EVASION OF PROTECTIVE IMMUNITY BY BORRELIA-BURGDORFERI BY TRUNCATION OF OUTER SURFACE PROTEIN-B
EVASION OF PROTECTIVE IMMUNITY BY BORRELIA-BURGDORFERI BY TRUNCATION OF OUTER SURFACE PROTEIN-B
复制标题
DOI：
10.1073/pnas.90.9.4092
复制
发表时间：
1993-05-01
影响因子：
11.1
通讯作者：
FLAVELL, RA
中科院分区：
文献类型：
--
作者：
FIKRIG, E;TAO, H;FLAVELL, RA
我们分析了莱姆病病原体伯氏疏螺旋体（B B）外表面蛋白B（Osp B）的变异性，以确定B B如何逃避免疫破坏。我们已经表明，用来自Bb菌株B31的OspB接种保护小鼠免受Bb B31的感染，但不抵抗Bb N40。本研究表明，Bb N40螺旋体逃避OspB的疫苗接种免疫具有截短形式的OspB，由于在核苷酸577处的TAA终止密码子。相反，表达全长OspB的Bb N40螺旋体不能感染用OspB免疫的小鼠，类似于我们先前用Bb B31的研究。OspB抗体应答的作图显示OspB的C末端中的表位是表面暴露的并且结合保护性单克隆和多克隆抗体。这表明OspB的C末端对于引发对OspB的保护性免疫应答是重要的。不结合保护性抗体的外表面蛋白的截短或修饰可能是Bb逃避宿主防御的一种手段。
We analyzed variability in outer surface protein B (OspB) from Borrelia burgdorferi (Bb), the causative agent of Lyme disease, to determine how Bb escapes immune destruction. We have shown that vaccination with OspB from Bb strain B31 protected mice from infection with Bb B31 but not against Bb N40. The present study demonstrates that Bb N40 spirochetes which evade vaccination immunity to OspB have a truncated form of OspB, due to a TAA stop codon at nucleotide 577. In contrast, Bb N40 spirochetes that express full-length OspB are unable to infect mice immunized with OspB, analogous to our previous studies with Bb B31. Mapping of the OspB antibody response shows that epitopes in the C terminus of OspB are surface-exposed and bind protective monoclonal and polyclonal antibodies. This suggests that the C terminus of OspB is important for eliciting a protective immune response to OspB. Truncation or modification of outer surface proteins that do not bind protective antibody may be a means by which Bb evades host defenses.