Autoantibodies in infectious mononucleosis have specificity for the glycine-alanine repeating region of the Epstein-Barr virus nuclear antigen
| Autor: | G Rhodes, P Kurki, Dennis A. Carson, H. Rumpold, K M Patrick, John H. Vaughan |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Herpesvirus 4
Human Immunology Glycine medicine.disease_cause Antigen Antibody Specificity medicine Immunology and Allergy Humans Amino Acid Sequence Infectious Mononucleosis Antigens Viral B cell Autoantibodies Repetitive Sequences Nucleic Acid B-Lymphocytes Alanine biology Autoantibody Articles Cell Transformation Viral Epstein–Barr virus Virology Molecular biology Molecular mimicry medicine.anatomical_structure Epstein-Barr Virus Nuclear Antigens Immunoglobulin M Polyclonal antibodies biology.protein Keratins Antibody |
| Zdroj: | The Journal of Experimental Medicine |
| ISSN: | 0022-1007 |
| Popis: | Viruses have been postulated to be involved in the induction of autoantibodies by: autoimmunization with tissue proteins released by virally induced tissue damage; immunization with virally encoded antigens bearing molecular similarities to normal tissue proteins; or nonspecific (polyclonal) B cell stimulation by the infection. Infectious mononucleosis (IM) is an experiment of nature that provides the opportunity for examining these possibilities. We show here that IgM antibodies produced in this disease react with at least nine normal tissue proteins, in addition to the virally encoded Epstein-Barr nuclear antigen (EBNA-1). The antibodies are generated to configurations in the glycine-alanine repeat region of EBNA-1 and are crossreactive with the normal tissue proteins through similar configurations, as demonstrated by the effectiveness of a synthetic glycine-alanine peptide in inhibiting the reactions. The antibodies are absent in preillness sera and gradually disappear over a period of months after illness, being replaced by IgG anti-EBNA-1 antibodies that do not crossreact with the normal tissue proteins but that are still inhibited by the glycine-alanine peptide. These findings are most easily explained by either a molecular mimicry model of IgM autoantibody production or by the polyclonal activation of a germline gene for a crossreactive antibody. It also indicates a selection of highly specific, non-crossreactive anti-EBNA-1 antibodies during IgM to IgG isotype switching. |
| Databáze: | OpenAIRE |
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