ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structural basis for the recognition-evasion arms race between Tomato mosaic virus and the resistance gene Tm-1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 48 citations in OpenAlex.
- Harnessing genomics for fast development and commercial introduction of high-resistant tomato varieties to Tomato Brown Rugose Fruit Virus.Breeding science · 2026Article
- Durable Management of Plant Viruses: Insights into Host Resistance and Tolerance Mechanisms.Biology · 2026Review
- BreedingFrontiers in plant science · 2026Article
- MarK, a Novosphingobium aromaticivorans kinase required for catabolism of multiple aromatic monomers.The Journal of biological chemistry · 2025Article
- Tm-1 back in business: an allele from Solanum pennellii accessions plays a major role in ToBRFV resistance.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- Genomic Diversity of Tomato Brown Rugose Fruit Virus in Canadian Greenhouse Production Systems.Viruses · 2025Article
- Tobacco Mosaic Virus Movement: From Capsid Disassembly to Transport Through Plasmodesmata.Viruses · 2025Review
- Tissue-specific resistance and susceptibility to the tomato brown rugose fruit virus (ToBRFV) conferred by Solanum pennellii loci.BMC plant biology · 2025Article
- Advances in understanding the interaction betweenPlant signaling & behavior · 2024Review
- Engineered Resistance to Tobamoviruses.Viruses · 2024Review
- Plant Immunity against Tobamoviruses.Viruses · 2024Review
- The Resistance of Soybean Variety Heinong 84 to Apple Latent Spherical Virus Is Controlled by Two Genetic Loci.International journal of molecular sciences · 2024Article
- Advances and Prospects of Virus-Resistant Breeding in Tomatoes.International journal of molecular sciences · 2023Review
- Signaling and Resistosome Formation in Plant Innate Immunity to Viruses: Is There a Common Mechanism of Antiviral Resistance Conserved across Kingdoms?International journal of molecular sciences · 2023Review
- In silico study on the Hepatitis E virus RNA Helicase and its inhibition by silvestrol, rocaglamide and other flavagline compounds.Scientific reports · 2022Article
- Transcriptomic and genomic analysis provides new insights in molecular and genetic processes involved in zucchini ZYMV tolerance.BMC genomics · 2022Article
- Resistance to Turnip Mosaic Virus in the FamilyThe plant pathology journal · 2021Review
- Eighty years of gene-for-gene relationship and its applications in identification and utilization ofJournal of genetics · 2021Review
- The Plant Noncanonical Antiviral Resistance Protein JAX1 Inhibits Potexviral Replication by Targeting the Viral RNA-Dependent RNA Polymerase.Journal of virology · 2019Article
- Binding studies between cytosinpeptidemycin and the superfamily 1 helicase protein of tobacco mosaic virus.RSC advances · 2018Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tomato mosaic virus (ToMV) resistance gene Tm-1 encodes a protein that shows no sequence homology to functionally characterized proteins. Tm-1 binds ToMV replication proteins and thereby inhibits replication complex formation. ToMV mutants that overcome this resistance have amino acid substitutions in the helicase domain of the replication proteins (ToMV-Hel). A small region of Tm-1 in the genome of the wild tomato Solanum habrochaites has been under positive selection during its antagonistic coevolution with ToMV. Here we report crystal structures for the N-terminal inhibitory domains of Tm-1 and a natural Tm-1 variant with an I91-to-T substitution that has a greater ability to inhibit ToMV RNA replication and their complexes with ToMV-Hel. Each complex contains a Tm-1 dimer and two ToMV-Hel monomers with the interfaces between Tm-1 and ToMV-Hel bridged by ATP. Residues in ToMV-Hel and Tm-1 involved in antagonistic coevolution are found at the interface. The structural differences between ToMV-Hel in its free form and in complex with Tm-1 suggest that Tm-1 affects nucleoside triphosphatase activity of ToMV-Hel, and this effect was confirmed experimentally. Molecular dynamics simulations of complexes formed by Tm-1 with ToMV-Hel variants showed how the amino acid changes in ToMV-Hel impair the interaction with Tm-1 to overcome the resistance. With these findings, together with the biochemical properties of the interactions between ToMV-Hel and Tm-1 variants and effects of the mutations in the polymorphic residues of Tm-1, an atomic view of a step-by-step coevolutionary arms race between a plant resistance protein and a viral protein emerges.
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