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首页> 外文期刊>Caries research >A Membrane-Targeted Peptide Inhibiting PtxA of Phosphotransferase System Blocks Streptococcus mutans
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A Membrane-Targeted Peptide Inhibiting PtxA of Phosphotransferase System Blocks Streptococcus mutans

机译：抑制磷酸转移酶体系嵌段的膜靶向肽抑制PTXA嵌段链球菌

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Streptococcus mutans, the primary cause of dental caries, takes up carbohydrates through the phosphoenolpyruvate sugar phosphotransferase system (PTS). This study aimed to identify a novel membrane-targeted antimicrobial peptide (AMP) that could also target the L-ascorbate-specific PtxA component of the S. mutans PTS system. C10-KKWW was identified and selected using virtual screening of a lipopeptide library, a minimum inhibiting concentration (MIC) assay, cytotoxicity assays and a hemolysis assay. Surface plasmon resonance confirmed that C10-KKWW had a high binding affinity for PtxA. Combining with scanning electron microscopy and cell permeability assay, it was shown that the effects of C10-KKWW could be attributed to both membrane and PtxA. Wild type (WT) S. mutans, a ptxA deletion mutant (Delta ptxA), and a mutant-complemented strain (CptxA), were cultured consistently in brain heart infusion (BHI) medium, tryptone-vitamin medium supplemented with 15 mM L-ascorbate (TVL), or for 5 h in BHI supplemented with 7.4 mM sodium L-ascorbate. Compared to Delta ptxA, in WT S. mutans and CptxA, C10-KKWW had a stronger MIC (3.9 mu g/mL), and distinctively decreased biofilm viability. The extracellular concentrations of L-ascorbate/sodium L-ascorbate were not changed before and after WT treated with C10-KKWW. L-ascorbate-induced operon genes, or other PTS genes, were significantly suppressed by C10-KKWW. In conclusion, C10-KKWW has been developed; it acts through interaction with the bacterial membrane and interferes with L-ascorbate translocation to inhibit S. mutans growth and eradicate its biofilm. C10-KKWW may be especially effective at optimal oral ascorbate levels. A combination of C10-KKWW with sodium L-ascorbate might also be a novel strategy for dental caries treatment. (c) 2018 S. Karger AG, Basel
机译：链球菌异常，龋齿的主要原因，通过磷酸丙酸胆盐磷翻转酶系统（PTS）占用碳水化合物。本研究旨在鉴定一种新型膜靶向抗微生物肽（AMP），其也可以靶向S.UlastAns PTS系统的L-抗坏血酸特异性PTXA组分。使用脂肽库的虚拟筛选鉴定并选择C10-KKWW，最小抑制浓度（MIC）测定，细胞毒性测定和溶血测定。表面等离子体共振证实C10-KKWW对PTXA具有高结合亲和力。结合扫描电子显微镜和细胞渗透性测定，表明C10-KKWW的效果可归因于膜和PTXA。野生型（WT）S.Ulans，PTXA缺失突变体（Delta PTXA）和突变互补的菌株（CPTXA）始终培养，均匀培养，培养为15mm L-抗坏血酸（TV1），或在补充有7.4mM抗坏血酸钠的BHI中的5小时。与δPTXA相比，在WT S. mutans和CPTXA中，C10-KKWW具有更强的MIC（3.9μg/ ml），并且具有明显降低的生物膜活力。在用C10-KKWW处理之前和之后，不会改变L-抗坏血酸盐/ L-抗坏血酸的细胞外浓度。 L-抗坏血酸诱导的操纵子基因或其他PTS基因被C10-KKWW显着抑制。总之，已开发C10-KKWW;它通过与细菌膜的相互作用作用，并干扰L-抗坏血酸易位，以抑制S. mutans生长并消除其生物膜。 C10-KKWW在最佳的口服抗坏血酸水平上可能特别有效。 C10-KKWW与L型抗坏血酸钠的组合也可能是龋齿治疗的新策略。 （c）2018年S. Karger AG，巴塞尔

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