Weis J J, Ma Y, Erdile L F
Department of Pathology, University of Utah School of Medicine, Salt Lake City 84132.
Infect Immun. 1994 Oct;62(10):4632-6. doi: 10.1128/iai.62.10.4632-4636.1994.
Borrelia burgdorferi lipoproteins are 50- to 500-fold more active as cytokine inducers and B-cell mitogens than Escherichia coli lipoproteins and synthetic peptides containing the tripalmitoyl-S-glyceryl-cysteine moiety. To investigate the source of this unique potency, we compared native OspA from B. burgdorferi with recombinant lipidated OspA produced in E. coli. As little as 10 ng of either protein per ml stimulated B-cell proliferation and production of cytokines and nitric oxide by macrophages. The two proteins induced comparable antibody responses in mice. Nonlipidated OspA made in E. coli had no stimulatory activity. Thus, lipid modification is essential both in vivo and in vitro for the immunological properties of OspA. The lipid moiety appears equally active whether produced in B. burgdorferi or in E. coli.
与大肠杆菌脂蛋白以及含有三棕榈酰-S-甘油基-半胱氨酸部分的合成肽相比，伯氏疏螺旋体脂蛋白作为细胞因子诱导剂和B细胞丝裂原的活性要高50至500倍。为了研究这种独特效力的来源，我们将伯氏疏螺旋体的天然OspA与在大肠杆菌中产生的重组脂化OspA进行了比较。每毫升低至10纳克的任何一种蛋白质均可刺激B细胞增殖以及巨噬细胞产生细胞因子和一氧化氮。这两种蛋白质在小鼠体内诱导出了相当的抗体反应。在大肠杆菌中产生的未脂化OspA没有刺激活性。因此，脂质修饰对于OspA的免疫特性在体内和体外都是必不可少的。无论在伯氏疏螺旋体中还是在大肠杆菌中产生，脂质部分似乎都具有同等活性。
