Heterogeneity of Anti-A and Anti-B Monoclonal Reagents

Gane, Pierre; Vellayoudom, J.; Mollicone, Rosella; Breimer, Michael E.; Samuelsson, Bo E.; Rouger, Ph.; Gérard, G.; Pendu, Jacques Le; Colobran, Roger

doi:10.1159/000461709

Cited by 3 publications

(3 citation statements)

References 7 publications

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“…This lectin recognizes the Leb and Y antigens (Spohr et al, 1985). Specificities of anti-A (Gane et al, 1987b), anti-B and anti-H or Lewis-related structures were defined with the synthetic oligosaccharides prepared by Dr R. U. Lemieux and Chembiomed Ltd (Edmonton, Canada).…”

Section: Anti-lewis-related Reagentsmentioning

confidence: 99%

Expression of Abh, Lewis and Related Tissue Antigens in the Human Thymus

Pendu

Dalix

Mollicone

et al. 1989

Int J Immunogenetics

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SUMMARY Expression of ABH, Lewis and related antigens was studied in the thymus of children of known ABO, Lewis and secretor status using a panel of specific reagents. ABH and Lewis antigens partly under control of the secretor status were expressed on the Hassals' bodies and a large fraction of the medullary epithelial cells. The sialyl‐Lea antigen was only present on some Hassals' bodies of Lewis‐positive individuals. ABH but not Lewis antigens were also present on cortical epithelial cells but this was independent of the secretor status. The X, sialyl‐X and Y antigens were only expressed on Hassals' bodies irrespective of the ABO, Lewis or secretor phenotype. Furthermore, the anti‐X and sialyl‐X antibodies labelled a subset of leucocytes of all the individuals tested. These results show that the genetic control of the expression of ABH and Lewis glycosidic tissue alloantigens in the thymus is different on cortical and medullary epithelial cells and stress the heterogeneity of the thymus epithelial cells.

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Section: Anti-lewis-related Reagentsmentioning

confidence: 99%

Expression of Abh, Lewis and Related Tissue Antigens in the Human Thymus

Pendu

Dalix

Mollicone

et al. 1989

Int J Immunogenetics

Self Cite

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“…The results in agglutination are compatible with this view. Interestingly, another monoclonal anti-A with high affinity for difucosylated type 2 chains was shown recently to agglutinate A, cells strongly (22). One may presume, therefore, that many A, cells have high proportions of difucosylated A oligosaccharides, while the proportion is usually lower on A, cells.…”

Section: Discussionmentioning

confidence: 99%

A study of immunogold‐labelled blood group A erythrocytes in the scanning electron microscope

Heier¹,

Namork²,

Falleth³

1988

European J of Haematology

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This report presents binding patterns on A1, A2, A3, Ax and Ae1 erythrocytes of a monoclonal anti‐A (A 003) antibody which reacts predominantly with difucosylated A oligosacccharides, visualized with colloidal gold particles in the backscattered electron imaging mode of a scanning electron microscope. A relatively weak labelling was found on most A, cells, while the labelling in subgroups A2, A3 and especially Ax appeared relatively stronger. Very few Ae1 cells were labelled. The results emphasize the qualitative uniqueness of A1 and suggest that many Ax cells have high proportions of difucosylated A oligosaccharides. Labelling variations were found between different A3 and Ax traits, and in all subgroups between cells and even between different parts of the cells. No immunolabelling differences were found in relation to secretor status.

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“…The relative inability of AL62 to agglutinate untreated A2B cells would appear paradoxical. Other antibodies have been reported [25] that, like AL62, recognize A type 3 and H type 3 oligosaccharides. Such antibodies, like AL62, give good agglutination of Al cells (which have A type 3) and A2 cells (which have H type 3); antibodies that recognize A type 3 but not H type 3 are anti-Al specific [26].…”

Section: Discussionmentioning

confidence: 99%

Analysis of the Heterogeneity of the Binding Site Specificities of Hyperimmune Human Anti‐A and ‐A,B Sera: The Application of Competition Assays Using Murine Monoclonal Antibodies

Lubenko¹,

Savage²

1989

Vox Sanguinis

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Monoclonal antibodies PL41 and AL62 have previously been shown to recognize two distinct blood group A epitopes on the red cell surface. Competitive inhibition of the binding of 125I-PL41 and 125I-AL62 to group A1 red cells, by hyperimmune polyclonal human antibodies, has been employed to investigate the binding site specificities of 15 anti-A and 8 anti-A,B sera. Differences in the degree of inhibition of the binding of the two MABs by individual anti-A or -A,B samples indicate that polyclonal reagents are composed of varying proportions of up to 3 (or more) different antibody specificities, each recognizing a distinct epitope: PL41-like, AL62-like and a third (as yet undefined) category of antibody. In general, those anti-A sera with PL41-like specificities are superior agglutinators of A2B cells with weakly expressed A antigens; similarly, the specificity of potent anti-A,B, sera capable of strongly agglutinating Ax cells was likewise directed towards PL41-binding blood group A trisaccharide haptens.

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Heterogeneity of Anti-A and Anti-B Monoclonal Reagents

Cited by 3 publications

References 7 publications

Expression of Abh, Lewis and Related Tissue Antigens in the Human Thymus

Expression of Abh, Lewis and Related Tissue Antigens in the Human Thymus

A study of immunogold‐labelled blood group A erythrocytes in the scanning electron microscope

Analysis of the Heterogeneity of the Binding Site Specificities of Hyperimmune Human Anti‐A and ‐A,B Sera: The Application of Competition Assays Using Murine Monoclonal Antibodies

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