Expression of the pneumolysin gene in Escherichia coli: rapid purification and biological properties

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Colleges, School and Institutes


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 languageEnglish
Pages (from-to)67-72
Number of pages6
JournalBiochimica et Biophysica Acta
Issue number1
Publication statusPublished - 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