Association of the M blood group system with bovine mastitis*

Associations of the 11 bovine blood group systems with mastitis were examined in Red Danish dairy cattle. The mastitis status was followed during three lactational periods. A significant effect of the M blood group system on mastitis incidence was observed in the first and second lactation periods and a lower frequency of mastitis is found among animals lacking the M' factor as compared to those having the M' blood group factor. The significance of these results are discussed in view of the close relation between the M blood group system and the bovine lymphocyte antigens (BoLA), and the expected effect of eliminating the M' gene from the breed is estimated. Among the remaining 10 blood group systems, the T' system was the only system showing an overall effect on mastitis, and only in first and third lactation. However, the T' system was inconsistent with regard to the effect of the T' gene on the various mastitis diagnoses.     

Multiple restriction fragment length polymorphisms associated with the Vc determinant of the MN blood group-related chimpanzee V-A-B-D system

Twelve restriction fragment length polymorphisms (RFLPs) were detected in common chimpanzee using two restriction enzymes (HindIII andMspI) and four DNA probes to the coding regions of the human glycophorin A (GPA) and glycophorin B (GPB) genes and their 3-untranslated regions. Seven RFLPs correlated with red cell expression of the V^c determinant of the MN blood group-related V-A-B-D system and five RFLPs correlated with nonexpression of this antigen. Animals heterozygous for theV allele that encodes the V^c determinant had all 12 polymorphic restriction fragments and appeared to show reduced intensity of probe hybridization to these fragments, consistent with the presence of aV and a non-V allele. No RFLPs were detected withEcoRI,SstI, orBamHI, in spite of the relatively large segment of DNA (at least 20 kb) involved in the polymorphisms. The RFLPs were chimpanzee specific and were not found in man, gorilla, orangutan, or gibbon. Multiple RFLPs distinguishing primate species are rare and may be useful markers for molecular evolution.This work was supported in part by National Institutes of Health Grants AM 33463 and CA 33000.     

A monoclonal antibody to swine erythrocytes recognizes the B blood group on the major glycophorin

Recently monoclonal antibodies (mAbs) to swine red blood cells have been described. One of them (1AC11) was specific for the major swine glycoprotein with a molecular weight of 45 kDa and another mAb, 2G2, recognized the B ^a allele in the B system of swine blood groups. Immunoblotting experiments to characterize the mAb 2G2 indicated that it reacts with an antigen of 45 kDa, present on the aqueous phase, glycophorin fraction, of swine red blood cells with the B ^a allele and does not react with B ^bB^b homozygous cells. The antigen recognized by 2G2 has the same characteristics as the major glycophorin recognized by 1AC11, so we can conclude that the B system of the swine blood group is on the major glycophorin of swine erythrocyte membranes.     

The blood group B type-4 heptaglycosylceramide is a minor blood group B structure in human B kidneys in contrast to the corresponding A type-4 compound in A kidneys. Structural and in vitro biosynthetic studies

Blood group A glycolipid antigens have been found based upon at least four different core saccharides (types 1 to 4). The biological significance of this structural polymorphism is not known, although the successful outcome of transplantations of blood group A₂ kidneys to blood group O individuals have been partly explained by the low expression of A type-3 and -4 chain glycolipid antigens in A₂ kidneys. If graft rejection due to ABO incompatibility is, in any way, correlated to the expression of type-3 and -4 chain blood group glycolipids, it is of interest to identify possible blood group B structures based on these core saccharides. In a non-acid glycosphingolipid fraction isolated from human blood group B kidneys, mass spectrometry, high-temperature gas chromatography-mass spectrometry and probing of thin-layer chromatograms with Galα1–4Gal-specific Escherichia coli and monoclonal anti-B antibodies provided evidence for minute amounts of Gaα1–3(Fucα1–2)Galβ-HexNac-Galα1–4Galβ-Hex-Ceramide structure consistent with a B type-4 chain heptaglycosylceramide. In contrast, blood group A kidneys have the corresponding A type-4 chain heptaglycosylceramide as the predominant glood group A glycolipid. No, or very low activity of the blood group B gene enzyme on the type-4 chain blood group H hexaglycosylceramide precursor was found by biosynthetic experiments in vitro, which migh explain the low expression of type-4 chain blood group heptaglycosylceramides in human blood group B kidneys.     

