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益生菌鼠李糖乳杆菌GG的SpaA主链菌毛蛋白亚基的纯化、结晶及初步晶体学分析

Purification, crystallization and preliminary crystallographic analysis of the SpaA backbone-pilin subunit from probiotic Lactobacillus rhamnosus GG.

作者信息

Singh Deepak, von Ossowski Ingemar, Palva Airi, Krishnan Vengadesan

机构信息

Regional Centre for Biotechnology, 180 Udyog Vihar Phase 1, Gurgaon, Haryana 122 016, India.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Oct;69(Pt 10):1182-5. doi: 10.1107/S1744309113024676. Epub 2013 Sep 30.

Abstract

Lactobacillus rhamnosus GG, a widely used Gram-positive probiotic strain, is clinically well known for its perceived health-promoting effects. It has recently been shown to display proteinaceous pilus fibres (called SpaCBA) on its cell surface. Structurally, SpaCBA pili possess a characteristic three-pilin polymerized architecture, with repeating SpaA major pilins that form the backbone and two types of minor subunits (SpaB and SpaC). In this study, recombinant SpaA protein was purified, characterized and crystallized. The crystals diffracted to a resolution of 2.0 Å and belonged to space group C2, with unit-cell parameters a=227.9, b=63.2, c=104.3 Å, β=95.1°.

摘要

鼠李糖乳杆菌GG是一种广泛使用的革兰氏阳性益生菌菌株,因其公认的促进健康作用而在临床上广为人知。最近发现它在细胞表面展示出蛋白质性菌毛纤维(称为SpaCBA)。从结构上看,SpaCBA菌毛具有独特的三聚体聚合结构,由重复的SpaA主要菌毛蛋白形成主干以及两种类型的次要亚基(SpaB和SpaC)。在本研究中,重组SpaA蛋白被纯化、表征并结晶。晶体的衍射分辨率为2.0 Å,属于空间群C2,晶胞参数a = 227.9、b = 63.2、c = 104.3 Å,β = 95.1°。

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