ArticleThe Plant cell2005
Structure of Ptr ToxA: an RGD-containing host-selective toxin from Pyrenophora tritici-repentis.
Article in The Plant cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 135 citations in OpenAlex.
- Structure-guided insights into the biology of fungal effectors.The New phytologist · 2025Review
- Computational studies reveal structural characterization and novel families of Puccinia striiformis f. sp. tritici effectors.PLoS computational biology · 2025Article
- Divergent ECC1 effector homologs modulate host-specific virulence in cucurbit-infectingFrontiers in cellular and infection microbiology · 2025Article
- Dual RNA-seq reveals distinct families of co-regulated and structurally conserved effectors in Botrytis cinerea infection of Arabidopsis thaliana.BMC biology · 2024Article
- Template-Based Modelling of the Structure of Fungal Effector Proteins.Molecular biotechnology · 2024Article
- The structural repertoire ofeLife · 2024Article
- Induced responses to the wheat pathogen: Tan Spot-(Pyrenophora tritici-repentis) in wheat (Triticum aestivum) focus on changes in defence associated and sugar metabolism.Metabolomics : Official journal of the Metabolomic Society · 2024Article
- Heterologous expression and characterization of ToxA1 haplotype from India and its interaction with Tsn1 for spot blotch susceptibility in spring wheat.Molecular biology reports · 2023Article
- Mildew RALPHs up in arms with cereals.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Ab Initio Modelling of the Structure of ToxA-like and MAX Fungal Effector Proteins.International journal of molecular sciences · 2023Article
- Prediction of effector protein structures from fungal phytopathogens enables evolutionary analyses.Nature microbiology · 2023Article
- Article
- A new family of structurally conserved fungal effectors displays epistatic interactions with plant resistance proteins.PLoS pathogens · 2022Article
- Systematic identification and functional characterization of the CFEM proteins in poplar fungusFrontiers in cellular and infection microbiology · 2022Article
- Remote homology clustering identifies lowly conserved families of effector proteins in plant-pathogenic fungi.Microbial genomics · 2021Article
- Simple and efficient heterologous expression of necrosis-inducing effectors using the model plantPlant direct · 2021Article
- Proteinaceous effector discovery and characterization in filamentous plant pathogens.Molecular plant pathology · 2020Review
- Genome-Wide Identification of Effector Candidates With Conserved Motifs From the Wheat Leaf Rust FungusFrontiers in microbiology · 2020Article
- Arms race: diverse effector proteins with conserved motifs.Plant signaling & behavior · 2019Article
- Structure-function analysis of the Fusarium oxysporum Avr2 effector allows uncoupling of its immune-suppressing activity from recognition.The New phytologist · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Tan spot of wheat (Triticum aestivum), caused by the fungus Pyrenophora tritici-repentis, has significant agricultural and economic impact. Ptr ToxA (ToxA), the first discovered proteinaceous host-selective toxin, is produced by certain P. tritici-repentis races and is necessary and sufficient to cause cell death in sensitive wheat cultivars. We present here the high-resolution crystal structure of ToxA in two different crystal forms, providing four independent views of the protein. ToxA adopts a single-domain, beta-sandwich fold of novel topology. Mapping of the existing mutation data onto the structure supports the hypothesized importance of an Arg-Gly-Asp (RGD) and surrounding sequence. Its occurrence in a single, solvent-exposed loop in the protein suggests that it is directly involved in recognition events required for ToxA action. Furthermore, the ToxA structure reveals a surprising similarity with the classic mammalian RGD-containing domain, the fibronectin type III (FnIII) domain: the two topologies are related by circular permutation. The similar topologies and the positional conservation of the RGD-containing loop raises the possibility that ToxA is distantly related to mammalian FnIII proteins and that to gain entry it binds to an integrin-like receptor in the plant host.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.