The Journal of Experimental Medicine
Keystone Symposia
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Journal of Experimental Medicine, Vol 145, 86-100, Copyright © 1977 by Rockefeller University Press

ARTICLES

Requirements for the solubilization of immune aggregates by complement: assembly of a factor B-dependent C3-convertase on the immune complexes

M Takahashi, BF Tack and V Nussenzweig

During the solubilization of immune precipitates BSA-rabbit antibodies to BSA by human complement, at least three stages can be distinguished. (A) Generation of alternative pathway C3-convertase sites associated with the immune complexes. During the first minutes of interaction between the immune aggregates and serum, before any solubilization has taken place, properdin (P), factor B, and C3 moieties are incorporated into the lattice. The washed precipitates have C3-convertase activity, which can be completely inhibited by antibodies to factor B, but not to C2. The assembly of the convertase is temperature-dependent, and does not take place in the absence of Mg++. The immune complex-associated C3- convertase activity decays rapidly at 37 degrees C, but it can be restored by addition of purified factor B and properdin. (B) Amplification. When the aggregates bearing C3-convertase are incubated with purified C3, solubilization takes place. It appears that solubilization is caused by the accumulation of a large number of C3 fragments on the Ag-Ab lattice. In solubilized complexes, the molar ratios of Ab/C3 are close to one. (C) Spontaneous release. The final step in the solubilization process is a secondary reaction, during which some rearrangement of the lattice takes place. It occurs in medium devoid of serum and does not require divalent cations.
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