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首页> 外文期刊>Journal of Oral Microbiology >Outer membrane channel protein of an oral pathogen binds human cytokine IL-8
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Outer membrane channel protein of an oral pathogen binds human cytokine IL-8

机译：口腔病原体的外膜通道蛋白结合人细胞因子IL-8

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Opportunistic pathogen Aggregatibacter actinomycetemcomitans resides in the multispecies biofilm in dento-gingival junction. A. actinomycetemcomitans binds and uptakes human proinflammatory cytokines, which may increase the bacterial virulence. Outer membrane ?secretin channel (here OMS), a DNA binder, is involved in uptake of DNA by A. actinomycetemcomitans. However, OMS homologue in Neisseria meningitidis binds cytokines.ELISA was used to characterize the binding of cytokines to extramembranous domain of OMS (emOMS). Binding of IL-8 to emOMS was studied with multiple methods: EuLISA, Thermofluor and Biacore. NMR and cross-linking were used to study the interaction sites. As OMS was previously described as a DNA binder, the interaction between IL-8 and DNA was studied with EMSA.emOMS bound multiple cytokines, IL-8 being the strongest binder with Kd values from nM to μM. Binding of IL-8 stabilized the structure of emOMS. NMR revealed binding to five residues in IL-8 near Lys15 that was close emOMS...
机译：机会性病原体放线菌聚集在牙龈-牙龈交界处的多种生物膜中。放线放线杆菌结合并摄取人促炎细胞因子，这可能会增加细菌的毒性。外膜分泌素通道（此处称为OMS）是一种DNA结合物，参与了放线放线杆菌对DNA的吸收。然而，脑膜炎奈瑟氏球菌中的OMS同源物结合细胞因子。ELISA用于表征细胞因子与OMS膜外结构域（emOMS）的结合。用多种方法研究了IL-8与emOMS的结合：EuLISA，Thermofluor和Biacore。 NMR和交联用于研究相互作用位点。由于以前将OMS描述为DNA结合物，因此使用EMSA研究了IL-8与DNA之间的相互作用.emOMS结合了多种细胞因子，IL-8是最强的结合物，Kd值从nM到μM。 IL-8的结合稳定了emOMS的结构。核磁共振显示与eMMS接近的Lys15附近的IL-8中的五个残基结合。

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