ArticleScientific reports2019
Structural genomics applied to the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine knot and NTF2-like protein folds.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Structure-guided insights into the biology of fungal effectors.The New phytologist · 2025Review
- Surface frustration re-patterning underlies the structural landscape and evolvability of fungal orphan candidate effectors.Nature communications · 2023Article
- In Silico Analysis of aPathogens (Basel, Switzerland) · 2023Article
- Article
- Current Status and Future Perspectives of Genomics Research in the Rust Fungi.International journal of molecular sciences · 2022Review
- The stem rust effector protein AvrSr50 escapes Sr50 recognition by a substitution in a single surface-exposed residue.The New phytologist · 2022Article
- Infection Strategies and Pathogenicity of Biotrophic Plant Fungal Pathogens.Frontiers in microbiology · 2022Review
- Remote homology clustering identifies lowly conserved families of effector proteins in plant-pathogenic fungi.Microbial genomics · 2021Article
- Article
- Proteinaceous effector discovery and characterization in filamentous plant pathogens.Molecular plant pathology · 2020Review
- Smut fungi as a stratagem to characterize rust effectors: opportunities and challenges.World journal of microbiology & biotechnology · 2020Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rust fungi are plant pathogens that secrete an arsenal of effector proteins interfering with plant functions and promoting parasitic infection. Effectors are often species-specific, evolve rapidly, and display low sequence similarities with known proteins. How rust fungal effectors function in host cells remains elusive, and biochemical and structural approaches have been scarcely used to tackle this question. In this study, we produced recombinant proteins of eleven candidate effectors of the leaf rust fungus Melampsora larici-populina in Escherichia coli. We successfully purified and solved the three-dimensional structure of two proteins, MLP124266 and MLP124017, using NMR spectroscopy. Although both MLP124266 and MLP124017 show no sequence similarity with known proteins, they exhibit structural similarities to knottins, which are disulfide-rich small proteins characterized by intricate disulfide bridges, and to nuclear transport factor 2-like proteins, which are molecular containers involved in a wide range of functions, respectively. Interestingly, such structural folds have not been reported so far in pathogen effectors, indicating that MLP124266 and MLP124017 may bear novel functions related to pathogenicity. Our findings show that sequence-unrelated effectors can adopt folds similar to known proteins, and encourage the use of biochemical and structural approaches to functionally characterize effector candidates.
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