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Production and purification of a recombinant staphylococcal enterotoxin B vaccine candidate expressed in Escherichia coli

  1. Author:
    Coffman, J. D.
    Zhu, J. W.
    Roach, J. M.
    Bavari, S.
    Ulrich, R. G.
    Giardina, S. L.

  2. Author Address

    NCI, SAIC Frederick, Biopharmaceut Dev Program, Frederick, MD 21702 USA. NCI, SAIC Frederick, Biopharmaceut Dev Program, Frederick, MD 21702 USA. USA, Med Res Inst Infect Dis, Ft Detrick, MD 21702 USA. Giardina SL NCI, SAIC Frederick, Biopharmaceut Dev Program, Frederick, MD 21702 USA.
    1. Year: 2002
  2. Journal: Protein Expression and Purification
    1. 24
    2. 2
    3. Pages: 302-312
  4. Type of Article: Article
  1. Abstract:

    An attenuated, recombinant form of Staphylococcus enterotoxin B (rSEB) was overexpressed in Escherichia coli under transcriptional control of the T7 promoter. The 28-kDa rSEB was partially purified from soluble, intracellular protein by tangential flow filtration and differential ammonium sulfate precipitation. The intermediate product was then further purified using low-pressure liquid chromatography including hydrophobic interaction, cation exchange, and size-exclusion matrices. The final vialed product was >95% pure as determined by Coomassie blue-stained sodium dodecyl sulfate-polyacrylamide gel electrophoresis, high-pressure size-exclusion chromatography, and capillary zonal electrophoresis. The endotoxin level was <0.6 EU/mg. Final estimated yield of purified rSEB was 147 mg/L of starting culture. Purified rSEB was stable, elicited an immune response in mice, and protected mice against a lethal challenge with the native toxin. (C) 2002 Elsevier Science (USA).

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