| Abstract: |
Based on previous studies it was predicted that amino acids 4 or 25 of the DR4β1 and DR7β1 chains are involved in polymorphic antibody binding epitopes on DR4 or DR7 molecules. These predictions were tested by analyzing monoclonal antibody (mAb) binding to transfectants expressing mutant DR4β1 or DR7β1 chains with single amino acid substitutions at positions 4 or 25. Antibody binding to transfectants expressing additional DR4/7β1 hybrids was also analyzed to assess further the contributions of four segments of the DR4β1 or DR7β1 chains: amino acids 1-20, 21-40, 41-97, and the β 2 domain. Single amino acid substitutions at positions 4 and 25 of the DR4β1 chain or DR7β1 chain eliminate binding of several mAb to DR4 or DR7 molecules, documenting that these residues are involved in antibody epitopes. However, the data with the hybrid DR4/7β1 chains indicate that some of these epitopes require contributions from both segments 1-20 and 21-40 of these DRβ chains, whereas other epitopes can be generated by placing the appropriate segment in the context of the other DRβ chain. In addition, the data with other mAb indicate that their epitopes are determined primarily by sequences within the 41-97 segment or in the β 2 domain. © 1992. |
| Keywords: |
nonhuman; animal cell; mouse; animal; mice; gene expression; amino acid substitution; transfection; monoclonal antibody; molecular cloning; cloning, molecular; fluorescent antibody technique; antibodies, monoclonal; genetic transfection; hla dr antigen; hla-dr antigens; epitope; fibroblast; mutagenesis, site-directed; nucleic acid hybridization; amino acids; antigen binding; mutant; genetic polymorphism; epitopes; beta chain; residue analysis; priority journal; article; polymorphism (genetics); hla dr4 antigen; support, u.s. gov't, p.h.s.; support, u.s. gov't, non-p.h.s.; l cells (cell line); l cell
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