MYCOBACTERIUM-LEPRAE PRODUCES EXTRACELLULAR HOMOLOGS OF THE ANTIGEN-85 COMPLEX
MYCOBACTERIUM-LEPRAE PRODUCES EXTRACELLULAR HOMOLOGS OF THE ANTIGEN-85 COMPLEX
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DOI：
10.1128/iai.60.11.4452-4459.1992
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发表时间：
1992-11-01
影响因子：
3.1
通讯作者：
BRENNAN, PJ
中科院分区：
文献类型：
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作者：
VONPESSOLANI, MC;BRENNAN, PJ
抗原85复合物是由结核分枝杆菌和其他分枝杆菌产生的一组至少三种密切相关的30至32 kDa的分泌蛋白（85 A、85 B和85 C）。它们在麻风分枝杆菌（该属的一种专性细胞内病原体）中的突出地位是基于免疫学证据和编码复合物85B蛋白的基因存在的证据而假定的。我们现在已经观察到M.通过使用针对牛分枝杆菌BCG 85 A、85 B和85 C蛋白的单特异性兔抗血清，通过蛋白质印迹（免疫印迹）分析麻风病的各个部分。在未破坏的完整M的提取物中检测到表观分子量为30 kDa的主要交叉反应条带。麻风和从M.麻风病感染的犰狳对该蛋白在细菌内的亚细胞分布的进一步研究证实，它是由生物体分泌的，这一观察结果解释了过去在检测M中抗原85复合物时的困难。麻风病人证实了M.通过肽指纹图谱与BCG产物的肽指纹图谱的比较，获得麻风产物是抗原85复合物的成员。M.麻风抗原85与抗M.牛BCG 85B血清和双向电泳结果表明，85B组分是M.麻风病人M.麻风和BCG 85复合物的新方法重新研究，并受到质疑。然而，用天然蛋白质获得的结果加强了以前的报道，主要来自同源蛋白质的使用，即抗原85复合物是麻风杆菌的主要蛋白质免疫原之一。
The antigen 85 complex is a set of at least three closely related secreted proteins (85A, 85B, and 85C) of 30 to 32 kDa produced by Mycobacterium tuberculosis and other mycobacteria. Their prominence in Mycobacterium leprae, the one obligate intracellular pathogen of the genus, had been assumed on the basis of immunological evidence and proof of the existence of the gene encoding the 85B protein of the complex. We have now observed the production of this family of proteins by M. leprae through analysis of various fractions by Western blotting (immunoblotting) with monospecific rabbit antisera raised against the individual Mycobacterium bovis BCG 85A, 85B, and 85C proteins. A predominant cross-reactive band with an apparent molecular mass of 30 kDa was detected in extracts of nondisrupted whole M. leprae and in soluble fractions prepared from the tissues of M. leprae-infected armadillos. Further studies of the subcellular distribution of this protein within the bacterium confirmed that it is secreted by the organism, an observation that explains past difficulties in detecting the antigen 85 complex in M. leprae. Confirmation that the M. leprae product is a member of the antigen 85 complex was obtained by comparison of peptide fingerprints with those from the BCG product. The pattern of reactivity of the M. leprae antigen 85 complex with anti-M. bovis BCG 85B serum, as well as two-dimensional electrophoresis, established that the 85B component was the predominant member of the complex in M. leprae. The fibronectin-binding capacity of the M. leprae and BCG 85 complexes was reinvestigated by new approaches and is questioned. Nevertheless, the results obtained with the native proteins reinforce previous reports, derived primarily from the use of homologous proteins, that the antigen 85 complex is one of the dominant protein immunogens of the leprosy bacillus.