ISOLATION, IDENTIFICATION, AND STRUCTURAL-ANALYSIS OF THE MYCOBACTINS OF MYCOBACTERIUM-AVIUM, MYCOBACTERIUM-INTRACELLULARE, MYCOBACTERIUM-SCROFULACEUM, AND MYCOBACTERIUM-PARATUBERCULOSIS

ISOLATION, IDENTIFICATION, AND STRUCTURAL-ANALYSIS OF THE MYCOBACTINS OF MYCOBACTERIUM-AVIUM, MYCOBACTERIUM-INTRACELLULARE, MYCOBACTERIUM-SCROFULACEUM, AND MYCOBACTERIUM-PARATUBERCULOSIS
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DOI:
10.1128/jb.164.2.896-903.1985
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发表时间:
1985-01-01
影响因子:
3.2
通讯作者:
RATLEDGE, C
RATLEDGE, C
中科院分区:
生物学3区
文献类型:
--
作者:
BARCLAY, R;EWING, DF;RATLEDGE, C

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设计了从亲缘关系密切的鸟分枝杆菌、胞内分枝杆菌和鞭毛分枝杆菌(即生物体的MAIS复合体)中提纯与细胞相关的铁结合化合物的方法。这三个物种的分枝杆菌蛋白显示出一种结构,这种结构与迄今为止所研究的所有分枝杆菌的分枝杆菌蛋白相同。然而,这些分枝杆菌毒素的独特之处在于它们有不止一个烷基链。曲霉分枝杆菌菌素与其他麦类分枝杆菌菌素的不同之处在于R1烷基链中双键的位置发生了移动。在这三个物种的乙醇提取物中观察到了其他类型的分枝杆菌蛋白,对这些分枝杆菌蛋白的层析性质的检测表明,每个物种都产生了五种类型的分枝杆菌蛋白。每个mycobactin可以通过其R1烷基链的长度进一步细分。这些新的分枝杆菌毒素的产量在不同物种之间没有差异。对3株副结核分枝杆菌和2株禽型分枝杆菌在实验室培养基中反复传代后失去对分枝杆菌生长蛋白的生长要求的菌株的分枝杆菌蛋白进行了薄层层析和高压液相色谱分析。每种生物产生一种与MAIS生物合成的类似的层析性质的Mycobactin。副结核分枝杆菌NADC 18在本实验室至少产生了两个组分,核磁共振分析表明该组分与胞内分枝杆菌M12产生的分枝杆菌蛋白完全相同。然而,Merkal和McCullough(Curr.微生物。7:333-335,1982)分离的副结核分枝杆菌NADC-18菌株与我们分离的菌株不同,似乎与我们在薄层层析中看到的一个微小的Mycobactin组分相对应。这种差异的原因是无法解释的。我们的发现表明,副结核分枝杆菌与MAIS复合体有密切的分类关系。
Methods were devised to purify the cell-associated, iron-binding compounds known as mycobactins from the closely related species Mycobacterium avium, Mycobacterium intracellulare, and Mycobacterium scrofulaceum (i.e., the MAIS complex of organisms). The mycobactins from these three species showed a structure that is common to the mycobactins from all the mycobacteria examined to date. However, these mycobactins were unique in that they had more than one alkyl chain. The M. scrofulaceum mycobactins differed from other MAIS mycobactins by a shift in the position of the double bond in the R1 alkyl chain. Traces of other mycobactin types were observed in ethanol extracts of the three species, and examination of the chromatographic properties of these mycobactins showed that each species produced five mycobactin types. Each mycobactin could be subdivided further by the length of its R1 alkyl chain. No differences in the production of these novel mycobactins were observed among species. Mycobactins from three strains of Mycobacterium paratuberculosis and two wood pigeon strains of Mycobacterium avium which had lost their original growth requirements for mycobactin after repeated subculturing in laboratory growth media were examined by thin-layer chromatography and high-pressure liquid chromatography. Each organism produced a mycobactin with similar chromatographic properties to those synthesized by MAIS organisms. M. paratuberculosis NADC 18 produced at least two components in our laboratory, and nuclear magnetic resonance analysis of the major component showed this mycobactin to be identical to that produced by M. intracellulare M12. However, a sample of mycobactin J isolated by Merkal and McCullough (Curr. Microbiol. 7:333-335, 1982) from M. paratuberculosis NADC 18 was different from our isolates and appeared to correspond to a minor mycobactin component we had seen by thin-layer chromatography. No reason for this difference could be evinced. Our findings indicate that there is a close taxonomic relationship between M. paratuberculosis and the MAIS complex.