Expression of the pneumolysin gene in Escherichia coli: rapid purification and biological properties
Research output: Contribution to journal › Article › peer-review
The gene for pneumolysin, the thiol-activated toxin from Streptococcus pneumoniae, has been expressed in Escherichia coli. The recombinant protein has been purified using a rapid, high yield, purification procedure and has been shown to be identical with respect to N-terminal amino-acid sequence, specific activity, effect on human polymorphonuclear phagocytes and effect on human complement to the native toxin purified from the pneumococcus. This provides a large enough source of material to begin investigation of pneumolysin as a candidate for inclusion in a pneumococcal vaccine.
|Number of pages||6|
|Journal||Biochimica et Biophysica Acta|
|Publication status||Published - 23 Jan 1989|
- Amino Acid Sequence, Bacterial Proteins, Cloning, Molecular, Complement Activation, Cytotoxins, Escherichia coli, Genes, Bacterial, Molecular Sequence Data, Neutrophils, Plasmids, Recombinant Proteins, Streptococcus pneumoniae, Streptolysins