We have greatly simplified production of the Bacillus anthracis protective antigen (PA), the immunoprotective antigen of the anthrax vaccine. By varying induction conditions, we have expressed stable, soluble PA in E. coli, affinity-tagged to facilitate rapid, single-step purification. Recombinant PA exhibited identical properties to B. anthracis PA. Our approach is an attractive strategy for generating purified vaccine antigens that are difficult to express recombinantly.
|Original language||English (US)|
|Number of pages||6|
|Journal||Protein and Peptide Letters|
|State||Published - 1998|
ASJC Scopus subject areas
- Structural Biology