Human anti-tetanus toxin precipitating and co-precipitating antibodies

Abstract

A comparative study has been made of human precipitating and co-precipitating anti-tetanus toxin antibodies. IgG co-precipitating antibody represented 10% of the total antibodies in the serum and had immunological and biological properties similar to those described for co-precipitating antibodies of other animal species.

Human precipitating and co-precipitating antibodies had the same electrophoretic mobility and were localized in the same immunoglobulin fraction. By immunoprecipitation it was not possible to find antigenic differences between precipitating and co-precipitating antibodies. Both antibodies were localized in the IgG1 and IgG3 subclasses and neither were in the IgG4 subclass. Only the precipitating antibody can form insoluble complexes with antigen. Precipitating and co-precipitating antibodies agglutinated sensitized sheep red cells, however, only the precipitating antibody agglutinated human red cells. Eight to ten times more co-precipitating antibody was required to obtain a positive reaction in PCA.

Precipitating antibody activated the complement system while co-precipitating antibody lacked this capacity. This difference in behaviour could not be attributed to localization of both antibodies in different IgG subclasses.

Precipitating and co-precipitating antibodies were cytophilic. Only the former activated phagocytosis and increased clearance of antigen from the blood. These results are not surprising since co-precipitating antibody does not fix complement. Competition between human precipitating and co-precipitating antibodies in opsonization was analysed. In this test competition of both antibodies for the antigen depends on their respective amounts. The K = 0.18 diminished to 0.05 when the ratio of pp:cop. antibody changed from 70:30 to 30:70.

The fact that co-precipitating antibody was isolated from the sera of vertebrates other than man indicate that this antibody could possibly play a role in some immune mechanisms. Taking into account that in previous papers we have demonstrated that co-precipitating antibody functions as a molecule with one combining site of high affinity and one of low affinity, we have proposed that this antibody could function univalently and blocks the antigen. This could facilitate chronic parasitic, bacterial and viral infections, tumour growth and other chronic infections.