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首页> 外文期刊>Microbial Biotechnology >Saturation mutagenesis of selected residues of the alpha-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity.
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Saturation mutagenesis of selected residues of the alpha-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity.

机译:羊毛硫抗生素乳酸3147的α-肽的选定残基的饱和诱变产生具有增强的抗微生物活性的衍生物。

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摘要

The lantibiotic lacticin 3147 consists of two ribosomally synthesized and post-translationally modified antimicrobial peptides, Ltnalpha and Ltnbeta, which act synergistically against a wide range of Gram-positive microorganisms. We performed saturation mutagenesis of specific residues of Ltnalpha to determine their functional importance. The results establish that Ltnalpha is more tolerant to change than previously suggested by alanine scanning mutagenesis. One substitution, LtnalphaH23S, was identified which improved the specific activity of lacticin 3147 against one pathogenic strain, Staphylococcus aureus NCDO1499. This represents the first occasion upon which the activity of a two peptide lantibiotic has been enhanced through bioengineering.
机译:羊毛硫抗生素乳酸菌素3147由两个核糖体合成的和翻译后修饰的抗菌肽Ltnalpha和Ltnbeta组成,它们对多种革兰氏阳性微生物具有协同作用。我们进行了Ltnalpha特定残基的饱和诱变,以确定其功能重要性。结果证实,Ltnalpha比以前通过丙氨酸扫描诱变所建议的更能耐受变化。鉴定出一种取代LtnalphaH23S,它可以提高乳酸菌素3147对一种病原菌株金黄色葡萄球菌NCDO1499的比活性。这代表了通过生物工程提高两种肽羊毛硫抗生素活性的首次机会。

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