Biochemical identification of the bovine blood group M' antigen as a major histocompatibility complex class I-like molecule

Absorption and elution experiments showed that it was impossible to separate antibodies against blood group factor M' from antibodies against bovine lymphocyte antigen (BoLA) A16 in an antiserum showing haemolytic activity against M' as well as lymphocytotoxic activity against BoLA-A16. To elucidate the structural relationship between BoLA-A16 and blood group antigen M', immunoprecipitation experiments on red and white cell lysates isolated from M'-A16 positive and negative cattle were carried out. These results showed that M_r 44 000 and M_r 12000 polypeptides can be precipitated from both red and white cells isolated from M'-A16 positive animals, whereas no bands were seen in M'-A16 negative animals in precipitations with the same antibody. Precipitation with a crossreacting human β₂-microglobulin (β₂-m) specific antibody confirmed a class-I-like structure associated with β₂-m on M' positive red cells and the absence of such a structure on M' negative red cells. Sequential precipitations gave analogous results. Proteolytic degradation by papain and V8 protease did not reveal any substantial difference between red and white M'-A16 positive cells, but a slight difference in the pI of the immunoprecipitable components of red and white cells was observed. All together, this indicates that either the blood group antigen M' is the BoLA-A16 class I antigen or M' and BoLA-A16 are two different class I polypeptides with the same relative mass, sharing identical epitopes and both associated with β₂-m. Comparable results were obtained with M₁ and BoLA-A24.     

Mm, a new factor in the porcine M blood group system

By means of a new antiserum, Mm, the Mae phenotype can be shown to be controlled by the Maem allele, the Mef phenotype by either the original Mef or a new Mefm allele, and the Mbe(f) phenotype by the Mbe(f)m allele. The complexity of the porcine M system is now extended to 13 internationally recognized blood group factors controlled by at least 19 alleles.     

Magnetic resonance study of 13C-enriched glycophorin A reconstituted into phospholipid vesicles

$\text{[S-[}{}^{13}\text{C}\text{]}\text{methylmethionine-8 and -81]glycophorin}$ A was reconstituted into l-α-phosphatidyl choline vesicles. Results indicate that the $\text{S-[}{}^{13}\text{C}\text{]}\text{methylmethyionine}\text{-81}$ residue in the phospholipid bilayer has limited mobility and is not susceptible to dealkylation, whereas the opposite effects are indicated for the $\text{S-[}{}^{13}\text{C}\text{]}\text{methylmethionine}\text{-8}$ residue.     

Norovirus binds to blood group A-like antigens in oyster gastrointestinal cells

AIMS: To determine if histo-blood group antigens (HBGA) present in oyster gastrointestinal (GI) cells mediate accumulation of human noroviruses (NoV) in oyster GI cells. METHODS AND RESULTS: HBGA-specific monoclonal antibodies (MAbs) were used to determine the presence of the corresponding HBGA in oyster GI cells. All oyster samples tested contained type A-like HBGA in GI tissue as measured by ELISA. Recombinant Norwalk virus viral like particles (rNVLP) were bound to plates coated with oyster GI homogenate. The binding was inhibited when rNVLPs were pre-incubated with MAbs specific for type A HBGA, or samples of human saliva from type A individuals. Co-localization of rNVLP and type A-like HBGA, but not type B-like or type H-like HBGA, on GI epithelial cells was observed by immunofluorescent histochemical staining and three-channel confocal scanning laser microscopy. CONCLUSION: Type A-like HBGA is present in oyster GI cells and responsible for binding of rNVLP. SIGNIFICANCE AND IMPACT OF THE STUDY: This is the first report of the presence of type A-like HBGA in oyster GI cells and the specific binding of rNVLP to type A-like HBGA on oyster GI cells. The results of this study suggest that human NoV concentrate in oyster GI cells by specific binding to concentrated type A-like HBGA rather than by a nonmolecular entrapment within the tissues.     

Design of the blood group AB glycotope

Although the nature of the blood groups A and B has been comprehensively studied for a long time, it is still unclear as to what exactly is the epitope that is recognized by antibodies having AB specificity, i.e. monoclonal and polyclonal antibodies which are capable of interacting equally well with the antigens GalNAcα 1-3(Fucα 1-2)Gal (A trisaccharide) and Galα 1-3(Fucα 1-2)Gal (B trisaccharide), but do not react with their common fragment Fucα 1-2Gal. We have supposed that besides Fucα 1-2Gal, A and B antigens have one more shared epitope. The trisaccharides A and B are practically identical from the conformational point of view, the only difference being situated at position 2 of Galα residue, i.e. trisaccharide A has a NHAc group, whereas trisaccharide B has a hydroxyl group (see formulas). We have hypothesized that the AB-epitope should be situated in the part of the molecule that is opposite to the NHAc group of GalNAc residue. In order to test this hypothesis we have synthesized a polymeric conjugate in such a way that de-N-acetylated A-trisaccharide is attached to a polymer via the nitrogen in position C-2 of the galactosamine residue. In this conjugate the supposed AB-epitope should be maximally accessible for antibodies from the solution, whereas the discrimination site of antigens A and B by the antibodies should be maximally hidden due to the close proximity of the polymer. Interaction with several anti-AB monoclonal antibodies revealed that a part of them really interacted with the synthetic AB-glycotope, thus confirming our hypothesis. Moreover, similar antibodies were revealed in the blood of healthy blood group 0 donors. Analysis of spatial models was performed in addition to identify the hydroxyl groups of Fuc, Galα, and Galβ residues, which are particularly involved in the composition of the AB-glycotope. Published in 2005.     

