Unique synthetic peptides stimulating streptolysin S production in streptococci.

Abstract

A peptide has been isolated from pronase digest of bovine serum albumin as the stimulatory factor of streptolysin S (SLS) production by Streptococcus pyogenes, and its primary structure has been deduced [Akao et al. (1992) Infect. Immun. 60, 4777-4780]. To determine the essential structure for the stimulation, a peptide (P-1) having the deduced structure, in which three peptide fragments are linked by two disulfide bonds, and shorter analogs (P-2 to P-4) of peptide P-1 were chemically synthesized. Another peptide (P-5), in which Ala is inserted between the two Cys residues in the middle peptide chain of P-1, was also synthesized. These synthetic peptides were identified by mass spectrometry and analysis of amino acid compositions. The synthetic P-1 stimulated SLS production in a dose-dependent manner. Other peptide analogs also showed remarkable stimulation of SLS production. Treatment of P-1 with performic acid resulted in loss of its stimulatory activity, indicating that disulfide bridges of the peptides are necessary for their activity on SLS production. These results suggest that the unique primary structure of three peptide chains linked by two disulfide bridges is requisite for the stimulatory effect on SLS production.