User:Mbennie/Notebook/Papers and Books/IgA Autotransporter

Adhesin-IgA-LeucineZipper pmid=12949111
 * Fused leucine zipper with autotransporter creating a protein that was expressed on the cell surface and adhered to a similar protein expressed in another population of cells, causing the cells to clump out of solution
 * Used IgA as the AT
 * Used Fos and Jun as the leucine zippers
 * Used an E-tag to test whether the protein was expressed on the surface (using an antibody)
 * Used pelB "for an efficient secretion"
 * Membrane remains stable

IgA-betacore pmid=8254661
 * Concludes a subset of IgA (882 bp) can transport and display a passenger protein by itself, called Iga beta-core
 * Figured out that Iga beta was enough, then kept cutting up the protein was no longer functional
 * This 227aa protein is very well conserved among Neisseria and Haemophilus
 * p. 583 - protein sequence of Iga beta-core
 * Suggests that cell express 50,000-100,000 copies
 * Iga beta-core is "structurally reminiscent of integral outer membrane proteins (OMPs)"
 * Suggests further that forty of the amino acids might not be needed (p. 590)
 * "Resembles a typical outer membrane protein with a few additional features"

Bioremediatio-Igab pmid=10835606
 * Describes method of bioremediation using r. eutropha using metallothionein (MT) expressed on the cellular surface using IgA beta
 * MT binds heavy metal atoms
 * Bioaccumulates about 5% of Cd2+ ions tested, but affects the growth of plants in contaminated soil much more (70%)

Iga-betacore-nodisulfide pmid=2189728
 * Discovery that IgA beta contains the ability to display surface proteins by itself
 * Observation that there is a highly conserved region within IgA beta, called IgA beta-core, which is the portion that facilitates outer membrane transport
 * Observed that disulphide-dependent folding can cause problems in surface display (protein stuck in periplasm)

First-IgA pmid=3027577
 * A basic description of IgA protein in Neisseria gonorrhoeae

disulfide pmid=10510237
 * It is possible to have disulfide-dependent folding, but it decreases efficiency (3-fold with Fv)


 * 1) Oomen-Structure pmid=15014442
 * Resolves crystal structure of N. meningitidis IgA (highly homologous to N. gonorrhoeae IgA)
 * "12-stranded beta-barrel with a hydrophilic pore of 10*12.5 A that is filled by an N-terminus alpha-helix"
 * Evidence supporting passenger-domain transport, evidence against oligomer of translocater domains
 * Alpha-helix has many interactions with interior of hydrophilic barrel: seven salt bridges, sixteen hydrogen bonds, and numerous van der Waals contacts
 * Deletion of alpha-helix results in much lower expression of the protein, but increased pore activity