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A New Activity of Complement Component C3: Cell-Bound C3b Potentiates Lysis of Erythrocytes by C5b,6 and Terminal Components¹

Department of Microbiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Abstract

EAC4b,3b (sheep erythrocytes carrying rabbit antibody and guinea pig complement component fragments C4b and C3) adsorb human C5b,6 reversibly; the avidity of binding varies inversely with ionic strength. We believe that the receptor of C5b,6 is contributed by the cell-bound C3b because the binding capacity of EAC4b,3b varies with C3b multiplicity and can be blocked with rabbit antibody to guinea pig C3. The fixation of C5b,6 to the erythrocyte-bound C3b serves to concentrate C5b,6 on the cell surface; as a consequence, the hemolytic efficiency of C5b,6 is almost 100 times greater when assayed with EAC4b,3b than with plain erythrocytes. This potentiation represents a hitherto unrecognized function of cell-bound C3b.

Footnotes

¹ This work was supported in part by a United States Public Health Service Research Grant 5 RO1 AI-02566-17 and a National Science Foundation Grant BMS75-09911.

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