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首页> 美国卫生研究院文献>Biochemical Journal >Purified meningococcal transferrin-binding protein B interacts with a secondary strain-specific binding site in the N-terminal lobe of human transferrin.
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Purified meningococcal transferrin-binding protein B interacts with a secondary strain-specific binding site in the N-terminal lobe of human transferrin.

机译：纯化的脑膜炎球菌转铁蛋白结合蛋白B与人转铁蛋白N端叶中的第二个菌株特异性结合位点相互作用。

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Neisseria meningitidis, grown in iron-limited conditions, produces two transferrin-binding proteins (TbpA and TbpB) that independently and specifically bind human serum transferrin (hTF) but not bovine serum transferrin (bTF). We have used surface plasmon resonance to characterize the interaction between individual TbpA and TbpB and a series of full-length human-bovine chimaeric transferrins (hbTFs) under conditions of variable saturation with iron. A comparative analysis of hTF and hbTF chimaera-binding data confirmed that the major features involved in Tbp binding are located in the C-terminal lobe of hTF and that isolated TbpA can recognize distinct sites present in, or conformationally influenced by, residues 598-679. Binding by TbpB was maintained at a significant but decreased level after replacement of the entire hTF C-terminal lobe by the equivalent bovine sequence. The extent of this binding difference was dependent on the meningococcal strain and on the presence of hTF residues 255-350. This indicated that TbpB from strain SD has a secondary, strain-specific, binding site located within this region, whereas TbpB from strain B16B6 does not share this recognition site. Binding of TbpA was influenced primarily by sequence substitutions in the hTF C-terminal lobe, and co-purified TbpA and TbpB (TbpA+B) was functionally distinct from either of its components. The limited divergence between hTF and bTF has been related to observed differences in binding by Tbps and has been used to delineate those regions of hTF that are important for such interactions.
机译：脑膜炎奈瑟氏球菌在铁受限的条件下生长，可产生两种转铁蛋白结合蛋白（TbpA和TbpB），这些蛋白独立且特异性地与人血清转铁蛋白（hTF）结合，而不与牛血清转铁蛋白（bTF）结合。我们已经使用表面等离振子共振来表征个体TbpA和TbpB与一系列全长人-牛嵌合金属转铁蛋白（hbTFs）在铁可变饱和条件下的相互作用。对hTF和hbTF chimaera结合数据的比较分析证实，与Tbp结合有关的主要特征位于hTF的C末端波瓣中，并且分离的TbpA可以识别存在于残基598或受其构象影响的不同位点。在用等效的牛序列取代整个hTF C末端叶后，TbpB的结合保持在显着但降低的水平。这种结合差异的程度取决于脑膜炎球菌菌株和hTF残基255-350的存在。这表明来自菌株SD的TbpB具有位于该区域内的第二个，菌株特异性的结合位点，而来自菌株B16B6的TbpB不共享该识别位点。 TbpA的结合主要受hTF C末端叶中的序列取代影响，并且共纯化的TbpA和TbpB（TbpA + B）在功能上不同于其任何一个成分。 hTF和bTF之间的有限差异与观察到的Tbps结合差异有关，并已被用于描述hTF对此类相互作用很重要的区域。

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