Degradation of C3 by Streptococcus pneumoniae.
After growth to exponential phase in Todd-Hewitt broth, clinical and laboratory isolates of Streptococcus pneumoniae serotypes 3, 4, and 14 readily degraded first the beta and then the alpha chains of purified human C3 in the absence of serum or other complement proteins, as assessed by SDS-PAGE. With exponentially growing pneumococci, degradation of native C3 was detectable within 30 min; methylamine-treated C3 and preformed C3b were degraded with equal avidity. Pneumococcal C3-degrading activity was cell associated, abolished by heat killing, and independent of the presence of the polysaccharide capsule. After degradation, 44% of C3 molecules contained a disrupted thiolester bond. Pneumococci treated with 100 micrograms of mutanolysin released 94% of C3-degrading activity from the pneumococcal surface into the supernatant. These studies demonstrate that clinical and laboratory isolates of virulent pneumococci degrade and inactivate soluble C3.
Angel
C S
CS
Department of Pediatrics, University of Minnesota Medical School, Minneapolis 55455.
Ruzek
M
M
Hostetter
M K
MK
D001345:Autoradiography; D003176:Complement C3 / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000302:isolation & purification; D012703:Serotyping; D013296:Streptococcus pneumoniae / Q000145:classification / Q000187:drug effects / Q000378:metabolism*; D013997:Time Factors; D014316:Tritium
D003176:Complement C3; D046911:Macromolecular Substances; D010446:Peptide Fragments; D014316:Tritium; D010450:Endopeptidases; C021816:mutanolysin