PEPTIDOGLYCAN-ASSOCIATED POLYPEPTIDES OF MYCOBACTERIUM-TUBERCULOSIS
PEPTIDOGLYCAN-ASSOCIATED POLYPEPTIDES OF MYCOBACTERIUM-TUBERCULOSIS
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DOI：
10.1128/jb.172.2.1005-1013.1990
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发表时间：
1990-02-01
影响因子：
3.2
通讯作者：
BRENNAN, PJ
中科院分区：
文献类型：
--
作者：
HIRSCHFIELD, GR;MCNEIL, M;BRENNAN, PJ
重要的基于蛋白质的免疫反应性长期以来一直与分枝杆菌的细胞壁核心相关。为了探索这种活动的分子基础，纯化的结核分枝杆菌细胞壁用十二烷基硫酸钠提取，产生由mycolylarabinogalactan-peptidoglycan复合物和约2%的不可提取的蛋白质组成的不溶性残留物。来自M.无毒力菌株的产物的处理。结核杆菌用三氟甲磺酸释放出一种分子大小为23千道尔顿的单一多肽，占所有不溶性细胞壁蛋白。广泛的纯化，然后分析的23千道尔顿的蛋白质表明，不存在二氨基庚二酸，胞壁酸，或其他肽聚糖组分，指向蛋白质和肽聚糖或非共价，但顽强的协会之间的一种新的连接。释放的23千道尔顿蛋白质显示出与大肠杆菌外膜蛋白OmpF的氨基酸同源性和其他相似性。虽然类似的产物从毒性M的细胞壁中少量释放。结核杆菌Erdman和H37 Rv的细胞壁中，毒性杆菌的细胞壁主要由聚-α-葡聚糖的存在所控制。L-谷氨酰胺，占其重量的10%。聚-α- L-谷氨酰胺被成功地从细胞壁分离，再次证明肽聚糖和聚合物之间不存在共价缔合。这些产品的抗原性进行了论证，并讨论了他们的角色，一个-一个-维斯类似多肽从其他细菌的免疫原性，致病性和细菌生理。
Important protein-based immunoreactivities have long been associated with the cell wall core of mycobacteria. In order to explore the molecular basis of such activities, purified cell walls of Mycobacterium tuberculosis were extracted with sodium dodecyl sulfate to produce an insoluble residue composed of the mycolylarabinogalactan-peptidoglycan complex and about 2% of unextractable protein. Treatment of the product from an avirulent strain of M. tuberculosis with trifluoromethanesulfonic acid released a single polypeptide with a molecular size of 23 kilodaltons, accounting for all of the insoluble cell wall protein. Extensive purification and then analysis of the 23-kilodalton protein demonstrated the absence of diaminopimelic acid, muramic acid, or other peptidolglycan components, pointing to either a novel linkage between protein and peptidoglycan or a noncovalent but tenacious association. The released 23-kilodalton protein showed amino acid homology and other similarities to the outer membrane protein OmpF of Escherichia coli. Although a similar product was released in small quantities from cell walls of the virulent M. tuberculosis Erdman and H37Rv by lysozyme treatment, the cell walls of virulent bacilli were dominated by the presence of poly-.alpha.-l-glutamine, accounting for as much as 10% of their weight. The poly-.alpha.-L-glutamine was successfully separated from the cell wall proper, demonstrating again the absence of a covalent association between peptidoglycan and the polymer. The antigenicity of these products is demonstrated, and their roles vis-a-vis analogous polypeptide from other bacteria in immunogenicity, pathogenicity, and bacterial physiology are discussed.