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- Mutational analysis on stable expression and LasB inhibition of LasB propeptide in Pseudomonas aeruginosa
- Youngsun Shin , Xi-Hui Li , Cheol Seung Lee , Joon-Hee Lee
- J. Microbiol. 2022;60(7):727-734. Published online May 25, 2022
- DOI: https://doi.org/10.1007/s12275-022-1671-5
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Abstract
- Three major proteases, elastase B (LasB), protease IV (PIV), and elastase A (LasA) expressed in Pseudomonas aeruginosa play important roles in infections and pathogeneses. These are activated by a proteolytic cascade initiated by the activation of LasB. In this study, we investigated whether LasB could be inhibited using its propeptide (LasBpp). Although LasA and PIV were inhibited by their propeptides, LasB was not inhibited by purified LasBpp because LasB degraded LasBpp. To address this problem, mutant LasBpp variants were constructed to obtain a mutant LasBpp resistant to LasB degradation. A C-terminal deletion series of LasBpp was tested in vivo, and two positive candidates, T2 and T2-1, were selected. However, both caused growth retardation and were unstably expressed in vivo. Since deleting the C-terminal end of LasBpp significantly affected its stable expression, substitution mutations were introduced at the two amino acids near the truncation site of T2-1. The resulting mutants, LasBppE172D, LasBppG173A, and LasBppE172DG173A, significantly diminished LasB activity when overexpressed in vivo and were stably expressed in MW1, a quorum sensing mutant that does not produce LasB. In vitro analysis showed that purified LasBppE172DG173A inhibited LasB activity to a small extent. Summarizing, Cterminal modification of LasBpp profoundly affected the stable expression of LasBpp, and little enhanced the ability of LasBpp to resist degradation by LasB.
- Short-chain fatty acids inhibit the biofilm formation of Streptococcus gordonii through negative regulation of competence-stimulating peptide signaling pathway
- Taehwan Park , Jintaek Im , A Reum Kim , Dongwook Lee , Sungho Jeong , Cheol-Heui Yun , Seung Hyun Han
- J. Microbiol. 2021;59(12):1142-1149. Published online December 4, 2021
- DOI: https://doi.org/10.1007/s12275-021-1576-8
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- 15 Web of Science
- 17 Crossref
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Abstract
- Streptococcus gordonii, a Gram-positive commensal bacterium, is an opportunistic pathogen closely related to initiation and progression of various oral diseases, such as periodontitis and dental caries. Its biofilm formation is linked with the development of such diseases by enhanced resistance against antimicrobial treatment or host immunity. In the present study, we investigated the effect of short-chain fatty acids (SCFAs) on the biofilm formation of S. gordonii. SCFAs, including sodium acetate (NaA), sodium propionate (NaP), and sodium butyrate (NaB), showed an effective inhibitory activity on the biofilm formation of S. gordonii without reduction in bacterial growth. SCFAs suppressed S. gordonii biofilm formation at early time points whereas SCFAs did not affect its preformed biofilm. A quorum-sensing system mediated by competence-stimulating peptide (CSP) is known to regulate biofilm formation of streptococci. Interestingly, SCFAs substantially decreased mRNA expression of comD and comE, which are CSP-sensor and its response regulator responsible for CSP pathway, respectively. Although S. gordonii biofilm formation was enhanced by exogenous synthetic CSP treatment, such effect was not observed in the presence of SCFAs. Collectively, these results suggest that SCFAs have an anti-biofilm activity on S. gordonii through inhibiting comD and comE expression which results in negative regulation of CSP quorum-sensing system. SCFAs could be an effective anti-biofilm agent against S. gordonii for the prevention of oral diseases.
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Citations
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Friederike Uhlig, Niall P. Hyland
Cells.2022; 11(11): 1734. CrossRef - Food-Grade Bacteria Combat Pathogens by Blocking AHL-Mediated Quorum Sensing and Biofilm Formation
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- Potential effects of prebiotic fibers on dental caries: a systematic review
- Improvement in the Stability of Glycinecin A through Protein Fusion of the Two Structural Components
- Youngmee Kim , Somi K. Cho , Moonjae Cho
- J. Microbiol. 2001;39(3):177-180.
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Abstract
- Glycinecin A, a bacteriocin produced by Xanthomonas campestris pv. glycines, inhibits the growth of X. c. pv. vesicatoria. We have reported that purified glycinecin A is composed of two polypeptides, is active over a wide range of pH (6 to 9), and is stable at temperatures up to 60 C. Glycinecin A is a heterodimer consisting of 39- and 14-kDa subunits; the two encoding genes, glyA and glyB, respectively, have been cloned (Heu et al. 2001. Appl. Environ. Microbiol. 67, 4105-4110). Co-expression of glyA and glyB in the same cell is essential for bacteriocin activity. We constructed and produced a chimeric glycinecin A connecting glyA and glyB in one open reading frame. The chimeric glycinecin A has the same bactericidal activity as the wild-type glycinecin A. However, the chimeric glycinecin A is more stable in a wider range of pH and temperature.
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