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We have purified HLA-DR from the spleen of a patient with rheumatoid arthritis. The patient had Felty's syndrome and was heterozygous for the DR4Dw4 antigen. We have isolated endogenous peptides from purified HLA-DR molecules. The peptides were purified by reverse phase HPLC and the major peaks were subjected to N-terminal sequencing. The peptides were derived from a variety of proteins: human serum albumin, human erythroid protein 4.1, 60S ribosomal proteins L31 and L35, VCAM-1, human immunoglobulin lambda chain and cathepsin-S. A peptide corresponding to the sequence of human serum albumin (HSA) residues 106-120 was synthesized and shown to bind to HLA-DR4Dw4 (IC50 = 1.41 microM). We have confirmed and refined current ideas about the structural motif for the binding of peptides to HLA-DR and HLA-DR4Dw4.

Original publication

DOI

10.1002/eji.1830250553

Type

Journal article

Journal

European journal of immunology

Publication Date

05/1995

Volume

25

Pages

1473 - 1476

Addresses

ZENECA Pharmaceuticals, Mereside, Alderley Park, Macclesfield, GB.

Keywords

Spleen, Cell Line, Animals, Humans, Spodoptera, Nucleopolyhedrovirus, Arthritis, Rheumatoid, Autoimmune Diseases, Macromolecular Substances, Cathepsins, Neuropeptides, Peptide Fragments, Serum Albumin, Cytoskeletal Proteins, Cell Adhesion Molecules, Vascular Cell Adhesion Molecule-1, Membrane Proteins, Recombinant Fusion Proteins, Ribosomal Proteins, HLA-D Antigens, Autoantigens, Epitopes, Chromatography, High Pressure Liquid, Sequence Alignment, Antigen Presentation, Amino Acid Sequence, Protein Structure, Tertiary, Protein Binding, Sequence Homology, Amino Acid, Genetic Vectors, Molecular Sequence Data, Immunoglobulin lambda-Chains