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

Error fetching PMID 16600968

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

Error fetching PMID 12039531

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

Error fetching PMID 12480350

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

Error fetching PMID 12522254

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"

Error fetching PMID 1625582

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