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

T. Hidvegi, Z. Prohaszka, E. Ujhelyi, N. M. Thielens, M. P. Dierich, H. Hampl, G. Arlaud, K. Nagy, G. Fust

Research output: Article

9 Citations (Scopus)

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 C1q/heated C1q) and anti-gp41 antibodies were added either after each other or simultaneously, and the amounts of bound antibody, and deposited C3b, C4b and C1q were measured. Complement-dependent inhibition of antibody binding to solid-phase rgp41 was found, and C1q seems to be at least partially responsible for this phenomenon. Heating of C1q 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 normal human serum almost totally abolished the antibody binding.

Original languageEnglish
Pages (from-to)490-493
Number of pages4
JournalClinical and Experimental Immunology
Volume94
Issue number3
DOIs
Publication statusPublished - 1993

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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