ArticleScientific reports2019
Structure-function relationship of a citrus salicylate methylesterase and role of salicylic acid in citrus canker resistance.
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 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- CitPH4 Confers Resistance to Citrus Canker by Activating Papain-Like Cysteine Protease.Plant biotechnology journal · 2026Article
- Molecular insights into volatile organic compound sensing and signaling in plants.The Plant journal : for cell and molecular biology · 2026Review
- Function and Evolution of the Plant MES Family of Methylesterases.Plants (Basel, Switzerland) · 2024Review
- FourFrontiers in plant science · 2024Article
- Overexpressing CsSABP2 enhances tolerance to Huanglongbing and citrus canker inFrontiers in plant science · 2024Article
- Functional characterization of two flavone synthase II members in citrus.Horticulture research · 2023Article
- Overexpression of the salicylic acid binding protein 2 (SABP2) from tobacco enhances tolerance against Huanglongbing in transgenic citrus.Plant cell reports · 2022Article
- Review
- Overexpression ofFrontiers in plant science · 2022Article
- Physiology and molecular biology of plants : an international journal of functional plant biology · 2021Article
- Article
- Identification and analysis of key genes involved in methyl salicylate biosynthesis in different birch species.PloS one · 2020Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Salicylic acid (SA) and its methyl ester, methyl salicylate (MeSA) are well known inducers of local and systemic plant defense responses, respectively. MeSA is a major mediator of systemic acquired resistance (SAR) and its conversion back into SA is thought to be required for SAR. In many plant species, conversion of MeSA into SA is mediated by MeSA esterases of the SABP2 family. Here we show that the Citrus sinensis SABP2 homologue protein CsMES1 catalyzes the hydrolysis of MeSA into SA. Molecular modeling studies suggest that CsMES1 shares the same structure and SA-binding mode with tobacco SABP2. However, an amino acid polymorphism in the active site of CsMES1-related proteins suggested an important role in enzyme regulation. We present evidence that the side chain of this polymorphic residue directly influences enzyme activity and SA binding affinity in CsMES proteins. We also show that SA and CsMES1 transcripts preferentially accumulate during the incompatible interaction between Xanthomonas aurantifolii pathotype C and sweet orange plants. Moreover, we demonstrate that SA and MeSA inhibited citrus canker caused by Xanthomonas citri, whereas an inhibitor of CsMES1 enhanced canker formation, suggesting that CsMES1 and SA play a role in the local defense against citrus canker bacteria.
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