Mapping of an HLA-DRw52-associated determinant on DR beta 1 molecules.
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Mapping of an HLA-DRw52-associated determinant on DR beta 1 molecules. / Ballas, M; Eiermann, Thomas; Wölpl, A; Goldmann, S F.
In: TISSUE ANTIGENS, Vol. 36, No. 5, 5, 1990, p. 187-193.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Mapping of an HLA-DRw52-associated determinant on DR beta 1 molecules.
AU - Ballas, M
AU - Eiermann, Thomas
AU - Wölpl, A
AU - Goldmann, S F
PY - 1990
Y1 - 1990
N2 - The molecular reaction patterns of the DRw52-specific mouse monoclonal antibodies UL-52 and 7.3.19.1 were investigated. Upon immunoprecipitation and two-dimensional IEF-SDS polyacrylamide gel electrophoresis analysis (2D-PAGE) mAb UL-52 selectively isolated DR beta 1 molecules from DRw52-positive cell lines, whereas mAb 7.3.19.1 predominantly precipitated DR beta 3 molecules. Reduced mAb UL-52 binding affinity was observed to DRw8- and DRw12-positive cells, potentially resulting from structural modifications within the antibody binding site. Comparison of mAb UL-52 reactivity with published DR beta chain amino acid sequences demonstrates that the amino acid residues -S- in positions 11 and 13 on DR beta 1 molecules essentially contribute to the formation of the antibody binding site. mAb 7.3.19.1 reactivity, on the other hand, correlates with the expression of DR beta 3 chain amino acid residues K, G and N, in positions 71, 73 and 77, respectively. In contrast to other DRw52 monoclonal antibodies described so far, mAb UL-52 demonstrates a similar reactivity to DRw52 allosera, suggesting that mAb UL-52 and DRw52 allosera possibly recognize the same or a similar determinant on DR beta 1 molecules.
AB - The molecular reaction patterns of the DRw52-specific mouse monoclonal antibodies UL-52 and 7.3.19.1 were investigated. Upon immunoprecipitation and two-dimensional IEF-SDS polyacrylamide gel electrophoresis analysis (2D-PAGE) mAb UL-52 selectively isolated DR beta 1 molecules from DRw52-positive cell lines, whereas mAb 7.3.19.1 predominantly precipitated DR beta 3 molecules. Reduced mAb UL-52 binding affinity was observed to DRw8- and DRw12-positive cells, potentially resulting from structural modifications within the antibody binding site. Comparison of mAb UL-52 reactivity with published DR beta chain amino acid sequences demonstrates that the amino acid residues -S- in positions 11 and 13 on DR beta 1 molecules essentially contribute to the formation of the antibody binding site. mAb 7.3.19.1 reactivity, on the other hand, correlates with the expression of DR beta 3 chain amino acid residues K, G and N, in positions 71, 73 and 77, respectively. In contrast to other DRw52 monoclonal antibodies described so far, mAb UL-52 demonstrates a similar reactivity to DRw52 allosera, suggesting that mAb UL-52 and DRw52 allosera possibly recognize the same or a similar determinant on DR beta 1 molecules.
M3 - SCORING: Zeitschriftenaufsatz
VL - 36
SP - 187
EP - 193
JO - TISSUE ANTIGENS
JF - TISSUE ANTIGENS
SN - 0001-2815
IS - 5
M1 - 5
ER -