胸膜肺炎放线杆菌转铁蛋白结合蛋白1基因的克隆、测序及表达
Cloning, sequencing and expression of the transferrin-binding protein 1 gene from Actinobacillus pleuropneumoniae.
作者信息
Daban M, Medrano A, Querol E
机构信息
Institut de Biologia Fonamental and Department de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Barcelona, Spain.
出版信息
Biochem J. 1996 Apr 1;315 ( Pt 1)(Pt 1):257-64. doi: 10.1042/bj3150257.
Abstract
Two outer-membrane proteins are involved in the uptake of iron from transferrin by certain Gram-negative bacteria, transferrin-binding proteins 1 and 2. The gene encoding transferrin-binding protein 1 from a serotype 1 isolate of the Gram-negative pathogen Actinobacillus pleuropneumoniae was cloned, and a fragment encoding 700 amino acids of Tbp1 was expressed in Escherichia coli. We also report here sequencing of the tbpl gene and a comparison of the deduced amino acid sequence with Tbpls from related species. The predicted polypeptide product of tbpl is a 106 kDa protein with a 22-residue signal peptide.
摘要
某些革兰氏阴性菌从转铁蛋白摄取铁的过程涉及两种外膜蛋白，即转铁蛋白结合蛋白1和2。对革兰氏阴性病原体胸膜肺炎放线杆菌血清型1分离株中编码转铁蛋白结合蛋白1的基因进行了克隆，并在大肠杆菌中表达了编码Tbp1 700个氨基酸的片段。我们还在此报告了tbpl基因的测序结果以及推导的氨基酸序列与相关物种的Tbpls的比较。tbpl预测的多肽产物是一种106 kDa的蛋白质，带有一个22个残基的信号肽。
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