HLA-DR polymorphism affects the interaction with CD4
| Autor: | Sylvain Fleury, H E Aronson, Nathalie Labrecque, E. O. Long, G. Croteau, R P Sékaly, C. Cantin, Jacques Thibodeau |
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| Rok vydání: | 1995 |
| Předmět: |
CD4-Positive T-Lymphocytes
Models Molecular Protein Conformation Molecular Sequence Data Immunology Transfection Major histocompatibility complex Mice Structure-Activity Relationship Protein structure MHC class I HLA-DR Animals Humans Immunology and Allergy Amino Acid Sequence Binding site Histocompatibility Antigen H-2D Peptide sequence Alleles HLA-DR Antigen MHC class II Binding Sites Hybridomas Polymorphism Genetic Sequence Homology Amino Acid biology H-2 Antigens HLA-DR Antigens Articles Molecular biology Cell biology CD4 Antigens biology.protein Interleukin-2 Sequence Alignment |
| Zdroj: | The Journal of Experimental Medicine |
| ISSN: | 1540-9538 0022-1007 |
| Popis: | Major histocompatibility complex (MHC) class II molecules are highly polymorphic and bind peptides for presentation to CD4+ T cells. Functional and adhesion assays have shown that CD4 interacts with MHC class II molecules, leading to enhanced responses of CD4+ T cells after the activation of the CD4-associated tyrosine kinase p56lck. We have addressed the possible contribution of allelic polymorphism in the interaction between CD4 and MHC class II molecules. Using mouse DAP-3-transfected cells expressing different isotypes and allelic forms of the HLA-DR molecule, we have shown in a functional assay that a hierarchy exists in the ability of class II molecules to interact with CD4. Also, the study of DR4 subtypes minimized the potential contribution of polymorphic residues of the peptide-binding groove in the interaction with CD4. Chimeras between the DR4 or DR1 molecules, which interact efficiently with CD4, and DRw53, which interacts poorly, allowed the mapping of polymorphic residues between positions beta 180 and 189 that can exert a dramatic influence on the interaction with CD4. |
| Databáze: | OpenAIRE |
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