Sasaki J, Dejehansart M, De Bruyn J
Department of Bacteriology, Hirosaki University School of Medicine, Japan.
Immunol Cell Biol. 1994 Oct;72(5):415-8. doi: 10.1038/icb.1994.61.
Immunological cross-reactivity between Mycobacterium bovis BCG stress protein (heat shock protein: HSP64) and Meth A tumour cells was analysed by using anti-BCG HSP64 mAb whose recognition epitopes were characterized against BCG HSP64 peptides. By indirect immunofluorescence analysis (IIFA), it was found that one of seven anti-BCG HSP64 mAb, XVIIIG1, bound to the cell surface of Meth A in BALB/c mice. This result was further confirmed by western blot analysis, demonstrating the presence of a 64 kDa protein which reacted with mAb XVIIIG1 that recognizes the 110-123 amino acid peptide of the BCG HSP64. Comparison of the amino acid sequence between the mouse HSP65 and BCG HSP64 recognized by mAb XVIIIG1 revealed 50% amino acid sequence homology. It was concluded from these results that Meth A tumour cells continuously express the stress protein HSP64 as a kind of tumour-associated antigen on the surface of tumour cells.
通过使用抗卡介苗热休克蛋白64（HSP64）单克隆抗体（mAb）分析了牛分枝杆菌卡介苗应激蛋白（热休克蛋白：HSP64）与Meth A肿瘤细胞之间的免疫交叉反应性，该单克隆抗体的识别表位是针对卡介苗HSP64肽进行表征的。通过间接免疫荧光分析（IIFA）发现，七种抗卡介苗HSP64单克隆抗体之一XVIIIG1与BALB/c小鼠体内的Meth A细胞表面结合。蛋白质印迹分析进一步证实了该结果，证明存在一种64 kDa的蛋白质，它与识别卡介苗HSP64 110-123氨基酸肽的单克隆抗体XVIIIG1发生反应。对单克隆抗体XVIIIG1识别的小鼠HSP65和卡介苗HSP64之间的氨基酸序列进行比较，发现氨基酸序列同源性为50%。从这些结果得出结论，Meth A肿瘤细胞在肿瘤细胞表面持续表达应激蛋白HSP64作为一种肿瘤相关抗原。
