Suneetha L M, Satish P R, Suneetha S, Job C K, Balasubramanian A S
Neurochemistry Laboratory, Christian Medical College Hospital, Vellore, Tamil Nadu, India.
Int J Lepr Other Mycobact Dis. 1997 Sep;65(3):352-6.
To understand Mycobacterium leprae-peripheral nerve interaction, we have investigated the binding of M. leprae to rat peripheral nerve proteins in an in vitro model using 32P-phosphorylated proteins of the peripheral nerve. Intact M. leprae binds to a major phosphorylated protein of 28-30 kDa and, to a minor extent, to a few proteins of molecular weight 45-55 kDa. This binding was more specific for M. leprae since only insignificant binding was observed with other bacteria, such as M. bovis or Escherichia coli. M. leprae did not show binding to several phosphorylated proteins of the rat brain. The 28-30-kDa binding protein of the rat peripheral nerve was found to be a glycoprotein by concanavalin A-Sepharose column chromatography.
为了解麻风分枝杆菌与外周神经的相互作用，我们利用外周神经的32P磷酸化蛋白，在体外模型中研究了麻风分枝杆菌与大鼠外周神经蛋白的结合情况。完整的麻风分枝杆菌与一种主要的28 - 30 kDa磷酸化蛋白结合，在较小程度上还与一些分子量为45 - 55 kDa的蛋白结合。这种结合对麻风分枝杆菌更具特异性，因为用其他细菌，如牛分枝杆菌或大肠杆菌进行检测时，仅观察到微不足道的结合。麻风分枝杆菌未显示与大鼠脑的几种磷酸化蛋白结合。通过伴刀豆球蛋白A - 琼脂糖柱层析法发现，大鼠外周神经的28 - 30 kDa结合蛋白是一种糖蛋白。
