In Vitro Characterization of an Rgg-Family Regulator from Fish-Derived and Its Modulation by Cyclosporin A.
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| Auteurs principaux: | , , , , , |
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| Format: | Artículo científico |
| Langue: | en |
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Microorganisms
2026
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| _version_ | 1868266053580095488 |
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| author | Tu, Chuandeng He, Libin Lin, Xiangri Zheng, Leyun Zhang, Dongling Lin, Mao |
| author_facet | Tu, Chuandeng He, Libin Lin, Xiangri Zheng, Leyun Zhang, Dongling Lin, Mao Tu, Chuandeng He, Libin Lin, Xiangri Zheng, Leyun Zhang, Dongling Lin, Mao |
| collection | PubMed - marine biology |
| contents | In Vitro Characterization of an Rgg-Family Regulator from Fish-Derived and Its Modulation by Cyclosporin A. Tu, Chuandeng He, Libin Lin, Xiangri Zheng, Leyun Zhang, Dongling Lin, Mao is a major pathogen responsible for streptococcosis in both marine and freshwater fish species, causing substantial economic losses in aquaculture. The increasing prevalence of multidrug resistance has highlighted the urgent need for alternative disease control strategies. Interference with bacterial quorum sensing (QS) systems represents a promising approach. This study aimed to identify and biochemically characterize an Rgg-family transcriptional regulator and evaluate its potential as a target for quorum sensing-related regulatory interference in vitro. We hypothesized that this Rgg regulator may function as a quorum sensing-associated transcription factor capable of promoter binding and modulation by small molecules. Bioinformatic analyses were used to identify the gene encoding an Rgg-family transcriptional regulator and predict its structural features. The gene was cloned, heterologously expressed, and purified. Promoter binding activity was examined using electrophoretic mobility shift assay (EMSA), and key amino acid residues were identified through site-directed mutagenesis. The inhibitory effect of the cyclic peptide cyclosporin A (CsA) on Rgg-promoter binding was further assessed. The gene (864 bp) encoding a 287-amino-acid protein (34.1 kDa) was successfully identified and expressed. Purified Rgg specifically bound to its own promoter region in a concentration-dependent manner. Mutations at conserved arginine residues R12 and R15 within the helix-turn-helix DNA-binding domain abolished promoter binding activity. Furthermore, CsA disturbed Rgg-promoter binding in a dose-dependent manner. This study provides the first in vitro characterization of an Rgg-family transcriptional regulator in fish-derived . The findings expand current understanding of Rgg-family regulators potentially associated with quorum sensing in aquatic streptococci and provide a preliminary basis for further investigation of quorum sensing-related regulatory interference strategies for controlling streptococcal diseases in aquaculture. |
| format | Artículo científico |
| id | pubmed_42075245 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | Microorganisms |
| record_format | pubmed |
| spellingShingle | In Vitro Characterization of an Rgg-Family Regulator from Fish-Derived and Its Modulation by Cyclosporin A. Tu, Chuandeng He, Libin Lin, Xiangri Zheng, Leyun Zhang, Dongling Lin, Mao In Vitro Characterization of an Rgg-Family Regulator from Fish-Derived and Its Modulation by Cyclosporin A. Tu, Chuandeng He, Libin Lin, Xiangri Zheng, Leyun Zhang, Dongling Lin, Mao is a major pathogen responsible for streptococcosis in both marine and freshwater fish species, causing substantial economic losses in aquaculture. The increasing prevalence of multidrug resistance has highlighted the urgent need for alternative disease control strategies. Interference with bacterial quorum sensing (QS) systems represents a promising approach. This study aimed to identify and biochemically characterize an Rgg-family transcriptional regulator and evaluate its potential as a target for quorum sensing-related regulatory interference in vitro. We hypothesized that this Rgg regulator may function as a quorum sensing-associated transcription factor capable of promoter binding and modulation by small molecules. Bioinformatic analyses were used to identify the gene encoding an Rgg-family transcriptional regulator and predict its structural features. The gene was cloned, heterologously expressed, and purified. Promoter binding activity was examined using electrophoretic mobility shift assay (EMSA), and key amino acid residues were identified through site-directed mutagenesis. The inhibitory effect of the cyclic peptide cyclosporin A (CsA) on Rgg-promoter binding was further assessed. The gene (864 bp) encoding a 287-amino-acid protein (34.1 kDa) was successfully identified and expressed. Purified Rgg specifically bound to its own promoter region in a concentration-dependent manner. Mutations at conserved arginine residues R12 and R15 within the helix-turn-helix DNA-binding domain abolished promoter binding activity. Furthermore, CsA disturbed Rgg-promoter binding in a dose-dependent manner. This study provides the first in vitro characterization of an Rgg-family transcriptional regulator in fish-derived . The findings expand current understanding of Rgg-family regulators potentially associated with quorum sensing in aquatic streptococci and provide a preliminary basis for further investigation of quorum sensing-related regulatory interference strategies for controlling streptococcal diseases in aquaculture. |
| title | In Vitro Characterization of an Rgg-Family Regulator from Fish-Derived and Its Modulation by Cyclosporin A. |
| url | https://pubmed.ncbi.nlm.nih.gov/42075245/ |