...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Infection and immunity >Differential effect of trypsin on infectivity of Chlamydia trachomatis: loss of infectivity requires cleavage of major outer membrane protein variable domains II and IV.
【24h】

Differential effect of trypsin on infectivity of Chlamydia trachomatis: loss of infectivity requires cleavage of major outer membrane protein variable domains II and IV.

机译：胰蛋白酶对沙眼衣原体感染的不同作用：感染力的丧失需要切割主要的外膜蛋白可变域II和IV。

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

摘要

The initial interaction of chlamydiae with host cells is not well understood. Chlamydial cell surface components that function in attachment are key virulence factors, and their identification is critical for understanding the pathogenic strategies of this very successful parasite. We used trypsin proteolysis of chlamydiae to define surface components that function in chlamydia-host cell interactions. We found that trypsin had a differential effect on the infectivity of Chlamydia trachomatis serovars B and L2 for HeLa 229 cells. Trypsin treatment resulted in a significant loss of attachment and infectivity of serovar B but had no effect on the infectivity of serovar L2. Fluorograms of chlamydiae metabolically labeled with 14C-amino acids and treated with trypsin showed that the major outer membrane protein (MOMP) of both serovars was cleaved. Evidence for two trypsin cleavage sites was found for the serovar B MOMP. One cleavage site was located between lysine 145 and valine 146 in variable domain (VD) II of the protein. The second site was located between lysine 309 and threonine 310 in VD IV. In contrast, the serovar L2 MOMP was cleaved only at lysine 309 in VD IV. These results suggest a functional role for MOMP in chlamydial attachment and implicate VDs II and IV of MOMP in this interaction.
机译：衣原体与宿主细胞的初始相互作用尚不清楚。在附着中起作用的衣原体细胞表面组分是关键的毒力因子，其鉴定对于理解这种非常成功的寄生虫的致病策略至关重要。我们使用衣原体的胰蛋白酶蛋白酶解来定义在衣原体-宿主细胞相互作用中起作用的表面组分。我们发现胰蛋白酶对沙眼衣原体血清B和L2感染HeLa 229细胞有不同的影响。胰蛋白酶处理导致血清B的附着力和感染力显着丧失，但对血清L2的感染力没有影响。用14C-氨基酸代谢标记并用胰蛋白酶处理的衣原体的荧光照片显示，两种血清型的主要外膜蛋白（MOMP）均被切割。血清B型MOMP有两个胰蛋白酶切割位点的证据。在该蛋白质的可变域（VD）II中，一个切割位点位于赖氨酸145和缬氨酸146之间。第二个位点位于VD IV中的赖氨酸309和苏氨酸310之间。相反，血清型L2 MOMP仅在VD IV中的赖氨酸309处裂解。这些结果表明MOMP在衣原体附着中的功能作用，并暗示在此相互作用中MOMP的VD II和IV。

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