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首页> 外文期刊>Infection and immunity >Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG.
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Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG.

机译：结核分枝杆菌和牛分枝杆菌BCG释放的纤连蛋白结合抗原的特征。

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Fibronectin (FN)-binding antigens are prominent components of short-term culture supernatants of Mycobacterium tuberculosis. In 3-day-old supernatants, a 30-kilodalton (kDa) protein was identified as the major FN-binding molecule. In 21-day-old supernatants, FN bound to a double protein band of 30 and 31 kDa, as well as to a group of antigens of larger molecular mass (57 to 60 kDa). FN-binding molecules in this size range, but not of 30 to 31 kDa, were also found in sonicates. We showed that the 31- and 30-kDa FN-binding bands correspond to components A and B of the BCG85 complex, previously shown to be abundant in culture supernatants of Mycobacterium bovis BCG. Thus, a polyclonal antibody to the BCG85 complex bound to the 30- and 31-kDa antigens and inhibited binding of FN to them on immunoblots of the culture filtrates. Similarly, FN bound to the purified components of the BCG85 complex, and this binding was blocked by the antibody. A monoclonal antibody, HYT27, also bound both to the BCG85 components A and B and to the 30- and 31-kDa FN-binding molecules of M. tuberculosis, but it did not block the binding of FN. Related molecules appear to be present on the surface of BCG and to mediate the binding of BCG to FN-coated plastic surfaces, since this binding could also be blocked by the polyclonal anti-BCG85 antibody and by the purified components of BCG85, particularly component A, but not by monoclonal antibody HYT27. The binding of these mycobacterial antigens to FN appears to be of very high affinity, and we suggest that this property of major secreted antigens of M. tuberculosis indicates an important role in mycobacterial disease and in the binding of BCG to tumor cells during immunotherapy of bladder cancer.
机译：纤连蛋白（FN）结合抗原是结核分枝杆菌短期培养上清液的重要组成部分。在3天大的上清液中，一种30千达尔顿（kDa）的蛋白质被确定为主要的FN结合分子。在21天大的上清液中，FN结合到30和31 kDa的双蛋白条带，以及更大分子量（57至60 kDa）的一组抗原上。在超声中也发现了这个大小范围内的FN结合分子，但不是30到31 kDa。我们显示31 kDa和30 kDa FN结合带对应于BCG85复合物的组分A和B，先前显示在牛分枝杆菌BCG的培养上清液中含量丰富。因此，针对BCG85复合物的多克隆抗体与30 kDa和31 kDa抗原结合，并在培养滤液的免疫印迹上抑制了FN与它们的结合。同样，FN与BCG85复合物的纯化成分结合，并且这种结合被抗体阻断。单克隆抗体HYT27也与BCG85组分A和B以及结核分枝杆菌的30 kDa和31 kDa FN结合分子都结合，但它并未阻断FN的结合。相关的分子似乎存在于BCG的表面上，并介导BCG与FN包被的塑料表面的结合，因为这种结合也可能被多克隆抗BCG85抗体和BCG85的纯化成分（尤其是成分A）阻断，而不是单克隆抗体HYT27。这些分枝杆菌抗原与FN的结合似乎具有很高的亲和力，我们建议结核分枝杆菌主要分泌抗原的这一特性表明在分枝杆菌疾病以及BCG与膀胱细胞免疫疗法中BCG与肿瘤细胞的结合中起着重要作用。癌症。

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