Brown T J, Jardine J, Ison C A
Department of Medical Microbiology, St Mary's Hospital Medical School, Paddington, London, U.K.
Microb Pathog. 1993 Aug;15(2):131-9. doi: 10.1006/mpat.1993.1063.
The response to heat shock in Haemophilus ducreyi has been investigated by labelling newly synthesized proteins with a pulse of 35S-methionine at a range of temperatures between 30-40 degrees C. Proteins were then separated by SDS-PAGE and analysed by autoradiography of the resultant profiles. Four heat shock proteins (HSP) were identified of apparent molecular weight < 14, 58.5, 74 and 78 kDa. The three larger proteins appeared to be independently controlled and inducible in a range of H. ducreyi strains. The protein profiles were also probed by Western blot with serum from an immunized rabbit, serum from a rabbit infected intradermally with H. ducreyi, mouse monoclonal antibodies (MAb) and a pool of human sera from patients with chancroid. The rabbit sera, the human serum pool and MAb (BB11) reacted with epitopes on the HSP of 58.5 kDa, whereas only the immunized rabbit serum and another MAb (CC11) reacted with epitopes on the HSP of 78 kDa. The HSP of 58.5 kDa appears to be immunogenic and may play a part in the host response to H. ducreyi and the pathogenesis of chancroid.
通过在30至40摄氏度的一系列温度下用35S-甲硫氨酸脉冲标记新合成的蛋白质,研究了杜克雷嗜血杆菌对热休克的反应。然后通过SDS-PAGE分离蛋白质,并对所得图谱进行放射自显影分析。鉴定出四种表观分子量分别小于14、58.5、74和78 kDa的热休克蛋白(HSP)。三种较大的蛋白质似乎受独立控制,并且在一系列杜克雷嗜血杆菌菌株中均可诱导产生。还用免疫兔血清、皮内感染杜克雷嗜血杆菌的兔血清、小鼠单克隆抗体(MAb)以及来自软下疳患者的人血清池进行蛋白质印迹法检测蛋白质图谱。兔血清、人血清池和单克隆抗体(BB11)与58.5 kDa热休克蛋白上的表位发生反应,而只有免疫兔血清和另一种单克隆抗体(CC11)与78 kDa热休克蛋白上的表位发生反应。58.5 kDa的热休克蛋白似乎具有免疫原性,可能在宿主对杜克雷嗜血杆菌的反应以及软下疳的发病机制中起作用。