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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Bacterial Proteins
-
Cloning, Molecular*
-
Complement Activation
-
Cytotoxins / genetics*
-
Cytotoxins / immunology
-
Cytotoxins / isolation & purification
-
Escherichia coli / genetics
-
Genes, Bacterial
-
Molecular Sequence Data
-
Neutrophils / metabolism
-
Plasmids
-
Recombinant Proteins / genetics
-
Recombinant Proteins / immunology
-
Recombinant Proteins / isolation & purification
-
Streptococcus pneumoniae / genetics*
-
Streptococcus pneumoniae / immunology
-
Streptolysins / genetics*
-
Streptolysins / immunology
-
Streptolysins / isolation & purification
Substances
-
Bacterial Proteins
-
Cytotoxins
-
Recombinant Proteins
-
Streptolysins
-
plY protein, Streptococcus pneumoniae