...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Infection and immunity >Tyrosine-Phosphorylated Ehrlichia chaffeensis and Ehrlichia canis Tandem Repeat Orthologs Contain a Major Continuous Cross-Reactive Antibody Epitope in Lysine-Rich Repeats
【24h】

Tyrosine-Phosphorylated Ehrlichia chaffeensis and Ehrlichia canis Tandem Repeat Orthologs Contain a Major Continuous Cross-Reactive Antibody Epitope in Lysine-Rich Repeats

机译：酪氨酸磷酸化恰菲埃里希氏菌和犬埃里希氏菌串联重复直系同源物在富含赖氨酸的重复序列中包含主要的连续交叉反应抗体表位

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

A small subset of major immunoreactive proteins have been identified in Ehrlichia chaffeensis and Ehrlichia canis, including three molecularly and immunologically characterized pairs of immunoreactive tandem repeat protein (TRP) orthologs with major continuous species-specific epitopes within acidic tandem repeats (TR) that stimulate strong antibody responses during infection. In this study, we identified a fourth major immunoreactive TR-containing ortholog pair and defined a major cross-reactive epitope in homologous nonidentical 24-amino-acid lysine-rich TRs. Antibodies from patients and dogs with ehrlichiosis reacted strongly with recombinant TR regions, and epitopes were mapped to the N-terminal TR region (18 amino acids) in E. chaffeensis and the complete TR (24 amino acids) in E. canis. Two less-dominant epitopes were mapped to adjacent glutamate/aspartate-rich and aspartate/tyrosine-rich regions in the acidic C terminus of E. canis TRP95 but not in E. chaffeensis TRP75. Major immunoreactive proteins in E. chaffeensis (75-kDa) and E. canis (95-kD) whole-cell lysates and supernatants were identified with TR-specific antibodies. Consistent with other ehrlichial TRPs, the TRPs identified in ehrlichial whole-cell lysates and the recombinant proteins migrated abnormally slow electrophoretically a characteristic that was demonstrated with the positively charged TR and negatively charged C-terminal domains. E. chaffeensis TRP75 and E. canis TRP95 were immunoprecipitated with anti-pTyr antibody, demonstrating that they are tyrosine phosphorylated during infection of the host cell.
机译：在查菲埃里希氏菌和犬埃里希氏菌中鉴定出一小部分主要的免疫反应蛋白，包括三个分子和免疫学特征的免疫反应性串联重复蛋白（TRP）直系同源物对，在酸性串联重复（TR）内具有主要的连续物种特异性表位，可刺激强烈的感染过程中的抗体反应。在这项研究中，我们确定了第四个主要的含有免疫反应性TR的直向同源物对，并在同源的不相同的24个氨基酸的富含赖氨酸的TRs中定义了一个主要的交叉反应性表位。埃希氏菌病患者和犬的抗体与重组TR区反应强烈，抗原决定簇定位于恰菲埃里希菌N末端TR区（18个氨基酸）和犬埃里希氏菌完整TR（24个氨基酸）。两个较不占优势的表位被定位到犬大肠杆菌（E. canis）TRP95的酸性C末端的邻近谷氨酸/天冬氨酸富集和天门冬氨酸/酪氨酸富集的区域，而不是在恰菲埃希菌TRP75中。用TR特异性抗体鉴定了恰菲大肠杆菌（75-kDa）和犬大肠杆菌（95-kD）全细胞裂解液和上清液中的主要免疫反应蛋白。与其他的ETR一样，在EFL的全细胞裂解物中鉴定到的TRP和重组蛋白的电泳迁移速度异常缓慢，这是带正电荷的TR和带负电荷的C末端结构域所证实的。用抗pTyr抗体免疫沉淀了查菲E. chaffeensis TRP75和E. canis TRP95，表明它们在感染宿主细胞期间被酪氨酸磷酸化。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号