ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structures of the flax-rust effector AvrM reveal insights into the molecular basis of plant-cell entry and effector-triggered immunity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 86 citations in OpenAlex.
- Beyond Resistance Genes: Silencing Susceptibility.International journal of molecular sciences · 2026Review
- Structure-guided insights into the biology of fungal effectors.The New phytologist · 2025Review
- Targeting effector proteins of plant pathogens as a strategy for durable plant disease resistance.Frontiers in microbiology · 2025Article
- Effector Pt9226 fromMicroorganisms · 2024Article
- BASIDIN as a New Protein Effector of the Phytopathogen Causing Witche's Broom Disease in Cocoa.International journal of molecular sciences · 2023Article
- Fungal Effectoromics: A World in Constant Evolution.International journal of molecular sciences · 2022Review
- Advances in Fungal Elicitor-Triggered Plant Immunity.International journal of molecular sciences · 2022Review
- Microbial Effectors: Key Determinants in Plant Health and Disease.Microorganisms · 2022Review
- The stem rust effector protein AvrSr50 escapes Sr50 recognition by a substitution in a single surface-exposed residue.The New phytologist · 2022Article
- The haustorium: The root of biotrophic fungal pathogens.Frontiers in plant science · 2022Review
- UhAVR1, an HR-Triggering Avirulence Effector ofJournal of fungi (Basel, Switzerland) · 2020Article
- Whole-genome sequencing of Puccinia striiformis f. sp. tritici mutant isolates identifies avirulence gene candidates.BMC genomics · 2020Article
- Article
- Structural genomics applied to the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine knot and NTF2-like protein folds.Scientific reports · 2019Article
- Structural and functional insights into the modulation of the activity of a flax cytokinin oxidase by flax rust effector AvrL567-A.Molecular plant pathology · 2019Article
- Arms race: diverse effector proteins with conserved motifs.Plant signaling & behavior · 2019Article
- Candidate Effectors FromFrontiers in plant science · 2019Article
- Effectors of plant-colonizing fungi and beyond.PLoS pathogens · 2018Review
- Crystal structure of the Melampsora lini effector AvrP reveals insights into a possible nuclear function and recognition by the flax disease resistance protein P.Molecular plant pathology · 2018Article
- Effectors of Filamentous Plant Pathogens: Commonalities amid Diversity.Microbiology and molecular biology reviews : MMBR · 2017Review
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fungal and oomycete pathogens cause some of the most devastating diseases in crop plants, and facilitate infection by delivering a large number of effector molecules into the plant cell. AvrM is a secreted effector protein from flax rust (Melampsora lini) that can internalize into plant cells in the absence of the pathogen, binds to phosphoinositides (PIPs), and is recognized directly by the resistance protein M in flax (Linum usitatissimum), resulting in effector-triggered immunity. We determined the crystal structures of two naturally occurring variants of AvrM, AvrM-A and avrM, and both reveal an L-shaped fold consisting of a tandem duplicated four-helix motif, which displays similarity to the WY domain core in oomycete effectors. In the crystals, both AvrM variants form a dimer with an unusual nonglobular shape. Our functional analysis of AvrM reveals that a hydrophobic surface patch conserved between both variants is required for internalization into plant cells, whereas the C-terminal coiled-coil domain mediates interaction with M. AvrM binding to PIPs is dependent on positive surface charges, and mutations that abrogate PIP binding have no significant effect on internalization, suggesting that AvrM binding to PIPs is not essential for transport of AvrM across the plant membrane. The structure of AvrM and the identification of functionally important surface regions advance our understanding of the molecular mechanisms underlying how effectors enter plant cells and how they are detected by the plant immune system.
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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.