Use of transfectants to characterize a monoclonal antibody recognizing a monomorphic DR β‐chain epitope shared by some DQ and DP molecules

Cayrol, Corinne; Moro, Françoise; Tkaczuk, Jean; Cambon‐Thomsen, Anne

doi:10.1111/j.1399-0039.1993.tb02002.x

Cited by 1 publication

(2 citation statements)

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“…(9,13,14) Unfortunately, immunization with whole human HLA þ cells may develop antibodies predominantly directed against other non-HLA molecules on the cell surface. (15,16) Later attempts using transfected mouse L cells expressing a single HLA allele raised MAbs specifically against HLA antigens. (15)(16)(17)(18)(19) However, these MAbs usually recognize and bind with native-form HLA class II antigens, but not with denatured proteins.…”

Section: Introductionmentioning

confidence: 99%

“…(15,16) Later attempts using transfected mouse L cells expressing a single HLA allele raised MAbs specifically against HLA antigens. (15)(16)(17)(18)(19) However, these MAbs usually recognize and bind with native-form HLA class II antigens, but not with denatured proteins. (20,21) Epitopes that these conformationally dependent MAbs interact with could be either two discontinuous segments on a single chain or separate aand b-chains.…”

Section: Introductionmentioning

confidence: 99%

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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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