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Encephalitogenic and immunogenic potential of the stress protein αB-crystallin in Biozzi ABH (H-2A(g7)) mice

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Author: Thoua, N.-M. · Noort, J.M. van · Baker, D. · Bose, A. · Sechel, A.C. van · Stipdonk, M.J.B. van · Travers, P.J. · Amor, S.
Type:article
Date:2000
Institution: TNO Preventie en Gezondheid
Source:Journal of Neuroimmunology, 1, 104, 47-57
Identifier: 235519
doi: doi:10.1016/S0165-5728(99)00246-5
Keywords: Health · αB-Crystallin · Experimental allergic encephalomyelitis · Multiple sclerosis · Peptide epitopes, tolerance · Alpha crystallin · Antigen · Beta crystallin · Epitope · Myelin · Allergic encephalomyelitis · Animal cell · Animal experiment · Animal model · Animal tissue · Autoimmunity · Immunological tolerance · Lymphoid tissue · Multiple sclerosis · Nonhuman · Protein expression · T lymphocyte activation · Animals · Cattle · Crystallins · Encephalitis · Epitopes · Lymphoid Tissue · Mice · Mice, Mutant Strains · Models, Chemical · Molecular Conformation · Peptide Mapping · T-Lymphocytes

Abstract

The stress protein αB-crystallin is an immunodominant antigen in multiple sclerosis (MS)-affected myelin for human T cells and is expressed at elevated levels in MS lesions. Using bovine αB-crystallin and synthetic peptides based on mouse αB-crystallin the ability of this stress protein to induce experimental allergic encephalomyelitis (EAE) was screened in Biozzi ABH (H-2A(g7)) mice. While whole αB-crystallin and the immunodominant T cell epitopes (49-64, 73-88, 153-168) failed to induce disease the subdominant or cryptic epitope (1-16) was weakly encephalitogenic. The lack of encephalitogenicity of whole protein and dominant epitopes may be due to the low constitutive expression of αB-crystallin in the CNS combined with a state of peripheral tolerance suggested by the constitutive expression of αB-crystallin in secondary lymphoid tissues in ABH mice. Further evidence for a role of αB-crystallin in the progression of chronic relapsing neurological disease is suggested by the development of T cell responses to αB-crystallin during MOG-induced relapsing EAE as myelin damage accumulates. Together our data indicate that normal tolerising mechanisms in ABH mice prevent the induction of EAE by αB-crystallin while the subdominant or cryptic epitope is able to circumvent these mechanisms and contribute to pathogenic myelin-directed autoimmunity following T cell activation. (C) 2000 Elsevier Science, B.V. Chemicals/CAS: Crystallins; Epitopes