One-Step Purification and Porin Transport Activity of the Major Outer Membrane Proteins P2 from Haemophilus influenzae, FomA from Fusobacterium nucleatum and PorB from Neis

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• 作者：Christof Kattner (1)
  Sabrina Pfennig (1)
  Paola Massari (2)
  Mikio Tanabe (1)
  
  1. HALOmem ; Membrane Protein Biochemistry ; Martin-Luther-University Halle-Wittenberg ; Kurt-Mothes-Str.3 ; 06120 ; Halle (Saale) ; Germany
  2. Section of Infectious Diseases ; Department of Medicine ; Boston University School of Medicine ; Boston ; MA ; USA
  
• 关键词：Outer membrane protein (OMP) ; Porin ; 尾 ; Barrel ; Inclusion body ; Solute transport
• 刊名：Applied Biochemistry and Biotechnology
• 出版年：2015
• 出版时间：March 2015
• 年：2015
• 卷：175
• 期：6
• 页码：2907-2915
• 全文大小：422 KB
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• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Biotechnology
  Biochemistry
  
• 出版者：Humana Press Inc.
• ISSN：1559-0291

文摘

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.