Using proximity biotinylation to detect herpesvirus entry glycoprotein interactions: Limitations for integral membrane glycoproteins.
Lajko M1, Haddad AF2, Robinson CA2, Connolly SA3.
Journal of virological methods.J Virol Methods.2015 Sep 1;221:81-9. doi: 10.1016/j.jviromet.2015.04.031. Epub 2015 May 6.
Herpesvirus entry into cells requires coordinated interactions among several viral transmembrane glycoproteins. Viral glycoproteins bind to receptors and interact with other glycoproteins to trigger virus-cell membrane fusion. Details of these glycoprotein interactions are not well understood becaus
Analysis of HIV-1 Gag protein interactions via biotin ligase tagging.
Ritchie C1, Cylinder I1, Platt EJ1, Barklis E2.
Journal of virology.J Virol.2015 Apr;89(7):3988-4001. doi: 10.1128/JVI.03584-14. Epub 2015 Jan 28.
We have examined the interactions of wild-type (WT) and matrix protein-deleted (ΔMA) HIV-1 precursor Gag (PrGag) proteins in virus-producing cells using a biotin ligase-tagging approach. To do so, WT and ΔMA PrGag proteins were tagged with the Escherichia coli promiscuous biotin ligase (BirA*), ex
Proteomic analysis of proteins surrounding occludin and claudin-4 reveals their proximity to signaling and trafficking networks.
Fredriksson K1, Van Itallie CM1, Aponte A2, Gucek M2, Tietgens AJ1, Anderson JM1.
PloS one.PLoS One.2015 Mar 19;10(3):e0117074. doi: 10.1371/journal.pone.0117074. eCollection 2015.
Tight junctions are complex membrane structures that regulate paracellular movement of material across epithelia and play a role in cell polarity, signaling and cytoskeletal organization. In order to expand knowledge of the tight junction proteome, we used biotin ligase (BioID) fused to occludin and