipPLA-IIδ2 to Suppress Plant Immunity in Grapevine.Molecular plant pathology · 2025Article
- Hijacking host metabolism: PstEXLX1 suppresses Triticum aestivum defense responses by targeting a formate dehydrogenase.Plant physiology · 2025Article
- Mutations in the signal peptide of effector gene Pi04314 contribute to the adaptive evolution of the Phytophthora infestans.BMC ecology and evolution · 2025Article
- Dynamics in theBiochemistry · 2025Article
- Computational studies reveal structural characterization and novel families of Puccinia striiformis f. sp. tritici effectors.PLoS computational biology · 2025Article
- Proteolytic processing of both RXLR and EER motifs in oomycete effectors.The New phytologist · 2025Article
- Conserved effector families render Phytophthora species vulnerable to recognition by NLR receptors in nonhost plants.Nature communications · 2024Article
- Effector-Mediated Suppression of Programmed Cell Death byJournal of fungi (Basel, Switzerland) · 2024Article
- A pathogen effector co-opts a host RabGAP protein to remodel pathogen interface and subvert defense-related secretion.Science advances · 2024Article
- Pangenome graph analysis reveals extensive effector copy-number variation in spinach downy mildew.PLoS genetics · 2024Article
- Identification and characterization of specific motifs in effector proteins of plant parasites using MOnSTER.Communications biology · 2024Article
45 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
Abstract
Phytopathogens deliver effector proteins inside host plant cells to promote infection. These proteins can also be sensed by the plant immune system, leading to restriction of pathogen growth. Effector genes can display signatures of positive selection and rapid evolution, presumably a consequence of their co-evolutionary arms race with plants. The molecular mechanisms underlying how effectors evolve to gain new virulence functions and/or evade the plant immune system are poorly understood. Here, we report the crystal structures of the effector domains from two oomycete RXLR proteins, Phytophthora capsici AVR3a11 and Phytophthora infestans PexRD2. Despite sharing <20% sequence identity in their effector domains, they display a conserved core α-helical fold. Bioinformatic analyses suggest that the core fold occurs in ∼44% of annotated Phytophthora RXLR effectors, both as a single domain and in tandem repeats of up to 11 units. Functionally important and polymorphic residues map to the surface of the structures, and PexRD2, but not AVR3a11, oligomerizes in planta. We conclude that the core α-helical fold enables functional adaptation of these fast evolving effectors through (i) insertion/deletions in loop regions between α-helices, (ii) extensions to the N and C termini, (iii) amino acid replacements in surface residues, (iv) tandem domain duplications, and (v) oligomerization. We hypothesize that the molecular stability provided by this core fold, combined with considerable potential for plasticity, underlies the evolution of effectors that maintain their virulence activities while evading recognition by the plant immune system.
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