Pneumococcal proteins ClpC and UvrC as novel host plasminogen binding factors
Pneumococcal proteins ClpC and UvrC as novel host plasminogen binding factors
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DOI：
10.1111/1348-0421.13040
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发表时间：
2022-12-14
影响因子：
2.6
通讯作者：
Terao, Yutaka
中科院分区：
文献类型：
--
作者：
Hirayama, Satoru;Yasui, Yoshihito;Terao, Yutaka
从感染肺炎链球菌的小鼠中鉴定出两种纤溶酶原结合蛋白。使用相对和绝对定量 (iTRAQ) 方法的同量异序标签将肺炎球菌蛋白注释为 ATP 依赖性 Clp 蛋白酶 ATP 结合亚基 (ClpC) 和核酸外切酶 ABC 亚基 C (UvrC)。两种蛋白质的重组体均显示出与纤溶酶原的显着结合，并被发现可通过组织型纤溶酶原激活剂促进纤溶酶原激活。此外，ClpC 和 UvrC 依赖 LytA 释放到培养物上清液中并与细菌表面结合。这些结果表明，肺炎链球菌通过自溶释放 ClpC 和 UvrC，并将它们招募到细菌表面，在那里它们与纤溶酶原结合并促进其激活，从而导致细胞外基质降解和组织侵袭。
Two plasminogen binding proteins were identified from a mouse infected with Streptococcus pneumoniae. The pneumococcal proteins were annotated as ATP-dependent Clp protease ATP-binding subunit (ClpC) and excinuclease ABC subunit C (UvrC) using the isobaric tags for relative and absolute quantification (iTRAQ) method. Recombinants of both proteins showed significant binding to plasminogen and were found to promote plasminogen activation by tissue-type plasminogen activator. In addition, ClpC and UvrC were LytA-dependently released into the culture supernatant and bound to the bacterial surface. These results suggest that S. pneumoniae releases ClpC and UvrC by autolysis and recruits them to the bacterial surface, where they bind to plasminogen and promote its activation, contributing to extracellular matrix degradation and tissue invasion.