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Structural characteristics of potential novel virulence factors, the host cytokine binding proteins of Aggregatibacter actinomycetemcomitans

机译:潜在的新型毒力因子的结构特征,聚合酶放线菌的宿主细胞因子结合蛋白

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Various gram-negative pathogens possess secreted or outer membrane proteins?(OMPs) which interact with host cytokines. Of periodontal pathogens only Aggregatibacter actinomycetemcomitans (Aa) has been shown to sequester and uptake cytokines. We have identified two (OMPs) of Aa, bacterial interleukin receptor I (BilRI) and OM secretin channel (OMS), which interact with several cytokines, the interaction with IL-8 being the strongest. The NMR studies confirmed that BilRI is intrinsically disordered, i.e. it does not have stabile fold without ligand. The structure of the extramembranous domains of OMS (emOMS) solved with X-ray crystallography showed that the C-terminal domain of emOMS displayed a type I KH domain fold. Crosslinking experiments indicate that one lysine of this domain is located in the IL-8 interaction site. Neisseria meningitides PilQ (NmPilQ) has role in the uptake of IL-8. Although the part of the NmPilQ which interacts with IL-8 is unidentified, the N1-domain of NmPilQ shows sequen...
机译:各种革兰氏阴性病原体都具有与宿主细胞因子相互作用的分泌或外膜蛋白?在牙周病原体中,仅聚集性放线菌(Aa)表现出螯合和摄取细胞因子。我们已经确定了两种Aa(OMP):细菌白介素受体I(BilRI)和OM促分泌素通道(OMS),它们与几种细胞因子相互作用,与IL-8的相互作用最强。 NMR研究证实BilRI本质上是无序的,即没有配体就没有稳定的折叠。 X射线晶体学分析的OMS膜外结构域(emOMS)的结构表明emOMS的C端结构域显示I型KH结构域折叠。交联实验表明该结构域的一个赖氨酸位于IL-8相互作用位点。脑膜炎奈瑟氏菌PilQ(NmPilQ)在摄取IL-8中具有作用。虽然尚不清楚与IL-8相互作用的NmPilQ的部分,但NmPilQ的N1结构域显示出序列...

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