Conservation of the biologically active portions of staphylococcal enterotoxins C1 and C2.
We determined the primary sequence of staphylococcal enterotoxin (SE) C2 by sequencing its cloned structural gene, entC2. The entC2 structural gene contains an 801-base-pair open reading frame which encodes a 266-amino-acid precursor with a molecular weight of 30,608. Mature SE C2, produced by removal of the signal peptide, contains 239 amino acids with a molecular weight of 27,531. A sequence comparison between SE C2 and SE C1 showed that the 167 carboxyl amino acids in both toxins were 100% conserved. In contrast, the 72 N-terminal residues were 10% divergent. This provides additional evidence that carboxyl regions of staphylococcal and streptococcal pyrogenic toxins determine shared biological activities and cross-reactive epitopes.
Bohach
G A
GA
Department of Microbiology, Medical School, University of Minnesota, Minneapolis 55455.
Schlievert
P M
PM
D000595:Amino Acid Sequence; D000942:Antigens, Bacterial / Q000235:genetics / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000633:toxicity; D001483:Base Sequence; D004768:Enterotoxins / Q000235:genetics* / Q000302:isolation & purification / Q000633:toxicity; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013211:Staphylococcus aureus / Q000235:genetics* / Q000502:physiology
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D004768:Enterotoxins; C034959:enterotoxin C, staphylococcal