Protein A of Staphylococcus aureus

J.J. Langone, Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumonococci. Adv. Immunol. 32,157—252 (1982). 

Plasmid pEScFv is a eukariotic expression vector containing an AM singlechain Fv (ScFv) fragment linked with domain B of protein A of Staphylococcus aureus. Sp2/0 myeloma cells transfected with pEScFv 2G42D7 secreted... 

Deisenhofer, J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9 and 2.8 A resolution. Biochemistry 20 2361-2369, 1981. 

Hjelm H, Hjelm K, Sjoquist J. Protein A from Staphylococcus aureus. Its isolation by affinity chromatography and its use as an immunosorbent for isolation of immunoglobulins. FEBS Lett 1972 28 73-76. 

Lindmark, R., Biriell, C., and Sjoquist, J., Quantitation of specific IgG antibodies in rabbits by a solid-phase radioimmunoassay with H-protein A from Staphylococcus aureus, Scand. J. Immunol., 14, 409 20, 1981. 

Variations, which avoid the use of radioisotopes, are replacing RIA. Some utilize stable isotopes. However, 14C at such low levels that there is no radioactive waste can be coupled with accelerator mass spectrometry to provide very sensitive immunoassays.1 A great variety of other procedures are available. Some involve coupling to antibodies that carry fluorescent labels. Many are now automated. Often protein A from Staphylococcus aureus is utilized in various ways that take advantage of its ability to bind to the Fc portion of IgG from virtually all mammals. For example, it may fix antibodies to a surface or to a label)... 

Shukla, D. D. and Gough, K. H. (1979) The use of protein A, from Staphylococcus aureus, in immune electron microscopy for detecting plant virus particles. J. Gen. Virol. 45, 533-536. 

F2. Farrell, C., Sogaard, H., and Svehag, S.-E., Detection of IgG aggregates or immune complexes using solid-phase Clq and protein A-rich Staphylococcus aureus as an indicator system. Scand. J. Immunol. 4, 673-680 (1975). 

If the antibody is unable to cross-link or aggregate the antigen of interest to the extent needed to induce precipitation of the complex (as is often the case with monoclonal antibodies), an alternative method may be employed. Protein A from Staphylococcus aureus is known to have a high affinity for immunoglobulins. If a soluble antigen-antibody complex is incubated with an insoluble matrix covalently conjugated with Protein A, the complex will be captured by the Protein A covalently attached to the matrix (Fig. IV-9). Because Protein A... 

Inganas M, Johansson SG, Bennich HH Interaction of human polyclonal IgE and IgG from different species with protein A from Staphylococcus aureus, demonstration of protein-A-reactive sites located in the Fab 2 fragment of human IgG. Scand J Immunol 1980 12 23-31. 

Inganas M Comparison of mechanisms of interaction between protein A from Staphylococcus aureus and human monoclonal IgG, IgA and IgM in relation to the classical Fc gamma and the alternative F(ab )2 epsilon protein A interactions. Scand J Immunol 1981 13 343-352. 

Bjerketorp, J., K. Jacobsson, L. Erykberg, The von Willebrand factor-binding protein (vWbp) of Staphylococcus aureus is a coagulase. FEMS Microbiol Lett 2004, 234, 309-314. 

Citrate buffer and saline (MCB) solutions were preelectrolyzed for 24 h at — 1100 mV versus SCE to remove metal ion impurities. Acetonitrile (MCB) was redistilled and stored over molecular sieves. DTPA (Aldrich), triethylamine (Aldrich), and isobutylchloroformate (Sigma) were of the highest available purity. HSA (essentially globulin free) and rabbit IgG specific for HSA (Sigma) were obtained in the lyophilized form. Indium was obtained as anhydrous, ultrapure InCls (Alfa Products). All solutions were prepared from distilled/deionized HgO of at least 10 ft resistivity. Protein A from Staphylococcus aureus (SPA, Enzyme Center) was employed as an immunoadsorbent. It was obtained as a 10% (w/v) suspension with a 1.47 mg/ml binding capacity for immune complexes. 2-mercaptoethanol, sodium dodecyl sulfate, and acrylamide reagents were all of electrophoretic grade (Bio-Rad). 

PHB biobeads displaying the ZZ domain of Protein A from Staphylococcus aureus as the result of N-terminal fusion to PhaC were found to be suitable to purify IgG from serum samples and culture supernatant with high binding capacity and purification power [20, 68]. Other binding domains were successfully displayed such as scFv (single-chain variable fragment) or streptavidin and enabled application of the respective beads as affinity purification resin [69,70). 

The Stability and Unfolding of an IgG Binding Protein Based Upon the B Domain of Protein A from Staphylococcus Aureus Probed by Tryptophan Substitution and Fluorescence Spectroscopy. 

Neyfakh AA, Borsch CM, Kaatz GW (1993) Fluoroquinolone resistance protein NorA of Staphylococcus aureus is a mirltidrug efflux transporter. Antimicrob Agents Chemother... 

Larsson, A., Wejaker, P.-E. and Sjoquist, J. Chicken anti-protein A for the detection and capturing of protein A from Staphylococcus aureus in the presence of absence of mammalian IgG. Hybrid-oma 11 239-243, 1992. 

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