Hartley M G, Green M, Choules G, Rogers D, Rees D G C, Newstead S, Sjostedt A, Titball R W
Bldg. 245, Defence Science and Technology Laboratory, Porton Down, Salisbury, Wilts SP4 0NS, United Kingdom.
Infect Immun. 2004 Jul;72(7):4109-13. doi: 10.1128/IAI.72.7.4109-4113.2004.
Heat shock proteins (Hsps) have attracted significant attention as protective antigens against a range of diseases caused by bacterial pathogens. However, more recently there have been suggestions that the protective response is due to the presence of peptide components other than Hsps. We have shown that mice that had been immunized with purified heat shock protein 60 (Hsp60) isolated from Francisella tularensis were protected against a subsequent challenge with some strains of the bacterium. However, this protection appeared to be due to trace amounts of lipopolysaccharide, which were too low to be detected by using the Limulus amoebocyte lysate assay. This finding raises the possibility that the protection afforded by other bacterial Hsp60 proteins may be due to trace quantities of polysaccharide antigens carried by and acting in conjunction with the Hsps.
热休克蛋白（Hsps）作为针对一系列由细菌病原体引起的疾病的保护性抗原，已引起了广泛关注。然而，最近有观点认为，这种保护反应是由于存在除Hsps之外的肽成分。我们已经证明，用从土拉弗朗西斯菌中分离出的纯化热休克蛋白60（Hsp60）免疫的小鼠，能抵抗随后该细菌某些菌株的攻击。然而，这种保护作用似乎是由于痕量的脂多糖，其含量过低，无法通过鲎试剂检测法检测到。这一发现增加了一种可能性，即其他细菌Hsp60蛋白所提供的保护作用可能归因于与Hsps结合并共同起作用的痕量多糖抗原。
