Scott J C, Sahl H G, Carne A, Tagg J R
Department of Microbiology, University of Otago, Dunedin, New Zealand.
FEMS Microbiol Lett. 1992 May 15;72(1):97-102. doi: 10.1016/0378-1097(92)90496-b.
Staphylococcus aureus strain 26 inhibited the growth of 23 of 26 lactobacilli of endocervical origin, but only two of 17 staphylococci, in deferred antagonism tests. The inhibitory agent, a bacteriocin-like inhibitory substance (BLIS) named staphylococcin Au-26, was obtained from vigorously shaken liquid cultures containing a 0.1% (v/v) supplement of Tween 80 and was purified by chromatographic fractionation on XAD-2, carboxymethyl Sephadex and reversed phase HPLC. The molecular mass of staphylococcin Au-26 was estimated by SDS-PAGE to be approx. 2700. The detection of lanthionine residues in the molecule, the high stability to heating at acidic but not alkaline pH values and inactivation by proteinases indicate that staphylococcin Au-26 is a member of the lantibiotic class of peptide antibiotics--the first reported to be produced by a S. aureus strain. Primary sequence analysis showed that the N-terminus of the molecule is isoleucine, a characteristic also displayed by the lantibiotics nisin, epidermin and gallidermin.
在延迟拮抗试验中，金黄色葡萄球菌26株抑制了26株宫颈来源乳酸杆菌中23株的生长，但仅抑制了17株葡萄球菌中的2株。一种名为葡萄球菌素Au - 26的类细菌素抑制物质（BLIS）从含有0.1%（v/v）吐温80补充剂的剧烈振荡液体培养物中获得，并通过在XAD - 2、羧甲基葡聚糖凝胶和反相高效液相色谱上的色谱分级分离进行纯化。通过SDS - PAGE估计葡萄球菌素Au - 26的分子量约为2700。分子中羊毛硫氨酸残基的检测、在酸性而非碱性pH值下对加热的高稳定性以及被蛋白酶灭活表明葡萄球菌素Au - 26是肽抗生素羊毛硫抗生素家族的一员——这是首次报道由金黄色葡萄球菌菌株产生的此类物质。一级序列分析表明该分子的N端是异亮氨酸，这也是乳链菌肽、表皮菌素和加里德菌素等羊毛硫抗生素所具有的特征。
