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Bordetella pertussis
is the causative agent of whooping cough. Traditional vaccines against this
disease are inherently reactogenic, thus research is
currently focussed on the production of less
reactive, acellular vaccines. Expression of candidate
antigens for these vaccines in Escherichia coli would be preferable,
however, several B. pertussis antigens undergo
incorrect post-translational processing in E. coli. The leader peptidase gene (lep) of B. pertussis encodes a
protein of 294 amino acid residues that shares homology with other prokaryote
leader peptidase I sequences. Hydrophilicity analysis
based on the predicted amino acid sequence has demonstrated a similar membrane
topology to that of E. coli and Salmonella typhimurium
leader peptidase I. Co-expression of the B. pertussis
lep gene in E. coli strain TOPP2 expressing the pertussis toxin S1 subunit was found to markedly increase
the expression and post-translational processing of the S1 protein.
PMID: 11024260 [PubMed - indexed for MEDLINE]