Purification and characterization of Streptococcus pyogenes erythrogenic toxin type A produced by a cloned gene in Streptococcus sanguis.
The gene of Streptococcus pyogenes erythrogenic toxin type A (speA) has been previously cloned in Streptococcus sanguis (Challis) and produces extracellular erythrogenic toxin type A (ET A). The ET A produced and secreted by this heterologous host was purified to homogeneity and shown to have properties identical to ET A produced by S. pyogenes strain NY-5; i.e., serological identity in immunodiffusion, migration in SDS-polyacrylamide gel electrophoresis, mitogenic activity, inhibition of mitogenic activity by specific antibody, and precipitation by an international scarlatina antitoxin preparation. The cloned speA gene specified an ET A which had a molecular weight identical to that of ET A from S. pyogenes previously reported from this laboratory. NH2-terminal sequence determination of the purified protein showed the first nine residues to be gln gln asp pro asp pro ser gln leu; this is consistent with predictions made from the nucleotide sequence of the speA gene according to Weeks and Ferretti and different from the sequence published by Johnson et al.
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D005098:Exotoxins / Q000032:analysis / Q000235:genetics / Q000302:isolation & purification*; D005798:Genes, Bacterial; D005779:Immunodiffusion; D008565:Membrane Proteins; D013297:Streptococcus pyogenes / Q000235:genetics*; D013298:Streptococcus sanguis / Q000235:genetics*
D000596:Amino Acids; D001426:Bacterial Proteins; D005098:Exotoxins; D008565:Membrane Proteins; C117980:SpeA protein, Streptococcus pyogenes; C027951:erythrogenic toxin