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Clinical and Experimental Immunology logoLink to Clinical and Experimental Immunology
. 1993 Dec;94(3):490–493. doi: 10.1111/j.1365-2249.1993.tb08223.x

Studies on the mechanism of complement-mediated inhibition of antibody binding to HIV gp41.

T Hidvégi 1, Z Prohászka 1, E Ujhelyi 1, N M Thielens 1, M P Dierich 1, H Hampl 1, G Arlaud 1, K Nagy 1, G Füst 1
PMCID: PMC1534428  PMID: 8252810

Abstract

We have previously demonstrated that HIV envelope gp41 binding to specific antibodies decreases after preincubation of fluid-phase gp41 in normal human serum. This inhibition is proven to be mediated by the classical complement pathway. In this study recombinant gp41 (rgp41) and/or synthetic peptides were preadsorbed to solid phase, and then complement (normal human serum/heated human serum/purified Clq/heated Clq) and anti-gp41 antibodies were added either after each other or simultaneously, and the amounts of bound antibody, and deposited C3b, C4b and Clq were measured. Complement-dependent inhibition of antibody binding to solid-phase rgp41 was found, and Clq seems to be at least partially responsible for this phenomenon. Heating of Clq did not affect this process. Higher amounts of anti-gp41 antibodies significantly and dose-dependently enhanced C4b and C3b fixation to solid-phase rgp41. In the case of synthetic peptides corresponding to the immunodominant region of gp41, significant antibody binding to the solid-phase peptides was also detected, and pretreatment of peptides preadsorbed to solid phase with normal human serum almost totally abolished the antibody binding.

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Selected References

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