Anti-fecundity immunity in mice immunized with anti idiotypic monoclonal antibody NP30 of Schistosoma japonicum

Objective To observe the effects of anti fecundity and anti embryonation immuntiy of anti idiotypic monoclonal antibody NP30 of Schistosoma japonicum on female adult worm Methods The active immunization of C57BL/6 mice was conducted by means of three intraperitoneal injections of NP30 The control group was injected with SP2/0 ascites intraperitoneally Results On the twenty seventh day after challenge infection, the number of eggs in the liver tissue and in uterus of the group immunized with NP30 decreased by 30 91% and by 38 55%, respectively On the thirty ninth day after the challenge infection, the number of mature eggs in the liver tissue of the group immunized with NP30 decreased by 66 63% and the number of dead eggs increased by 60 66% Conclusions NP30, with which mice were actively immunized, possesses double effects of anti fecundity and anti embryonation immunity on female adult worm of Schistosoma japonicum , therefore it can be used as a promising candidate of anti pathologic vaccine molecule against Schistosomiasis japonica

Monoclonal anti-idiotype antibody bearing the internal image of nasopharyngeal carcinoma associated antigen

Objective To generate and characterize anti-idiotypic monoclonal antibody (Ab2) that bears the internal image of nasopharyngeal carcinoma (NPC) associated antigen. Methods Using NPC monoclonal antibody (Ab1) as immunogen, hybridoma cells were obtained by fusion of SP2/0 myeloma cells with immunized murine spleen cells. Positive clones were screened by Sandwich ELISA and a binding inhibition test. To determine whether Ab2 possess the internal image of the original antigen or not, mice were immunized with Ab2. ELISA and the competitive inhibition assay tested anti-anti-idiotypic antibodies (Ab3) in anti-sera. Cell-mediated immunity to tumors induced by Ab2 was investigated by a delayed-type hypersensitivity response and the mouse T-cell proliferation assay. Results Anti-idiotypic monoclonal antibodies against the monoclonal anti-NPC antibodies FC2 and HNL5 were generated that recognize NPC associated antigens. These Ab2, which were designated 2H4 and 5D3, could inhibit the binding of FC2 or HNL5 to NPC cell lines. Anti-sera from the immunized mice, which contained Ab3, could compete with FC2 or HNL5 for binding with NPC cell by a competitive inhibition assay. Mice immunized with 2H4 or 5D3 coupled with keyhole limpet hemocyanin (KLH), showed a positive and specific delayed-type hypersensitivity (DTH) reaction after stimulation by NPC cells. The mouse T cell proliferative assay indicated that there was a significantly higher proliferative response of the splenocytes in the experimental groups than that in control groups. Conclusions Anti-idiotypic antibodies 2H4 and 5D3 are Ab2 beta bearing the internal image of the epitope of NPC associated antigen. Either 2H4 or 5D3 expressing three-dimensional shapes that resemble the structure of natural antigens could induce humoral and cellular immune response.

Monoclonal Anti-CD4 Antibody MT310 Binds HIV-1 gp120 Binding Site on CD4

Tests show the monoclonal anti CD4 antibody (mAb) MT310 recognizes the gp120 binding site on CD4 as part of its mechanism for strongly inhibiting human immunodeficiency virus type 1 (HIV 1) infection of CD4 + T cells. In competition tests, mAb MT310 and mAb Leu3a (an anti CD4 mAb recognizing the gp120 binding site) all inhibited gp120 binding to CD4 + T lymphocytes, while mAb MT405 did not. This result suggests that MT310, like Leu3a, recognizes the gp120 binding site on CD4. To further confirm whether MT310 recognizes the gp120 binding site on CD4, we prepared rabbit anti idiotypic antisera (Ab2) against MT310 (Ab1). The anti idiotypic antisera against MT310 inhibited binding of MT310 and Leu3a to human CD4 + T lymphocytes, but did not block binding of MT151 with the second domain of CD4, while rabbit anti idiotypic antisera to MT151 could block binding of itself to these cells, but could not inhibit the binding of MT310 and Leu3a, further indicating that MT310 recognized the gp120 binding site on CD4.