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

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Error fetching PMID 12949111:
  1. Error fetching PMID 12949111: [Adhesin-IgA-LeucineZipper]
  • 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

Error fetching PMID 8254661:
  1. Error fetching PMID 8254661: [IgA-betacore]
  • 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"

Error fetching PMID 10835606:
  1. Error fetching PMID 10835606: [Bioremediatio-Igab]
  • 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%)

Error fetching PMID 2189728:
  1. Error fetching PMID 2189728: [Iga-betacore-nodisulfide]
  • 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)

Error fetching PMID 3027577:
  1. Error fetching PMID 3027577: [First-IgA]
  • A basic description of IgA protein in Neisseria gonorrhoeae

Error fetching PMID 10510237:
  1. Error fetching PMID 10510237: [disulfide]
  • It is possible to have disulfide-dependent folding, but it decreases efficiency (3-fold with Fv)

Error fetching PMID 15014442:
  1. Error fetching PMID 15014442: [Oomen-Structure]
  • 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
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