Complement activating property of the protein-rich endotoxin (OEP) of Pseudomonas aeruginosa. I. Activation of both the classical and the alternative pathways of guinea pig complement

Abstract

Complement activating property of the protein-rich endotoxin (OEP) of Pseudomonas aeruginosa was investigated. The ability of OEP to consume the hemolytic complement (CH50) of guinea pig serum (GPS) was relatively lower than zymosan, a potent activator of the alternative pathway (AP). The profiles of the complement consumption with OEP in GPS suggested that classical pathway (CP) activation seems to occur in addition to the AP-activation, because the consumption of the C3-C9, i.e., C3 total was relatively higher than those of C1, C4 and C2. Further results stated below is confirmed this. OEP consumed complement in certain extent in C4-deficient GPS and also in factor B- or D-depleted GPS. In these sera either pathway of the AP or the CP was operated. However, OEP consumed complement quite in full extent in the EGTA-chelated serum, in which AP-activation took place in normal level. OEP was therefore found in this experiment to activate only the AP. The conversion of C3 in immunoelectrophoresis which is a evidence of the CP-and/or AP-activation was observed with OEP. It was suggested that the antibody against OEP did not participate in the consumption of complement, because the GPS priorly absorbed with OEP-coated sheep RBC, was retained fully to react with OEP. It was discussed that the active site of OEP as to the complement activation located on the LPS portion of OEP.