• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Virulence >The mutated staphylococcal H35A α-toxin inhibits adhesion and invasion of staphylococcus aureus and group a streptococci
【24h】

The mutated staphylococcal H35A α-toxin inhibits adhesion and invasion of staphylococcus aureus and group a streptococci

机译：突变的葡萄球菌H35Aα毒素可抑制金黄色葡萄球菌的黏附和侵袭，并将链球菌分组

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

In previous studies we demonstrated that the staphylococcal α-toxin inhibits adhesion and invasion of S. aureus by epithelial cells through binding to α5β1 integrin, a receptor of fibronectin. Moreover, we revealed that a H35A mutation abolishes the cytotoxicity of α-toxin completely. These findings led us to hypothesize that the H35A mutated α-toxin may be explored as a potential inhibitor for bacterial adhesion and invasion of epithelial cells. In this study, we examined the impact of the H35A α-toxin on staphylococcal capacity of adhering to and invading into epithelial cells and found that the addition of H35A α-toxin in the culture medium dramatically inhibited S. aureus' ability to adhere to and internalize into epithelial cells. Importantly, we demonstrated that both the staphylococcal α-toxin and H35A mutated α-toxin are capable of retarding the adhesion and invasion of epithelial cells by Streptococcus pyogenes. These findings suggest that the H35A toxoid has the potential to be utilized as an inhibitor of S. aureus and S. pyogenes ability to adhere to and invade epithelial cells.
机译：在先前的研究中，我们证明了葡萄球菌α毒素通过与纤连蛋白的受体α5β1整合素结合，抑制上皮细胞对金黄色葡萄球菌的粘附和侵袭。此外，我们发现H35A突变完全消除了α毒素的细胞毒性。这些发现使我们假设H35A突变的α-毒素可能被探索为细菌粘附和上皮细胞入侵的潜在抑制剂。在这项研究中，我们研究了H35Aα毒素对葡萄球菌粘附和侵袭上皮细胞的能力的影响，发现在培养基中添加H35Aα毒素可显着抑制金黄色葡萄球菌的粘附和侵袭能力。内化为上皮细胞。重要的是，我们证明了葡萄球菌的α毒素和H35A突变的α毒素都能够延缓化脓性链球菌对上皮细胞的粘附和侵袭。这些发现表明，H35A类毒素具有用作金黄色葡萄球菌抑制剂和化脓性链球菌粘附和侵袭上皮细胞的能力。

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