Comparative study of hemolytic substances produced by coagulase-negative Staphylococcus strains

Abstract

Hemolytic substances H7, H62, and E56, produced by Staphylococcus haemolyticus 7 and 62 and S. epidermidis 56, respectively, were purified. H7 and H62 are probably similar on the basis of their isoelectric focusing profiles in 8 M urea and complete immunological identity as revealed by immunodiffusion with rabbit anti-H7 and anti-E56 sera. For E56, we observed seven bands instead of three in isoelectric focusing and only partial immunological identity with H7 and H62. However, H7 and E56 were similar with regard to the following characteristics: hemolytic spectra against different erythrocytes, kinetics of erythrocyte lysis, heat stability, and inhibition by phosphatidylcholine. E56 was not active at a temperature lower than or equal to 25°C, and its activity increased more rapidly with increased temperature compared with H7. For both substances, the complexes obtained by molecular filtration on Ultrogel AcA54 and the purified peptides by reverse-phase high-pressure liquid chromatography showed some hemolytic activity. These results suggest that a particular association or the presence of a given peptide could enhance the activity.

An Inflammatory Polypeptide Complex from Staphylococcus epidermidis: Isolation and Characterization

“…aureus delta toxin ( 34 , 35 ) and S . hemolyticus gonococcal growth inhibitor ( 36 ) have been reported to form complexes or aggregates of various sizes and similar aggregation or complexing of S . epidermidis PSM appears to occur as well.…”

“…However, sephadex gel chromatography either of the crude extract or the S. epidermidis PSM suggested an active product with mol wt ‫53ف‬ kD, which is consistent with its retention during dialysis and ultrafiltration. Both S. aureus delta toxin (34,35) and S. hemolyticus gonococcal growth inhibitor (36) have been reported to form complexes or aggregates of various sizes and similar aggregation or complexing of S. epidermidis PSM appears to occur as well. It is not clear whether the polypeptides assemble into a highly ordered complex or whether they aggregate due to hydrophobic interactions with little or no order.…”