Dhiman N, Sinha R K, Khuller G K
Department of Biochemistry, Postgraduate Institute of Medical Education & Research, Chandigarh, India.
Indian J Exp Biol. 1998 Jul;36(7):663-7.
Mechanism of immunoprotection and specificity of two highly immunoprotective mycobacterial proteins, viz. 71 and 30 kDa were investigated. The adoptive transfer studies indicated that immunoprotection was mainly mediated by cooperative effect of CD4+ and CD8+ (66.7-73.3% on the basis of percent survival) which was further enhanced marginally by supplementation of B cells, natural killer cells, dendritic cells, macrophages and other immune cells. The specificity studies indicated that both the proteins did not cross react with the unrelated intracellular pathogens i.e. Aspergillus fumigatus, Salmonella typhi and Leishmania donovani as seen by T cell proliferation assay. The protection imparted by these mycobacterial proteins was also specific as the 71 and 30 kDa primed mice did not exhibit any cross protection against sublethal challenge of S typhi. The results indicate 71 and 30 kDa mycobacterial proteins to contain T cell specific epitopes responsible for specific immunoprotection, thus indicating their potential role as antituberculous vaccine candidates.
对两种高度免疫保护性的分枝杆菌蛋白(即71 kDa和30 kDa蛋白)的免疫保护机制和特异性进行了研究。过继转移研究表明,免疫保护主要由CD4+和CD8+的协同作用介导(基于生存率为66.7 - 73.3%),补充B细胞、自然杀伤细胞、树突状细胞、巨噬细胞和其他免疫细胞可使其进一步略有增强。特异性研究表明,通过T细胞增殖试验可见,这两种蛋白均不与无关的细胞内病原体即烟曲霉、伤寒沙门菌和杜氏利什曼原虫发生交叉反应。这些分枝杆菌蛋白所提供的保护也是特异性的,因为用71 kDa和30 kDa蛋白免疫的小鼠对伤寒沙门菌的亚致死攻击未表现出任何交叉保护作用。结果表明,71 kDa和30 kDa分枝杆菌蛋白含有负责特异性免疫保护的T细胞特异性表位,因此表明它们作为抗结核疫苗候选物的潜在作用。