Molecular mimicry in T cell-mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein
Identifieur interne : 001280 ( Main/Merge ); précédent : 001279; suivant : 001281Molecular mimicry in T cell-mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein
Auteurs : Kai W. Wucherpfennig [États-Unis] ; Jack L. Strominger [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1995.
English descriptors
- Teeft :
- Adenovirus, Aliphatic, Allogeneic feeder cells, Amino, Amino acids, Antigenic, Aromatic residues, Aspartic acid, Autoimmunity, Autoreactive, Bacterial peptides, Cell activation, Cell clone, Cell clones, Cell epitope, Cell epitopes, Cell line, Cell lines, Cell proliferation, Cell receptor, Cell recognition, Cell response, Cell stimulation, Cerebrospinal fluid, Clonal, Clonal expansion, Clone, Contact residues, Cytomegalovirus, Drb1, Epitope, Hemagglutinin, Herpes, Herpes simplex, Immunodominant, Immunodominant myelin, Immunodominant peptide, Immunol, Influenza, Influenza type, Lymphocyte, Lytic cycle, Mimicry, Mimicry epitopes, Mimicry peptide, Mimicry peptides, Molecular mimicry, Multiple sclerosis, Multiple sclerosis patients, Mutational analysis, Myelin, Papillomavirus, Pathogen, Peptide, Peptide conformation, Phorbol, Polymerase, Positive control, Protein peptide, Pseudomonas, Sclerosis, Search criteria, Simplex, Stimulatory, Stimulatory capacity, Structural requirements, Substitution, Subtypes, Viral, Viral mimicry peptides, Viral peptides, Wucherpfennig.
Abstract
Abstract: Structural similarity between viral T cell epitopes and self-peptides could lead to the induction of an autoaggressive T cell response. Based on the structural requirements for both MHC class 11 binding and TCR recognition of an immunodominant myelin basic protein (MBP) peptide, criteria for a data base search were developed in which the degeneracy of amino acid side chains required for MHC class 11 binding and the conservation of those required for T cell activation were considered. A panel of 129 peptides that matched the molecular mimicry motif was tested on seven MBP-specific T cell clones from multiple sclerosis patients. Seven viral and one bacterial peptide efficiently activated three of these clones. Only one peptide could have been identified as a molecular mimic by sequence alignment. The observation that a single T cell receptor can recognize quite distinct but structurally related peptides from multiple pathogens has important implications for understanding the pathogenesis of autoimmunity.
Url:
DOI: 10.1016/0092-8674(95)90348-8
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ISTEX:B1572F523C527B4C00D93E43B7B100F47D61DEA0Le document en format XML
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<term>Aliphatic</term>
<term>Allogeneic feeder cells</term>
<term>Amino</term>
<term>Amino acids</term>
<term>Antigenic</term>
<term>Aromatic residues</term>
<term>Aspartic acid</term>
<term>Autoimmunity</term>
<term>Autoreactive</term>
<term>Bacterial peptides</term>
<term>Cell activation</term>
<term>Cell clone</term>
<term>Cell clones</term>
<term>Cell epitope</term>
<term>Cell epitopes</term>
<term>Cell line</term>
<term>Cell lines</term>
<term>Cell proliferation</term>
<term>Cell receptor</term>
<term>Cell recognition</term>
<term>Cell response</term>
<term>Cell stimulation</term>
<term>Cerebrospinal fluid</term>
<term>Clonal</term>
<term>Clonal expansion</term>
<term>Clone</term>
<term>Contact residues</term>
<term>Cytomegalovirus</term>
<term>Drb1</term>
<term>Epitope</term>
<term>Hemagglutinin</term>
<term>Herpes</term>
<term>Herpes simplex</term>
<term>Immunodominant</term>
<term>Immunodominant myelin</term>
<term>Immunodominant peptide</term>
<term>Immunol</term>
<term>Influenza</term>
<term>Influenza type</term>
<term>Lymphocyte</term>
<term>Lytic cycle</term>
<term>Mimicry</term>
<term>Mimicry epitopes</term>
<term>Mimicry peptide</term>
<term>Mimicry peptides</term>
<term>Molecular mimicry</term>
<term>Multiple sclerosis</term>
<term>Multiple sclerosis patients</term>
<term>Mutational analysis</term>
<term>Myelin</term>
<term>Papillomavirus</term>
<term>Pathogen</term>
<term>Peptide</term>
<term>Peptide conformation</term>
<term>Phorbol</term>
<term>Polymerase</term>
<term>Positive control</term>
<term>Protein peptide</term>
<term>Pseudomonas</term>
<term>Sclerosis</term>
<term>Search criteria</term>
<term>Simplex</term>
<term>Stimulatory</term>
<term>Stimulatory capacity</term>
<term>Structural requirements</term>
<term>Substitution</term>
<term>Subtypes</term>
<term>Viral</term>
<term>Viral mimicry peptides</term>
<term>Viral peptides</term>
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<front><div type="abstract" xml:lang="en">Abstract: Structural similarity between viral T cell epitopes and self-peptides could lead to the induction of an autoaggressive T cell response. Based on the structural requirements for both MHC class 11 binding and TCR recognition of an immunodominant myelin basic protein (MBP) peptide, criteria for a data base search were developed in which the degeneracy of amino acid side chains required for MHC class 11 binding and the conservation of those required for T cell activation were considered. A panel of 129 peptides that matched the molecular mimicry motif was tested on seven MBP-specific T cell clones from multiple sclerosis patients. Seven viral and one bacterial peptide efficiently activated three of these clones. Only one peptide could have been identified as a molecular mimic by sequence alignment. The observation that a single T cell receptor can recognize quite distinct but structurally related peptides from multiple pathogens has important implications for understanding the pathogenesis of autoimmunity.</div>
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