INVITRO PORE-FORMING ACTIVITY OF THE LANTIBIOTIC NISIN - ROLE OF PROTONMOTIVE FORCE AND LIPID-COMPOSITION
INVITRO PORE-FORMING ACTIVITY OF THE LANTIBIOTIC NISIN - ROLE OF PROTONMOTIVE FORCE AND LIPID-COMPOSITION
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DOI：
10.1111/j.1432-1033.1993.tb17677.x
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发表时间：
1993-03-01
期刊：
影响因子：
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通讯作者：
KONINGS, WN
中科院分区：
文献类型：
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作者：
GARCERA, MJG;ELFERINK, MGL;KONINGS, WN
乳链菌肽是由乳酸乳球菌乳酸亚种（Lactococcus lactis subsp.）乳酸菌。乳链菌肽作用的靶标是革兰氏阳性菌的细胞质膜。乳链菌肽消散膜电位（DELTApsi）并诱导低分子量化合物的流出。已有证据表明乳链菌肽作用需要DELTApsi。研究了乳链菌肽在荧光团羧基荧光素脂质体中的体外作用。乳链菌肽诱导的羧基荧光素流出的情况下，观察到的DELTApsi从脂质体组成的大肠杆菌脂质或二油酰甘油磷酸胆碱（Ole 2GroPCho）在低乳链菌肽/脂质比。羧基荧光素流出的初始速率取决于乳链菌肽/脂质比率，并且在高比率下饱和。DELTApsi（内负）和DELTApH（内碱性）都增强了乳酸链球菌素的作用，而乳酸链球菌素在酸性外部pH值下更有效。用两性离子磷脂Ole 2GroPCho或Ole 2GroPCho与二油酰甘油磷酸乙醇胺和中性糖脂的混合物观察到有效的羧基荧光素流出，而阴离子磷脂具有强烈的抑制作用。它的结论是DELTApsi是不是必不可少的，但总的质子动力刺激乳链菌肽的行动。
Nisin is a lantibiotic produced by some strains of Lactococcus lactis subsp. lactis. The target for nisin action is the cytoplasmic membrane of Gram-positive bacteria. Nisin dissipates the membrane potential (DELTApsi) and induces efflux of low-molecular-mass compounds. Evidence has been presented that a DELTApsi is needed for nisin action. The in vitro action of nisin was studied on liposomes loaded with the fluorophore carboxyfluorescein. Nisin-induced efflux of carboxyfluorescein was observed in the absence of a DELTApsi from liposomes composed of Escherichia coli lipids or dioleoylglycerophosphocholine (Ole2GroPCho) at low nisin/lipid ratios. The initial rate of carboxyfluorescein efflux is dependent on the nisin/lipid ratio and saturates at high ratios. Both DELTApsi (inside negative) and DELTApH (inside alkaline) enhance the action of nisin, while nisin is more potent at acidic external pH values. Efficient carboxyfluorescein efflux is observed with the zwitterionic phospholipid Ole2GroPCho or mixtures of Ole2GroPCho with dioleoylglycerophosphoethanolamine and neutral glycolipids, while anionic phospholipids are strongly inhibitory. It is concluded that a DELTApsi is not essential, but that the total protonmotive force stimulates the action of nisin.