Dual binding capabilities of anti-double-stranded DNA antibodies and anti-ribosomal phosphoprotein (P) antibodies

Author:

Takeda I,Rayno K,Movafagh F B,Wolfson-Reichlin M1,Reichlin M2

Affiliation:

1. Arthritis and Immunology Program, Oklahoma Medical Research Foundation, Oklahoma University Health Sciences Center, Oklahoma City, Oklahoma, USA

2. Arthritis and Immunology Program, Oklahoma Medical Research Foundation, Oklahoma University Health Sciences Center, Oklahoma City, Oklahoma, USA; Rheumatology, Immunology and Allergy Section, Department of Medicine, Oklahoma University Health Sciences Center, Oklahoma City, Oklahoma, USA; 825 Northeast 13th Street, Oklahoma City, OK 73104, USA

Abstract

The aimof this study is to identify distinctive properties of pathogenic anti-double stranded DNA antibodies and anti-ribosomal P antibodies. The binding activity of anti-dsDNA and anti-ribosomal P antibodies to their cognate antigens in 0.15 M and 1.5 M NaCl solutions on ELISA was examined. All anti-dsDNA and anti-ribosomal P antibodies exhibited a loss of their binding activity from37.5 to 100% and from2.3 to 97.4% in high ionic strength buffers, respectively. In contrast, anti-U1RNP antibodies and anti-Ro/SSA antibodies lost from0 to 32.7% and from0 to 40.1% of their binding activity, respectively. Anti-dsDNA and anti-ribosomal P antibodies from patients with nephropathy showed significantly higher binding activity in high ionic strength buffers than those frompatients without nephropathy. Study of paired sera fromlupus nephritis patients revealed that anti-dsDNA and anti-ribosomal P antibodies frompatients during disease flare show stronger binding activity in high ionic strength buffer than those during remission. Most anti-dsDNA and anti-ribosomal P antibodies bind their antigens by ionic interactions that are sensitive to high salt. Such dual binding capability of anti-dsDNA and anti-ribosomal P antibodies may underlie their multiple cross reactivities to various epitopes and help elucidate the pathogenic potential of autoantibody subsets.

Publisher

SAGE Publications

Subject

Rheumatology

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