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Búsquedas previas al 2023, Núm. 3. En la sección Volúmenes 30 - 41 (2012 - 2023).
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Potential biological control Mechanisms of Bacillus paralicheniformis TRQ65 against phytopathogenic fungi

By Valeria Valenzuela Ruiz, Fannie Isela Parra Cota, Gustavo Santoyo, María Isabel Estrada Alvarado, Luis Alberto Cira Chávez, Ernestina Castro Longoria, Sergio de los Santos Villalobos*

* Corresponding Author. Email: / Institution:

Received: 01/July/2024 – Published: 18/December/2024DOI: https://doi.org/10.18781/R.MEX.FIT.2024-18

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Abstract Background/Objetive. Bacillus paralicheniformis TRQ65 was isolated from wheat (Triticum turgidum subsp. durum) rhizosphere in commercial fields in the Yaqui Valley, Mexico. This strain was one of the most abundant bacteria in the rhizosphere. The objective of this study is to explore the potential biological control action mechanisms of Bacillus paralicheniformis TRQ65 against phytopathogenic fungi of agricultural importance, through genome sequencing and mining.

Materials and methods. The biocontrol activity of this strain was quantified through in vitro dual assays evaluating inhibition zones against 11 agronomically important fungi. A whole-genome analysis was conducted as genomic mining to evaluate its potential for biological control.

Results. Strain TRQ65 showed biocontrol activity against 45% of the studied fungi, where the highest inhibition was against Botrytis cinerea, 43.8% ± 9% on day 5. Based on genome sequencing and mining (antiSMASH), this bioactivity could be associated with the biosynthesis of lichenysin, bacillibactin, and/or fengycin.

Conclusion. This research provides the first insight into the potential biological control activity of strain TRQ65. Further studies need to be carried out to validate Bacillus paralicheniformis TRQ65 as an active ingredient in sustainable bacterial inoculants for eco-friendly agriculture.

Keywords: Biological Control Agents, Agriculture, Bacillus, Fengycins, Lichenysins, Bacillibactin

Figure 1. Subsystem category distribution of coding DNA sequences (CDS) in the <em>B. paralicheniformis</em> TRQ65 genome, following the RAST pipeline.
Figure 1. Subsystem category distribution of coding DNA sequences (CDS) in the B. paralicheniformis TRQ65 genome, following the RAST pipeline.
Figure 2. A) Bacillibactin structure (National Center for Biotechnology Information, 2024). Bacillibactin is builtaround a trilactone core formed by the cyclization of three molecules of 2,3-dihydroxybenzoic acid (DHB) linked to a central scaffold of threonine residues. The trilactone ring is formed through ester bonds between the hydroxyl groups of the threonine and the carboxyl groups of DHB. Each DHB moiety in bacillibactin contains catechol (2,3-dihydroxybenzoate) functional groups. These catechol groups are responsible for the high-affinity binding of Fe³⁺. B) Lichenysin structure (National Center for Biotechnology Information, 2024). Lichenysin contains a cyclic peptide ring consisting of 13 amino acid residues. Attached to the cyclic peptide core is a lipid tail, typically a β-hydroxy fatty acid chain.The peptide chain forms a cyclic structure through an amide bond between the carboxyl group of one amino acid and the amine group of another, creating a stable ring structure. C) Fengycin structure (National Center for Biotechnology Information, 2024). Fengycin consists of a decapeptide forming a cyclic structure through a lactone linkage. Attached to the peptide ring is a β-hydroxy fatty acid, which can vary in length, usually between 14 and 18 carbon atoms. The exact sequence of amino acids can vary slightly depending on the specific isoform of fengycin.
Figure 2. A) Bacillibactin structure (National Center for Biotechnology Information, 2024). Bacillibactin is builtaround a trilactone core formed by the cyclization of three molecules of 2,3-dihydroxybenzoic acid (DHB) linked to a central scaffold of threonine residues. The trilactone ring is formed through ester bonds between the hydroxyl groups of the threonine and the carboxyl groups of DHB. Each DHB moiety in bacillibactin contains catechol (2,3-dihydroxybenzoate) functional groups. These catechol groups are responsible for the high-affinity binding of Fe³⁺. B) Lichenysin structure (National Center for Biotechnology Information, 2024). Lichenysin contains a cyclic peptide ring consisting of 13 amino acid residues. Attached to the cyclic peptide core is a lipid tail, typically a β-hydroxy fatty acid chain.The peptide chain forms a cyclic structure through an amide bond between the carboxyl group of one amino acid and the amine group of another, creating a stable ring structure. C) Fengycin structure (National Center for Biotechnology Information, 2024). Fengycin consists of a decapeptide forming a cyclic structure through a lactone linkage. Attached to the peptide ring is a β-hydroxy fatty acid, which can vary in length, usually between 14 and 18 carbon atoms. The exact sequence of amino acids can vary slightly depending on the specific isoform of fengycin.
Table 1. Inhibition zone (percentage) of <em>Bacillus paralicheniformis</em> TRQ65 against agriculturally important fungal plant pathogens.
Table 1. Inhibition zone (percentage) of Bacillus paralicheniformis TRQ65 against agriculturally important fungal plant pathogens.