Synthetic peptides that inhibit binding of the myelin basic protein 85-99 epitope to multiple sclerosis-associated HLA-DR2 molecules and MBP-specific T-cell responses
Identifieur interne : 003504 ( Main/Exploration ); précédent : 003503; suivant : 003505Synthetic peptides that inhibit binding of the myelin basic protein 85-99 epitope to multiple sclerosis-associated HLA-DR2 molecules and MBP-specific T-cell responses
Auteurs : Masha Fridkis-Hareli [États-Unis] ; Joel N. H Stern [États-Unis] ; Lars Fugger [Danemark] ; Jack L. Strominger [États-Unis]Source :
- Human Immunology [ 0198-8859 ] ; 2001.
English descriptors
- KwdEn :
- Teeft :
- Acad, Amino acids, Antigen presentation, Arnon, Assay, Binding motif, Binding motifs, Biotinylated, Cell clones, Clone, Copolymer, Crystal structure, Encephalomyelitis, Epitope, Final peptide concentration, Hafler, Histocompatibility, Hy1b, Immunodominant, Immunodominant epitope, Immunodominant myelin, Immunol, Inhibitor, Major histocompatibility, Methods section, Molecule, Multiple sclerosis, Myelin, Natl, Peptide, Polyclonal antibodies, Proc, Proc natl acad, Protein peptide, Random polypeptides, Sclerosis, Sela, Several peptides, Side chains, Sodium chloride, Strominger, Synthetic peptides, Teitelbaum, Unlabeled, Wucherpfennig.
Abstract
Abstract: Copolymer 1 (Cop 1, poly [Y, E, A, K]) is a random synthetic amino acid copolymer effective in the treatment of relapsing forms of multiple sclerosis (MS), a disease that is linked to HLA-DR2 (DRB1∗1501). In the present study various peptides, synthesized according to the binding motifs for both the immunodominant epitope of myelin basic protein (MBP) 85-99, a candidate autoantigen in MS, and Cop 1, differentially inhibited binding of these antigens to disease-associated HLA-DR2 (DRB1∗1501) molecules. In particular, two peptides with residue K at position P-1, as referred to MBP 85-99, inhibited effectively the binding of both biotinylated MBP 85-99 and Cop 1 to HLA-DR2 molecules as well as IL-2 production by two MBP-specific HLA-DR2-restricted T-cell clones. These findings suggest the possible utility of these compounds or their more stable derivatives in treatment of MS.
Url:
DOI: 10.1016/S0198-8859(01)00279-8
Affiliations:
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Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cop 1</term>
<term>HA</term>
<term>HLA-DR</term>
<term>MBP</term>
<term>MS</term>
<term>RA</term>
<term>T cells</term>
<term>peptides</term>
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<term>Antigen presentation</term>
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<term>Assay</term>
<term>Binding motif</term>
<term>Binding motifs</term>
<term>Biotinylated</term>
<term>Cell clones</term>
<term>Clone</term>
<term>Copolymer</term>
<term>Crystal structure</term>
<term>Encephalomyelitis</term>
<term>Epitope</term>
<term>Final peptide concentration</term>
<term>Hafler</term>
<term>Histocompatibility</term>
<term>Hy1b</term>
<term>Immunodominant</term>
<term>Immunodominant epitope</term>
<term>Immunodominant myelin</term>
<term>Immunol</term>
<term>Inhibitor</term>
<term>Major histocompatibility</term>
<term>Methods section</term>
<term>Molecule</term>
<term>Multiple sclerosis</term>
<term>Myelin</term>
<term>Natl</term>
<term>Peptide</term>
<term>Polyclonal antibodies</term>
<term>Proc</term>
<term>Proc natl acad</term>
<term>Protein peptide</term>
<term>Random polypeptides</term>
<term>Sclerosis</term>
<term>Sela</term>
<term>Several peptides</term>
<term>Side chains</term>
<term>Sodium chloride</term>
<term>Strominger</term>
<term>Synthetic peptides</term>
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<front><div type="abstract" xml:lang="en">Abstract: Copolymer 1 (Cop 1, poly [Y, E, A, K]) is a random synthetic amino acid copolymer effective in the treatment of relapsing forms of multiple sclerosis (MS), a disease that is linked to HLA-DR2 (DRB1∗1501). In the present study various peptides, synthesized according to the binding motifs for both the immunodominant epitope of myelin basic protein (MBP) 85-99, a candidate autoantigen in MS, and Cop 1, differentially inhibited binding of these antigens to disease-associated HLA-DR2 (DRB1∗1501) molecules. In particular, two peptides with residue K at position P-1, as referred to MBP 85-99, inhibited effectively the binding of both biotinylated MBP 85-99 and Cop 1 to HLA-DR2 molecules as well as IL-2 production by two MBP-specific HLA-DR2-restricted T-cell clones. These findings suggest the possible utility of these compounds or their more stable derivatives in treatment of MS.</div>
</front>
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