Expression of the pneumolysin gene in Escherichia coli: rapid purification and biological properties.
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.
Mitchell
T J
TJ
Department of Microbiology, University of Leicester, U.K.
Walker
J A
JA
Saunders
F K
FK
Andrew
P W
PW
Boulnois
G J
GJ
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003001:Cloning, Molecular; D003167:Complement Activation; D003603:Cytotoxins / Q000235:genetics* / Q000276:immunology / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000378:metabolism; D010957:Plasmids; D011994:Recombinant Proteins / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification; D013296:Streptococcus pneumoniae / Q000235:genetics* / Q000276:immunology; D013301:Streptolysins / Q000235:genetics* / Q000276:immunology / Q000302:isolation & purification
D001426:Bacterial Proteins; D003603:Cytotoxins; D011994:Recombinant Proteins; D013301:Streptolysins; C032290:plY protein, Streptococcus pneumoniae