Mouse Monoclonal Antibodies with Anti-A,
Anti-B and Anti-A,B Specificities; Some Superior to
Human Polyclonal ABO Reagents

The human ABO blood group determinants are simple carbohydrate structures which are widely distributed in nature. Much work has been done on the structure of the A and B antigens but little is known on the regulation of anti-A and anti-B immune responses. To develop a model system, we have characterized the AB0 immunity of normal Balb/c mice and found a significant level of serum natural anti-A but almost no anti-B. This finding and the known IgM predominance among immune anti-A produced in the Balb/c mouse indicate that the ABO immunity of this mouse strain is comparable to the one of human blood group B individuals. Following immunization with human red blood cells, similar levels of anti-A were produced in normal and athymie Balb/c mice showing that the anti-A response is T cell independent. Furthermore, no anti-A or anti-B antibodies were produced in CBA/xid mice indicating a type 2 T-cell-independent immune response. These results may contribute to a better understanding of human AB0 responses and establish the mouse as a suitable model to study the immunobiology of AB0 antigens.

Section: Natural Abo Immunity In Balb/c Micesupporting

confidence: 75%

Type 2 T-Cell-Independent Murine Immune Response to the Human ABO Blood Group Antigens

Néron¹,

Lemieux²

1994

“…The main conclusion of this study, in agreement with Messeter et al [45], is that some monoclonal antibodies are better agglutinating reagents for some weak A or B variants than the conventional polyclonal antibodies.…”

Section: Binding Of P1a2 and P1a4 On Glycolipids Separated By Thin-lasupporting

confidence: 92%

Heterogeneity of Anti-A and Anti-B Monoclonal Reagents

Gane¹,

Vellayoudom²,

Mollicone³

et al. 1987

Eight anti-A and seven anti-B monoclonal reagents were tested in parallel, with normal and weak ABH red cell phenotypes. A whole range of different reactivity patterns was found, but by making a comparison with the results obtained using polyclonal standard reagents, two major categories of reagents were distinguished: (a) stronger and more specific reagents, and (b) reagents similar to, or weaker than, the standard polyclonal controls. The analysis of the specificity of the reagents by tissue fluorescence staining and reactivity with synthetic oligosaccharides and purified glycolipids confirmed the existence of broad and restricted specificities. Two kinds of anti-A(1) reagents are described. One related to type 3/4 structures, which stains the Golgi apparatus, and another with broad anti-A specificity which cross-reacts with ‘A-like’ structures. The inhibition of anti-A reagents with salivas and synthetic oligosaccharide antigens gave parallel results for the secretor salivas and the difucosylated A antigens.

“…Investigation revealed that the blood donors concerned had elevated levels of the B-determining enzyme, D-galactosyltransferase, and that this enzyme in addition to its nor mal function of transferring Z)-galactose to the acceptor substrate has the capacity to transfer the A-determining sugar N-acetyl-Z)-galactosamine. Incidentally, Beck et al [15] pointed out that the in vitro biosynthesis of blood group B determinants by the A transferase had been demon strated by Yates and Watkins [16], and predicted that a similar phenomenon would be observed using potent monoclonal anti-B reagents with group A cells. This has in fact been noted by Sonneborn and Voak [17] and more recently by ourselves.…”

Section: Discussionmentioning

confidence: 99%

A New Monoclonal Anti-A Antibody BIRMA-1

McDonald¹,

Thompson²

1991

A monoclonal anti-A antibody, BIRMA-1, has been evaluated and found to be eminently suitable as a blood-grouping reagent. The culture supernatant is potent, avid and specific as demonstrated by its reactivity with a large sample of donor bloods tested manually and on the Olympus PK 7100 automated blood grouping machine. Over 100 cord blood samples were tested manually, and all were correctly grouped using this antibody. No false-positive reactions were obtained with papainized group B cells. Reagent prepared from BIRMA-1 detected most examples of Ax and all other A subgroups and A variants tested. Negative reactions with B(A) cells indicate that it is possible to have an antibody capable of detecting Ax which will not react with B cells from individuals with high levels of galactosyltransférase.