Cornelissen C N, Sparling P F
Department of Medicine, School of Medicine, University of North Carolina, Chapel Hill 27599.
Mol Microbiol. 1994 Dec;14(5):843-50. doi: 10.1111/j.1365-2958.1994.tb01320.x.
The mechanism of iron utilization from transferrin has been most extensively characterized in the pathogenic Neisseria species and Haemophilus species. Two transferrin-binding proteins, Tbp1 and Tbp2, have been identified in these pathogens and are thought to be components of the transferrin receptor. Tbp1 appears to be an integral, TonB-dependent outer membrane protein while Tbp2, a lipoprotein, may be peripherally associated with the outer membrane. The relative contribution of each of these proteins to transferrin binding and utilization is discussed and a model of iron uptake from transferrin is presented. Sequence comparisons of the genes encoding neisserial transferrin-binding proteins suggest that they are probably under positive selection for variation and may have resulted from inter-species genetic exchange.
在致病性奈瑟菌属和嗜血杆菌属中,对转铁蛋白中铁利用机制的研究最为广泛。在这些病原体中已鉴定出两种转铁蛋白结合蛋白,即Tbp1和Tbp2,它们被认为是转铁蛋白受体的组成部分。Tbp1似乎是一种完整的、依赖TonB的外膜蛋白,而Tbp2作为一种脂蛋白,可能与外膜存在外周关联。本文讨论了这些蛋白质各自对转铁蛋白结合和利用的相对贡献,并提出了从转铁蛋白摄取铁的模型。编码奈瑟菌转铁蛋白结合蛋白的基因序列比较表明,它们可能处于正向选择以发生变异,并且可能是种间基因交换的结果。