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Leppla, Norman C.; Drees, Bastiaan M.; Showler, Allan T.; Capinera, John L.; Peña, Jorge E.; Mannion, Catharine M.; Howard, F. William; Hoy, Marjorie A.; Al-Ajlan, Abdulaziz M.; Stocks, Ian; Raina, Ashok K.; Devorshak, Christina; Fishe, Fred; Garcia, Lloyd; Gerberg, Eugene J.; Gratz, Norman G.; Nation, James L.; Berlinger, Menachem J.; Verma, K. K.; Lecoq, Michel; Magalhães, Bonifácio; Cutkomp, Lawrence K.; Heppner, John B.; Brown, Harley P.; McCravy, Kenneth W.; Coons, Lewis B.; Rothschild, Marjorie; Lysyk, Tim; Lee, Clarence M.; Armstrong, Earlene; Negrón, José F.; Frank, J. Howard; Thomas, M. C.

doi:10.1007/978-1-4020-6359-6_3345

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“…The causative agent of anthrax, Bacillus anthrax, is a Grampositive spore-forming bacterium. The major virulence factor of B. anthrax is a tripartite anthrax toxin, consisting of three proteins: PA (protective antigen), LF (lethal factor) and OF (oedema factor) [1,2]. The three proteins are encoded by the virulence plasmid pXO1 and non-toxic individually [3,4].…”

Section: Introductionmentioning

confidence: 99%

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High‐level expression and single‐step purification of recombinant Bacillus anthracis protective antigen from Escherichia coli

Dong

Wang

et al. 2009

Biotech and App Biochem

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PA (protective antigen) is a major immunogen of the vaccine against anthrax. In the present study, a new expression system, Escherichia coli strain Rosetta 2(DE3), was used for high-level expression of rPA (recombinant PA) whose gene contains 66 rare E. coli codons (9.0% of 733 total PA gene codons). The rPA-formed inclusion bodies were washed with Triton X-100 and 2 M urea and solubilized in 5 M urea, followed by a 60%-satd.-ammonium sulfate precipitation. Finally, the untagged rPA was efficiently and rapidly purified by single-step hydrophobic-interaction chromatography using Phenyl-Sepharose High Performance resin on an AKTA Purifier 10 system. The yield was approx. 13 mg of high-purity (>99%) biologically active rPA per litre of culture, which can be used for the detection of anthrax and as a potential component of a vaccine against anthrax.

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Section: Introductionmentioning

confidence: 99%

“…In the past, PA was prepared from Bacillus anthracis, requiring stringent safety measures for culturing, and the removal of OF and LF residual impurities was difficult [1]. More recently, PA has been expressed and purified from other expression hosts, such as Bacillus subtilis, baculovirus and Escherichia coli.…”

Section: Introductionmentioning

confidence: 99%

High‐level expression and single‐step purification of recombinant Bacillus anthracis protective antigen from Escherichia coli

Dong

Wang

et al. 2009

Biotech and App Biochem

View full text Add to dashboard Cite

show abstract

Relative Methods of Sampling

Cited by 1 publication

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High‐level expression and single‐step purification of recombinant Bacillus anthracis protective antigen from Escherichia coli

High‐level expression and single‐step purification of recombinant Bacillus anthracis protective antigen from Escherichia coli

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