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1.
Curr Eye Res ; 7(11): 1077-85, 1988 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-2468448

RESUMEN

Human S-antigen (HSA) is a 50,000 molecular weight photoreceptor cell protein capable of inducing an experimental autoimmune uveitis (EAU) in susceptible animal strains. In order to determine specific sites responsible for its uveitopathogenicity, we synthesized 39 overlapping peptides corresponding to its entire 404 amino acid sequence and tested each peptide for its ability to induce an EAU in Lewis rats. Two synthetic peptides designated peptide HSA 319 (amino acid positions 286 to 305) and peptide HSA 320 (amino acid positions 306 to 325) were uveitopathogenic when used at 50 and 100 micrograms immunizing doses. Smaller peptides corresponding to the amino, mid, and carboxy terminal portions of each peptide further refined each uveitopathogenic site to 12 amino acids. A computerized analysis of the amino acid sequence of S-antigen indicates that these uveitopathogenic sites are complex and may be related to a two-fold symmetry in the molecule. Our present and previous studies provide a basis for the uveitopathogenicity of human and bovine S-antigen in the pathogenesis of EAU as well as the pathogenesis of certain forms of uveitis in humans.


Asunto(s)
Antígenos/inmunología , Proteínas del Ojo/inmunología , Uveítis/etiología , Secuencia de Aminoácidos , Animales , Arrestina , Autoantígenos/análisis , Epítopos/inmunología , Femenino , Humanos , Datos de Secuencia Molecular , Fragmentos de Péptidos/inmunología , Mapeo Peptídico , Ratas , Ratas Endogámicas Lew , Uveítis/patología
2.
Curr Eye Res ; 6(9): 1151-9, 1987 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-2444394

RESUMEN

S-antigen (48K protein) is a photoreceptor cell protein highly pathogenic for the induction of experimental autoimmune uveitis (EAU) and intimately involved in the visual process. EAU is characterized, in part, as a T-cell mediated autoimmune disease which results in a severe inflammation of the uveal tract, and pineal gland. In order to determine specific sites in S-antigen responsible for its pathogenicity we synthesized twenty-three peptides, corresponding to the entire 404 amino acid sequence, and tested each peptide for its ability to induce EAU in Lewis rats. One peptide, peptide M (18 amino acids in length), was found to be highly pathogenic and consistently induced an EAU that was identical to the disease caused by native S-antigen. Clinically, the disease that developed in the eye was characterized by iris and pericorneal hyperemia, followed by inflammatory exudates in the anterior and vitreous chambers. Histopathologically a severe inflammatory response was observed which resulted in the complete destruction of the photoreceptor cell layer of the retina. In order to more fully characterize this pathogenic site, 14 additional smaller peptides (eight to eighteen amino acids in length) corresponding to the left and right portions of peptide M were synthesized. Of these peptides, peptide M16L, M15L, and M12L induced EAU, further localizing this pathogenic site to a small well-characterized region of S-antigen consisting of twelve amino acids. In addition, animals with ocular inflammatory disease had an associated pinealitis characterized by a lymphocytic infiltration of the subcapsular and central area of the pineal gland. The significance of these findings and the relationship of S-antigen in the pathogenesis of EAU and other autoimmune diseases is discussed.


Asunto(s)
Antígenos/inmunología , Enfermedades Autoinmunes/inmunología , Encefalitis/inmunología , Epítopos , Proteínas del Ojo/inmunología , Glándula Pineal , Uveítis/inmunología , Secuencia de Aminoácidos , Animales , Arrestina , Enfermedades Autoinmunes/patología , Datos de Secuencia Molecular , Ratas , Ratas Endogámicas Lew , Uveítis/patología
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