A human hybridoma monoclonal antibody (TrJ11) recognizing a new HLA-DR epitope shared by DR4, DR8, DR11, and DRB1∗1303

Ge, Junbo; Bratlie, A.; Hannestad, Kristian

doi:10.1016/0198-8859(94)00083-3

Cited by 5 publications

(2 citation statements)

References 38 publications

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“…The most distinct example is displayed in Figure 2. These findings imply that some polymorphic amino acid residues may be indirectly involved in antibody-antigen interactions by modifying the threedimensional structure of the antigen or by selection of peptides that can fit in the peptide binding groove (19,22). Since many of the identified potential donor antibody epitopes are not surface residues, we further investigated the correlation between antibody cytotoxicity and the location of epitopes.…”

Section: Discussionmentioning

confidence: 99%

Development of Nondonor-Specific HLA-DR Antibodies in Allograft Recipients Is Associated with Shared Epitopes with Mismatched Donor DR Antigens

Cai

Terasaki

Mao

et al. 2006

American Journal of Transplantation

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Our previous studies showed that not only donorspecific antibodies (DSA) but also nondonor-specific antibodies (NDSA) were detected in the peripheral blood of allograft recipients. The molecular mechanism involved in the development of NDSA is examined here. HLA class II single antigen (SA) beads were used to determine the presence of HLA DR-specific antibodies in renal transplant recipients with failed allografts. Sequence-based antibody-epitope mapping was determined by the comparison of the reaction profiles of different SA recombinant cell lines containing unique epitope pattern. We found that 22 out of 65 recipients with failed grafts developed antibodies against donor HLA DR that is a mismatch with the recipient. Three of them had only DSA while 19 patients had not only DSA but also NDSA. An average of 77.3% of NDSA reacted with targets that share amino acid sequence with mismatched donor DR antigens. Either surface or nonsurface amino acid residues may constitute an antibody epitope. In conclusion, development of NDSA in allograft recipients may be associated with shared amino acids with mismatched donor antigens. SA beads technique not only helps to determine antibody specificities but also provides an ideal approach for the identification of potential HLA antibody epitopes.

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Section: Discussionmentioning

confidence: 99%

Development of Nondonor-Specific HLA-DR Antibodies in Allograft Recipients Is Associated with Shared Epitopes with Mismatched Donor DR Antigens

Cai

Terasaki

Mao

et al. 2006

American Journal of Transplantation

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“…(12,34) Monoclonal antibodies available to date that react with denatured HLA-DR antigens are mainly limited in specificity to the cytoplasmic a-chain, or the b-chain N-terminus. (39)(40)(41)(42)(43) Other MAb, such as the HLA-DRa chain-specific MAb HC2.1, (10) may show similar reactivity as 1C4.6, in that both MAb preferentially bind denatured HLA-DRa. However, the HC2.1 epitope within HLA-DRa is yet to be precisely defined.…”

Section: Discussionmentioning

confidence: 99%

A New Monoclonal Antibody Recognizing a Linear Determinant on the HLA-DRα Chain N-terminus

et al. 2009

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We report the generation of a monoclonal antibody (MAb) that reacts to the N-terminus of the denatured HLA-DRalpha chain. The 1C4.6 MAb was raised against a peptide corresponding to amino acid residues 10 to 32 of a highly conserved region within the alpha1 domain of HLA-DR. This region partially overlaps with the epitope recognized by the conformationally dependent L243 MAb. In Western blot analysis, MAb 1C4.6 reacted with denatured HLA-DRalpha chains, but failed to bind the HLA-DRbeta chain expressed individually by transfectant cells, confirming that it recognizes an epitope on the alpha-chain of HLA-DR. In addition, this antibody was found to be isotype specific to HLA-DRalpha, as it did not cross-react to HLA class II proteins HLA-DP and-HLA-DQ. The 1C4.6 MAb is a valuable addition to existing reagents used to probe the structure and function of MHC class II molecules. This anti-HLA-DRalpha1 domain MAb may prove valuable for studies of HLA class II heterodimer assembly, structure, and function, as well as for studies into the release of soluble MHC class II.

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First report on the antibody verification of HLA-DR, HLA-DQ and HLA-DP epitopes recorded in the HLA Epitope Registry

et al. 2014

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A human hybridoma monoclonal antibody (TrJ11) recognizing a new HLA-DR epitope shared by DR4, DR8, DR11, and DRB1∗1303

Cited by 5 publications

References 38 publications

Development of Nondonor-Specific HLA-DR Antibodies in Allograft Recipients Is Associated with Shared Epitopes with Mismatched Donor DR Antigens

Development of Nondonor-Specific HLA-DR Antibodies in Allograft Recipients Is Associated with Shared Epitopes with Mismatched Donor DR Antigens

A New Monoclonal Antibody Recognizing a Linear Determinant on the HLA-DRα Chain N-terminus

First report on the antibody verification of HLA-DR, HLA-DQ and HLA-DP epitopes recorded in the HLA Epitope Registry

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