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Antibodies to a microbial peptide sharing sequence homology with betaA3-crystallin damage lens epithelial cells in vitro and in vivo.
Antibodies to a microbial peptide sharing sequence homology with betaA3-crystallin damage lens epithelial cells in vitro and in vivo.
- Source :
-
Autoimmunity [Autoimmunity] 1999; Vol. 29 (4), pp. 311-22. - Publication Year :
- 1999
-
Abstract
- Circulating auto-antibodies (Abs) against lens antigens (Ags) are highly prevalent in patients with cataract, but their origin and pathogenic significance are unknown. We hypothesized that Abs raised after exposure to infectious microbes could cross-react with lens Ags. To test this hypothesis, we generated a monoclonal Ab to human betaA3-crystallin. Epitope analysis indicated that the ETQAE sequence in the N-terminus region of betaA3-crystallin was critical for mounting a humoral response. Similar sequences were found in three microbial Ags. Mice injected with a microbial oligopeptide containing ETQAE emulsified with complete Freund's adjuvant (CFA) raised Abs which cross-reacted with betaA3-crystallin and developed lens epithelial cell (LEC) damage in vitro. We also genetically engineered an betaA3-crystallin-expressing E. coli. Mice immunized with the recombinant E. coli developed LEC damage. These results support the hypothesis that exposure to microbes having Ags homologous to self Ags can trigger a humoral immune response that leads to LEC damage in mice.
- Subjects :
- Amino Acid Sequence
Animals
Autoimmunity
Cross Reactions
Crystallins genetics
Epithelial Cells immunology
Epithelial Cells pathology
Epitopes genetics
Epitopes immunology
Humans
Immunization
Lens, Crystalline pathology
Mice
Molecular Sequence Data
Oligopeptides genetics
Oligopeptides immunology
Recombinant Proteins genetics
Recombinant Proteins immunology
beta-Crystallin A Chain
Crystallins immunology
Lens, Crystalline immunology
Subjects
Details
- Language :
- English
- ISSN :
- 0891-6934
- Volume :
- 29
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Autoimmunity
- Publication Type :
- Academic Journal
- Accession number :
- 10433087
- Full Text :
- https://doi.org/10.3109/08916939908994751