Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 67-72 |
| Number of pages | 6 |
| Journal | Biochimica et Biophysica Acta |
| Volume | 1007 |
| Issue number | 1 |
| Publication status | Published - 23 Jan 1989 |
Keywords
- Amino Acid Sequence
- Bacterial Proteins
- Cloning, Molecular
- Complement Activation
- Cytotoxins
- Escherichia coli
- Genes, Bacterial
- Molecular Sequence Data
- Neutrophils
- Plasmids
- Recombinant Proteins
- Streptococcus pneumoniae
- Streptolysins
