Human T-cell clones recognize a major M. leprae protein antigen expressed in E. coli

Human T-cell clones recognize a major M. leprae protein antigen expressed in E. coli
复制标题

人类 T 细胞克隆识别大肠杆菌中表达的主要麻风分枝杆菌蛋白抗原

DOI:
--
复制
发表时间:
1986
期刊:
影响因子:
64.8
通讯作者:
T. Godal
T. Godal
中科院分区:
综合性期刊1区
文献类型:
--
作者:
A. Mustafa;H. K. Gill;A. Nerland;W. Britton;V. Mehra;B. Bloom;R. Young;T. Godal

文献摘要

被引文献

相似文献

麻风病是由麻风分枝杆菌引起的一种慢性传染病。与其他细胞内寄生虫一样,保护性免疫依赖于T细胞和细胞介导的免疫1。在动物模型中,用灭活的犰狳衍生的M.麻风引起强烈的T细胞反应、迟发型超敏反应和抵抗活菌攻击的保护作用2 -5。我们最近发现,M。麻风病可在健康志愿者中诱导迟发型超敏反应6。鉴定了M.被T细胞识别并可能参与保护的麻风抗原由于不能在体外培养生物体和难以从有限数量的源自犰狳的芽孢杆菌中纯化抗原而受到阻碍。因为M.通过小鼠单克隆抗体观察到的麻风已经被分离7,8,因此测试这些单个抗原是否被T细胞识别已经成为可能。我们筛选了含有单个M.麻风抗原,使用M.从M.麻风疫苗志愿者用这种方法,我们发现,近一半的M。麻风特异性T细胞克隆被含有M的表位的裂解物刺激增殖。相对分子质量为18,000(18 K)的麻风蛋白。
Leprosy is a chronic infectious disease caused by Mycobacterium leprae. As with other intracellular parasites, protective immunity is dependent on T cells and cell-mediated immunity1. In animal models, immunization with killed armadillo-derived M. leprae elicits strong T-cell responses, delayed-type hypersensitivity and protection against viable challenge2–5. We have recently shown that killed M. leprae can induce delayed-type hypersensitivity in healthy human volunteers6. Identification of the M. leprae antigens that are recognized by T cells and may be involved in protection has been hampered by the inability to cultivate the organism in vitro and by difficulties in antigen purification from limited quantities of armadillo-derived bacillus. Because genes for the major protein antigens of M. leprae as seen by mouse monoclonal antibodies have been isolated7,8, it has become possible to test whether these individual antigens are recognized by T cells. We screened crude λ gtll phage lysates of Escherichia coli containing individual M. leprae antigens using M. leprae-specific T-cell clones isolated from M. leprae-vaccinated volunteers. Using this method, we find that nearly half of the M. leprae-specific T-cell clones are stimulated to proliferate by lysates containing an epitope of a M. leprae protein of relative molecular mass 18,000 (18K).