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首页> 外文期刊>Infection and immunity >Structure and mapping of antigenic domains of protein antigen b, a 38,000-molecular-weight protein of Mycobacterium tuberculosis.
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Structure and mapping of antigenic domains of protein antigen b, a 38,000-molecular-weight protein of Mycobacterium tuberculosis.

机译：蛋白质抗原b（一种结核分枝杆菌的38,000分子量蛋白质）的抗原域的结构和定位。

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摘要

Only a limited number of proteins from Mycobacterium tuberculosis have so far been shown to possess species-specific epitopes as defined by monoclonal antibodies. One such protein is protein antigen b (Pab) of molecular weight 38,000, which binds the monoclonal antibodies HYT 28, HAT 2, HBT 12, HGT 3, TB 71, and TB 72. The gene encoding this protein was isolated from a lambda gt11 M. tuberculosis DNA library. The nucleotide sequence of the recombinant mycobacterial insert was determined, and an open reading frame of 374 amino acids was identified. The amino acid sequence exhibited 30% homology to a phosphate-binding protein, PstS, from Escherichia coli. The pab gene was subcloned into pBR322 in conjunction with the lacZ gene, and deletions were obtained from the 3' end. The anti-Pab monoclonal antibodies were used to probe crude protein lysates of E. coli transformed with the deletion plasmids. The monoclonal antibodies showed two reactivity patterns; one group of antibodies were dependent on the presence of the ultimate 91 amino acids of the protein, whereas another group of antibodies recognized an antigenic domain located on the middle portion of the molecule. None of the antibodies bound to the N-terminal 117-amino-acid peptide.
机译：迄今为止，仅显示出来自结核分枝杆菌的有限数量的蛋白质具有如单克隆抗体所定义的物种特异性表位。一种这样的蛋白质是分子量为38,000的蛋白质抗原b（Pab），它与单克隆抗体HYT 28，HAT 2，HBT 12，HGT 3，TB 71和TB 72结合。从λ11分离出编码该蛋白质的基因。结核分枝杆菌DNA文库。确定了重组分枝杆菌插入物的核苷酸序列，并鉴定了374个氨基酸的开放阅读框。氨基酸序列与大肠杆菌的磷酸盐结合蛋白PstS具有30％的同源性。将pab基因与lacZ基因一起亚克隆到pBR322中，并从3'端获得了缺失。抗Pab单克隆抗体用于探测用缺失质粒转化的大肠杆菌的粗蛋白裂解物。单克隆抗体表现出两种反应模式：一组抗体取决于蛋白质最终91个氨基酸的存在，而另一组抗体识别位于分子中间部分的抗原结构域。没有抗体与N-末端117-氨基酸肽结合。

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