Lim Y, Shin S H, Jang I Y, Rhee J H, Kim I S
Department of Microbiology, Chosun University Medical School, Dong-Gu, Kwangju, South Korea.
FEMS Microbiol Lett. 1998 Sep 15;166(2):225-30. doi: 10.1111/j.1574-6968.1998.tb13894.x.
To understand human immune responses against the human transferrin-binding protein of Staphylococcus aureus (SA-tbp), we examined cell wall proteins from S. aureus ATCC 6538 using human convalescent sera, and a monoclonal antibody specific for human transferrin receptor (McAb-HTR). The SA-tbp, detected by immunoblot assay, was iron-repressible, reacted with the convalescent sera, and cross-reacted with McAb-HTR. Immunoelectron microscopy probed with McAb-HTR showed a reaction zone around the test strain from the deferrated BHI. After being preincubated with an S. aureus-bacteremic serum, the electroblot of the SA-tbp still reacted with McAb-HTR, but not with human transferrin-horseradish peroxidase conjugate. We conclude, there are at least two kinds of epitopes in the SA-tbp; one able to bind to human transferrin is immunogenic in humans, but the other sharing epitopes common with human transferrin receptor is not immunogenic in humans.
为了解人类针对金黄色葡萄球菌转铁蛋白结合蛋白（SA-tbp）的免疫反应，我们使用人类恢复期血清和一种针对人类转铁蛋白受体的单克隆抗体（McAb-HTR）检测了金黄色葡萄球菌ATCC 6538的细胞壁蛋白。通过免疫印迹分析检测到的SA-tbp受铁抑制，与恢复期血清发生反应，并与McAb-HTR发生交叉反应。用McAb-HTR进行免疫电子显微镜检测显示，来自脱铁脑心浸液肉汤（deferrated BHI）的测试菌株周围有一个反应区。在用金黄色葡萄球菌菌血症血清预孵育后，SA-tbp的电印迹仍与McAb-HTR反应，但不与人转铁蛋白-辣根过氧化物酶偶联物反应。我们得出结论，SA-tbp中至少存在两种表位；一种能够与人转铁蛋白结合，在人类中具有免疫原性，但另一种与人转铁蛋白受体共享共同表位，在人类中不具有免疫原性。
