Bacterial-fungal crosstalk is defined by a fungal lactone mycotoxin and its degradation by a bacterial lactonase.
Autor: | Dor S; Department of Molecular and Computational Biosciences and Biotechnology, Migal-Galilee Research Institute, Kiryat Shmona, Israel., Nudel K; Department of Molecular and Computational Biosciences and Biotechnology, Migal-Galilee Research Institute, Kiryat Shmona, Israel.; Faculty of Sciences and Technology, Tel-Hai College, Upper Galilee, Israel., Eagan JL; Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, Wisconsin, USA., Cohen R; Department of Molecular and Computational Biosciences and Biotechnology, Migal-Galilee Research Institute, Kiryat Shmona, Israel., Hull CM; Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, Wisconsin, USA.; Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA., Keller NP; Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, Wisconsin, USA.; Department of Plant Pathology, University of Wisconsin-Madison, Madison, Wisconsin, USA., Prusky D; Department of Postharvest Science, Agricultural Research Organization, Rishon LeZion, Israel., Afriat-Jurnou L; Department of Molecular and Computational Biosciences and Biotechnology, Migal-Galilee Research Institute, Kiryat Shmona, Israel.; Faculty of Sciences and Technology, Tel-Hai College, Upper Galilee, Israel. |
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Jazyk: | angličtina |
Zdroj: | Applied and environmental microbiology [Appl Environ Microbiol] 2024 Jun 18; Vol. 90 (6), pp. e0029924. Date of Electronic Publication: 2024 May 24. |
DOI: | 10.1128/aem.00299-24 |
Abstrakt: | Bacteria, fungi, and mammals contain lactonases that can degrade the Gram-negative bacterial quorum sensing (QS) molecules N-acyl homoserine lactones (AHLs). AHLs are critical for bacteria to coordinate gene expression and pathogenicity with population density. However, AHL-degrading lactonases present variable substrate ranges, including degradation of the Pencillium expansum lactone mycotoxin patulin. We selected Erwinia spp. as our model bacteria to further investigate this interaction. We find both native apple microbiome Erwinia spp. and the fruit tree pathogen Erwinia amylovora to be inhibited by patulin. At patulin concentrations that inhibited E. amylovora growth, expression of E. amylovora lactonase encoded by EaaiiA was increased. EaAiiA demonstrated the ability to degrade patulin in vitro, as well, as in vivo where it reduced apple disease and patulin production by P. expansum . Fungal-bacterial co-cultures revealed that the E. amylovora Δ eaaiia strain failed to protect apples from P. expansum infections, which contained significant amounts of patulin. Our results suggest that bacterial lactonase production can modulate the pathogenicity of P. expansum in response to the secretion of toxic patulin. Importance: Chemical signaling in the microbial world facilitates the regulation of gene expression as a function of cell population density. This is especially true for the Gram-negative bacterial signal N-acyl homoserine lactone (AHL). Lactonases that deactivate AHLs have attracted a lot of attention because of their antibacterial potential. However, the involvement of these enzymes in inhibiting fungal pathogens and the potential role of these enzymes in bacterial-fungal interactions are unknown. Here, we find that a bacterial enzyme involved in the degradation of AHLs is also induced by and degrades the fungal lactone mycotoxin, patulin. This work supports the potential use of bacterial enzymes and/or the producing bacteria in controlling the post-harvest fruit disease caused by the patulin-producing fungus Penicillium expansum . Competing Interests: D.P. and L.A.-J. are inventors on U.S. patent application no. 18/336,378: “Lactonase and stabilized mutants thereof for treating fungal infections in plants.” L.A.-J. is an inventor on PCT application no. PCT/IL2020/050673, filed on 17 June 2020: “Stabilized mutants of quorum quenching lactonase as an antibacterial treatment for plant pathogens.” |
Databáze: | MEDLINE |
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