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首页> 外文期刊>Applied biochemistry and biotechnology, Part A. enzyme engineering and biotechnology >One-Step Purification and Porin Transport Activity of the Major Outer Membrane Proteins P2 from Haemophilus influenzae, FomA from Fusobacterium nucleatum and PorB from Neisseria meningitidis
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One-Step Purification and Porin Transport Activity of the Major Outer Membrane Proteins P2 from Haemophilus influenzae, FomA from Fusobacterium nucleatum and PorB from Neisseria meningitidis

机译：流感嗜血杆菌主要外膜蛋白P2，核梭菌FomA和脑膜炎奈瑟氏菌PorB的一步纯化和孔蛋白运输活性

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摘要

Bacterial porins are major outer membrane proteins that function as essential solute transporters between the bacteria and the extracellular environment. Structural features of porins are also recognized by eukaryotic cell receptors involved in innate and adaptive immunity. To better investigate the function of porins, proper refolding is necessary following purification from inclusion bodies [1, 2]. Using a single-step size exclusion chromatographic method, we have purified three major porins from pathogenic bacteria, the OmpP2 (P2) from Haemophilus influenzae, FomA from Fusobacterium nucleatum and PorB from Neisseria meningitidis, at high yield and report their unique solute transport activity with size exclusion limit. Furthermore, we have optimized their purification method and achieved improvement of their thermostability for facilitating functional and structural analyses.
机译：细菌孔蛋白是主要的外膜蛋白，在细菌和细胞外环境之间起着必不可少的溶质转运蛋白的作用。参与先天和适应性免疫的真核细胞受体也可以识别孔蛋白的结构特征。为了更好地研究孔蛋白的功能，从包涵体中纯化后必须适当地重新折叠[1、2]。使用单步大小排阻色谱法，我们以高收率纯化了病原菌中的三种主要孔蛋白，分别来自流感嗜血杆菌的OmpP2（P2），来自核梭形芽孢杆菌的FomA和来自脑膜炎奈瑟氏球菌的PorB，并报告了其独特的溶质转运活性大小排除限制。此外，我们优化了它们的纯化方法，并提高了其热稳定性，以促进功能和结构分析。

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