By Henry G. Kunkel and Frank J. Dixon (Eds.)
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Extra info for Advances in Immunology, Vol. 29
1979a). Pathway activation can have three biological consequences that affect the relationship between parasite and host: two result in host defense; the third facilitates parasitemia. These consequences are ( a ) the direct antibody-independent lysis of the parasite; ( b ) the induction of cell-mediated killing of the parasite; and (c) mediation of red cell parasitization. Susceptibility to killing via the alternative pathway may be dependent on the stage of differentiation of the parasite. The conversion ofS.
The mechanism of neutralization of NDV has yet to be defined. Only one other virus has been shown to interact with the alternative pathway, Moloney leukemia virus. , 1978). XII. Effects on Host-Parasite Relationship A number of different parasites have been shown to activate the alternative pathway. , 1979a). Pathway activation can have three biological consequences that affect the relationship between parasite and host: two result in host defense; the third facilitates parasitemia. These consequences are ( a ) the direct antibody-independent lysis of the parasite; ( b ) the induction of cell-mediated killing of the parasite; and (c) mediation of red cell parasitization.
1979b). The affinity of B for C3b in the presence of Mgz+ was only 1/5 that of P1H. Binding of P1H to C3b was approximately stoichiometric. Binding of C3bINA could also be demonstrated by stabilizing the enzyme substrate complex ECSb, P l H , C3bINA at 0°C. Binding of C3bINA to EC3b in the presence of P1H was 30-fold greater than in its absence, it was stoichiometric with respect to bound P l H , and the binding constant at 0°C was 10sM-' (Pangburn and Muller-Eberhard, 1978b). V. The Metastable Binding Site Although complement can function in cell-free solution, it has the unusual ability to transfer itself from solution to the surface of biological particles and to function as a solid phase enzyme system and membrane attack mechanism.
Advances in Immunology, Vol. 29 by Henry G. Kunkel and Frank J. Dixon (Eds.)