The HLA Molecules DQA1*0501/B1*0201 and DQA1*0301/B1*0302 Share an Extensive Overlap in Peptide Binding Specificity

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The HLA molecules DQA1*0501/B1*0201 and DQA1*0301/B1*0302 share an extensive overlap in peptide binding specificity.

Assays to measure the binding capacity of peptides for HLA-DQA1*0501/B*0201 (DQ2.3) and DQA1*0301/B*0302 (DQ3.2) were developed using solubilized MHC molecules purified from EBV-transformed cell lines. These quantitative assays, based on the principle of the inhibition of binding of a high-affinity radiolabeled ligand, were validated by examining the binding capacity of known DQ-restricted epit...

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Five HLA-DP molecules frequently expressed in the worldwide human population share a common HLA supertypic binding specificity.

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Peptide binding specificity of HLA-DR4 molecules: correlation with rheumatoid arthritis association

We have investigated whether sequence 67 to 74 shared by beta chains of rheumatoid arthritis (RA)-associated HLA-DR molecules imparts a specific pattern of peptide binding. The peptide binding specificity of the RA-associated molecules, DRB1*0401, DRB1*0404, and the closely related, RA nonassociated DRB1*0402 was, therefore, determined using designer peptide libraries. The effect of single key ...

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Major Histocompatibility Complex (MHC) peptide interactions are at the heart of the cellular immune response, as they are responsible for the presentation of pathogen-derived peptides on the surface of infected cells. Therefore considerable experimental and computational efforts have been made to characterize this interaction and predict epitopes for peptide-based vaccines. This task is complic...

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HLA-DP4, the most frequent HLA II molecule, defines a new supertype of peptide-binding specificity.

Among HLA-DP specificities, HLA-DP4 specificity involves at least two molecules, HLA-DPA1*0103/DPB1*0401 (DP401) and HLA-DPA1*0103/DPB1*0402 (DP402), which differ from each other by only three residues. Together, they are present worldwide at an allelic frequency of 20-60% and are the most abundant human HLA II alleles. Strikingly, the peptide-binding specificities of these molecules have never...

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ژورنال

عنوان ژورنال: The Journal of Immunology

سال: 2002

ISSN: 0022-1767,1550-6606

DOI: 10.4049/jimmunol.169.9.5098