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

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.

journal_name

Clin Exp Immunol

journal_title

Clinical and experimental immunology

authors

Hidvégi T,Prohászka Z,Ujhelyi E,Thielens NM,Dierich MP,Hampl H,Arlaud G,Nagy K,Füst G

doi

10.1111/j.1365-2249.1993.tb08223.x

subject

Has Abstract

pub_date

1993-12-01 00:00:00

pages

490-3

issue

3

eissn

0009-9104

issn

1365-2249

journal_volume

94

pub_type

杂志文章

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