Production of two human hybridomas secreting antibodies to HLA-DRw11 and -DRw8+w12 specificities

Pistillo, Maria Pia; Mazzoleni, Osvaldo; Lü, Kun; Falco, Michela; Tazzari, Pier Luigi; Ferrara, Giovanni Battista

doi:10.1016/0198-8859(91)90010-7

Cited by 17 publications

(4 citation statements)

References 22 publications

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“…Table 1 describes two variations. Human and mouse monoclonal antibodies are specific for rp58E shared between DRB1*11:01/03/04 and DPB1*02, *03, *04:02, *06, *09, *10, *14, *16, *17, *18, *20 and *28 [27][28][29][30][31][32][33][34]. All rp58E-carrying alleles have the same 54G, 55R, 56P, 57D, 60Y, 61W and 62N residues within a 3.5 Ångstrom radius and the reactivity of a rp58E-specific antibody is unaffected by the presence of 59D* which has a Blosum score of +2 when compared to 59E.…”

Section: Antibody-verified Interlocus Rp58e and Rp58ee Epletsmentioning

confidence: 99%

Eplet-Based HLA Class II Matching for Transplantation: Design of a Repertoire of Interlocus Eplets Shared between HLA-DR, -DQ and -DP Alleles

Duquesnoy¹,

Marrari²

2020

OBM Transplantation

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Many studies have demonstrated that HLA-DR, HLA-DQ and HLA-DP matching at the eplet level reduces allograft rejection and improves transplant outcome. Such studies have examined the eplet effect for the individual class II loci, but until now little attention has been given to so-called interlocus class II eplets shared between HLA-DR, HLA-DQ and/or HLA-DP alleles. This report summarizes current information about antibody-verified interlocus class II eplets. It describes a structural modeling method to determine potentially immunogenic interlocus class II eplets and to identify non-immunogenic eplets because they are monomorphic at another class II locus. We propose that the inclusion of interlocus class II eplets will enhance the efficiency of eplet-based HLA-DR,-DQ,-DP matching in organ transplantation.

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Section: Antibody-verified Interlocus Rp58e and Rp58ee Epletsmentioning

confidence: 99%

Eplet-Based HLA Class II Matching for Transplantation: Design of a Repertoire of Interlocus Eplets Shared between HLA-DR, -DQ and -DP Alleles

Duquesnoy¹,

Marrari²

2020

OBM Transplantation

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“…[10][11][12][13][14][30][31][32][33][34][35] Critical residues defining serotypes or determining epitopes of HLA class II products were identified by similar approaches for HLA-DR, [36][37][38][39][40][41][42][43] DQ [43][44][45] and DP. [46][47][48] Many of the epitopes defined in early studies were identified by non-human mAbs; additional work confirmed that these same epitopes were also identified by both, allo-antisera and mAbs of human origin. 6,7,49,50 The simultaneous application of molecular typing methods and serologic testing in IHIW exercises allowed inference of which amino acids at polymorphic positions in the HLA class I and class II proteins, may determine epitopes recognized by sets of mAbs or by clusters of alloantibody reagents evaluated in the 12th 4,5 and 13th 6,7 IHIW.…”

Section: Introductionmentioning

confidence: 81%

“…The evaluation of the reactivity of mAbs with different alleles allowed for the identification of residues possibly defining HLA class I epitopes to be mapped to residues shared by different alleles 10–14,30–35 . Critical residues defining serotypes or determining epitopes of HLA class II products were identified by similar approaches for HLA‐DR, 36–43 DQ 43–45 and DP 46–48 . Many of the epitopes defined in early studies were identified by non‐human mAbs; additional work confirmed that these same epitopes were also identified by both, allo‐antisera and mAbs of human origin 6,7,49,50 …”

Section: Introductionmentioning

confidence: 97%

A new strategy for systematically classifying HLA alleles into serological specificities

Osoegawa

Marsh

Holdsworth

et al. 2022

HLA

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HLA serological specificities were defined by the reactivity of HLA molecules with sets of sera and monoclonal antibodies. Many recently identified alleles defined by molecular typing lack their serotype assignment. We surveyed the literature describing the correlation of the reactivity of serologic reagents with AA residues. 20 ‐ 25 AA residues determining epitopes (DEP) that correlated with 82 WHO serologic specificities were identified for HLA class I loci. Thirteen DEP each located in the beta‐1 domains that correlated with 24 WHO serologic specificities were identified for HLA‐DRB1 and ‐DQB1 loci. The designation of possible HLA‐DPB1, ‐DQA1, ‐DPA1, and additional serological specificities that result from epitopes defined by residues located at both ‐DQA1 and ‐DQB1 subunits were also examined. HATS software was developed for automated serotype assignments to HLA alleles in one of the three hierarchical matching criteria: (1) all DEP (FULL); (2) selected DEP specific to each serological specificity (SEROTYPE); (3) one AA mismatch with one or more SEROTYPES (INCOMPLETE). Results were validated by evaluating the alleles whose serotypes do not correspond to the first field of the allele name listed in the HLA dictionary. Additional 85 and 21 DEP patterns that do not correspond to any WHO serologic specificities for common HLA class I and DRB1 alleles were identified, respectively. A comprehensive antibody identification panel would allow for accurate unacceptable antigen listing and compatibility predictions in solid organ transplantation. We propose that antibody‐screening panels should include all serologic specificities identified in this study.

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“…(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. (15,(22)(23)(24)(25) Another approach is to use affinity or lectin columnpurified HLA-DR as the immunogen, an approach that results in a predominance of anti-HLA-DRa MAb, (10,26) some of which react to the HLA-DRa cytoplasmic domain. (27) Synthetic peptides of antigenic segments are often employed as a method for developing MAb that target linear epitopes (4) and could be useful for Western blot analysis.…”

Section: Introductionmentioning

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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Production of two human hybridomas secreting antibodies to HLA-DRw11 and -DRw8+w12 specificities

Cited by 17 publications

References 22 publications

Eplet-Based HLA Class II Matching for Transplantation: Design of a Repertoire of Interlocus Eplets Shared between HLA-DR, -DQ and -DP Alleles

Eplet-Based HLA Class II Matching for Transplantation: Design of a Repertoire of Interlocus Eplets Shared between HLA-DR, -DQ and -DP Alleles

A new strategy for systematically classifying HLA alleles into serological specificities

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

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