User:Mbennie/Notebook/Papers and Books/Outer Membrane Proteins Overviews

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  1. Rice JJ, Schohn A, Bessette PH, Boulware KT, and Daugherty PS. Bacterial display using circularly permuted outer membrane protein OmpX yields high affinity peptide ligands. Protein Sci. 2006 Apr;15(4):825-36. DOI:10.1110/ps.051897806 | PubMed ID:16600968 | HubMed [OmpX]
  • Fused the N and C terminals of the OmpX protein and created a protein with a N and C terminus that are outside the cell (by 'cutting' one of the beta-barrel loops that was outside the cell)
  • About 500 bp
  • Other systems that might have external display of C or N terminal: INP, EaeA intimin, and EstA
  • Can be overexpressed without damage to membrane
  • Less efficient than OmpX
  • MIT 2007 IGEM team is working with this protein - check back in the fall and hopefully it will already be a part


  1. Samuelson P, Gunneriusson E, Nygren PA, and Ståhl S. Display of proteins on bacteria. J Biotechnol. 2002 Jun 26;96(2):129-54. DOI:10.1016/s0168-1656(02)00043-3 | PubMed ID:12039531 | HubMed [Protein-Display-Review]
  • Thorough review of all significant surface display proteins
  • Surface proteins facilitate diverse functions such as "cell-cell recognition, signal transduction, surface adherence, colonization, and immunoreactions"
  • Table 1 (p. 131) contains good overview of surface display proteins sorted by family
  • Promising system: Lpp'OmpA (p. 133) carries large passenger and expresses on cell surface, folding of passenger can be a problem
  • Lots of system with various drawbacks: not well studied, small passenger, and structure
  • Section on Gram positive bacteria and applications


  1. Lee SY, Choi JH, and Xu Z. Microbial cell-surface display. Trends Biotechnol. 2003 Jan;21(1):45-52. DOI:10.1016/s0167-7799(02)00006-9 | PubMed ID:12480350 | HubMed [Microbial-Surface-Display-Review]
  • Four requirements for a carrier protein (all quoted)
    • Efficient signal peptide or transporting signal to allow premature fusion protein to go through the inner membrane
    • Strong anchoring structure to keep fusion proteins on the cell surface
    • Compatible with foreign protein
    • Resistant to proteases in the the periplasmic space or medium
  • Describes several system of surface display including sections on Gram positive bacteria and yeast


  1. Voulhoux R, Bos MP, Geurtsen J, Mols M, and Tommassen J. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science. 2003 Jan 10;299(5604):262-5. DOI:10.1126/science.1078973 | PubMed ID:12522254 | HubMed [Voulhoux-Role]
  • Omp85 plays a crucial role in the functionality of IgA and other outer membrane proteins
  • Inner membrane - phospholipid bilayer, outer membrane - asymmetric with phospholipids and lipopolysaccharides
  • Signal sequence is cleaved off after translocation into the periplasm
  • omp85 is essential for growth
  • "In the Omp85-depleted strain, the processed passenger domain of IgA1 protease was barely detectable, and the full-length form was found to accumulate"


  1. Benz I and Schmidt MA. AIDA-I, the adhesin involved in diffuse adherence of the diarrhoeagenic Escherichia coli strain 2787 (O126:H27), is synthesized via a precursor molecule. Mol Microbiol. 1992 Jun;6(11):1539-46. DOI:10.1111/j.1365-2958.1992.tb00875.x | PubMed ID:1625582 | HubMed [Benz-AIDA-1]
  • Discovery of adhesin involved in diffuse adherence (AIDA) in e coli
  • Has 49 aa signal sequence
  • 50% homology to virG in S. flexneri
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