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致病奈瑟菌中主要的铁调节外膜蛋白FrpB的序列变异性。

Sequence variability of FrpB, a major iron-regulated outer-membrane protein in the pathogenic neisseriae.

作者信息

van der Ley P, van der Biezen J, Sutmuller R, Hoogerhout P, Poolman J T

机构信息

Laboratory of Vaccine Development and Immune Mechanisms, National Institute of Public Health and the Environment, Bilthoven, The Netherlands.

出版信息

Microbiology (Reading). 1996 Nov;142 ( Pt 11):3269-74. doi: 10.1099/13500872-142-11-3269.

Abstract

The FrpB protein from pathogenic neisseriae is a 77 kDa iron-regulated outer-membrane protein that belongs to the family of TonB-dependent receptors and may have potential as a vaccine component. Comparison between the frpB gene from three different meningococcal strains and a published gonococcal one revealed that the region from residues 350 to 390 displays pronounced sequence variability. In a model for the topology of FrpB in the outer membrane, this region corresponds to loop 7, the longest of the predicted 13 surface-exposed loops. Binding of four out of a total of eight bactericidal monoclonal antibodies to synthetic peptides corresponding to loop 7 showed that their epitopes are located here. The frpB genes from five additional meningococcal strains were cloned and sequenced in this region. Pairwise comparisons showed different degrees of similarity.

摘要

致病性奈瑟氏菌的FrpB蛋白是一种77 kDa的铁调节外膜蛋白,属于TonB依赖性受体家族,可能具有作为疫苗成分的潜力。对三种不同脑膜炎球菌菌株的frpB基因与已发表的淋球菌frpB基因进行比较后发现,第350至390位氨基酸残基区域显示出明显的序列变异性。在FrpB在外膜中的拓扑结构模型中,该区域对应于环7,是预测的13个表面暴露环中最长的一个。总共8种杀菌性单克隆抗体中的4种与对应于环7的合成肽结合,表明它们的表位位于此处。另外克隆并测序了5种脑膜炎球菌菌株的frpB基因在该区域的序列。成对比较显示出不同程度的相似性。

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