Abstract
Reduced streptolysin O, a toxin produced by certain β-haemolytic streptococci, lyses human erythrocytes. The reaction is inhibited by cholesterol at concentrations of about 1.0μg/ml. Other sterols inhibit the lysin and there is a specific requirement for a 3β-hydroxyl group. Inhibition was obtained with 3β-hydroxychol-5-en-24-oic acid, containing a hydrophilic group at C-24. The mode of inhibition is likely to involve attachment to the fixation site of the lysin which attaches the molecule to cell membranes, probably to membrane cholesterol. A second streptolysin site, concerned in the final haemolytic event, may also be involved. Inhibitors of the latter site have not been characterized, other than antibody with specificity for the site.
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Selected References
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