Ontogeny and expression of chicken A blood group antigens

Expression of chicken red blood cell (RBC) surface antigens was studied by using a monoclonal antibody (ISU-cA) specific for chicken A blood group antigens. Erythrocytes were examined from embryos of 3-18 days of incubation and from chicks at hatch up to 21 weeks of age. Specific antigens were detected on embryonic RBC surfaces by immunofluorescence as early as 3 days of incubation. Antigenic expression was examined by both haemagglutination and immunofluorescence and found to increase with age from embryos to mature birds. The antigen concentration on the cell surface was found to be affected by genotype; heterozygotes had an intermediate level of antigen between that of the two parental genotypes. These data confirm the co-dominance that is observed with most blood group antigens. Flow cytometric analysis allowed confirmation that the entire erythrocyte population gradually increased in antigenic expression over time, rather than having an antigen-negative subpopulation being replaced by a positive subpopulation.     

ABO blood group system

The accuracy of regular serum methods to detect ABO blood groups can be negatively affected by some factors, such as irregular antibodies, autoantibodies or effects of diseases leading to false or weak agglutination. This study aimed to accurately identify ambiguous ABO blood groups by serological and gene detection methods. The samples were collected in the First Affiliated Hospital of Nanjing Medical University from December 2018 to December 2019. ABO genotyping was performed by polymerase chain reaction-sequence specific primer (PCR-SSP) method in 20 samples, and ABO exons 6 and 7 or FUT1 and FUT2 genes were sequenced in 5 samples. The genes detected in the 21 specimens included 4 cases of A/B, 2 cases of A205/O01, 3 cases of A/O01, 3 cases of A/O02, 1 case of O01/O01, 1 case of O01/O02, 1 case of B/O01, 1 case of B/O02, 1 case of Bel/O01, 1 case of Cisab01/O01, 1 case of rare B/O04, 1 case of Bombay-like Bmh, 1 case of new gene showing c.261del G of exon 6, c.579 T > C of exon 7 and B new/O01. This study suggests that ABO blood group genotyping technology combined with serological typing can be used for accurately typing ambiguous blood groups.     

Structural characterization of blood group A glycosphingolipids recognized by the antibody 3G9-A

In this study, the antibody 3G9-A was assayed for activity against human erythrocyte glycosphingolipids. The antibody was found to recognize glycosphingolipid components from blood group A erythrocytes but not glycosphingolipids from blood group B or O erythrocytes. Subsequent investigation revealed that the glycosphingolipid components recognized by the antibody were also recognized by a blood group A specific monoclonal antibody. The structures of two of the isolated active glycosphingolipid components were structurally characterized using proteon nuclear magnetic resonance (¹H NMR) and gas chromatography-mass spectrometry (GC-MS) techniques and were found to consist of two blood group A glycosphingolipids; the type 2 chain A^b and type 3 chain A^a glycosphingolipids. Subsequent analysis of the remaining active components by GC-MS and immunostaining techniques revealed that all of the active components were blood group A glycosphingolipids. Furthermore, structural studies of the active components suggested that the epitope of the antibody consisted of the group A trisaccharide, GalNAc1,3(Fuc1,2)Gal.Abbreviations GC-MS gas chromatography-mass spectrometry - ¹H NMR proton nuclear magnetic resonance - Gal d-galactose - Glc d-glucose - Fuc l-fucose - GalNAc N-acetylgalactosamine - GlcNAc N-acetylglucosamine - Cer ceramide - mAb monoclonal antibody - BSA bovine serum albumin - PBS phosphate buffered saline - FID free induction decay - PMAA partially methylated alditol acetates     

Vicia villosa B4 lectin is the second anti-Tn lectin shown to react better with blood group N than M antigen

Earlier studies showed thatMoluccella laevis lectin, which has anti-Tn specificity, reacts more strongly with native or desialylated blood group N glycophorin A than with the respective glycophorins of blood group M. We now present results indicating thatVicia villosa B4 anti-Tn lectin, which does not show detectable reaction with untreated glycophorins or erythrocytes, reacts better with desialylated blood group N antigen than with asialo M antigen. This was demonstrated by three assays: (1) agglutination of asialoerythrocytes; (2) binding of biotinylated lectin to asialoerythrocytes immobilized on ELISA plates; and (3) inhibition of lectin binding to asialo-agalactoglycophorin with asialoglycophorins M and N. These results supply further support for the conclusion that glycophorin of blood group N has more GalNAc residues unsubstituted with Gal (Tn receptors) than glycophorin of blood group M.Abbreviations GPA glycophorin A - GPA-M and GPA-N GPA from OM and ON erythrocytes, respectively - MLL Moluccella laevis lectin - PBS 0.02m phosphate buffer/0.15m NaCl, pH 7.4 - PNA peanut agglutinin - RBC erythrocytes - TBS 0.05m Tris buffer/0.15m NaCl, pH 7.4 - TBS-T TBS containing 0.02% Tween 20 - VVL Vicia villosa B4 lectin     

Serology and gene sequence analysis of rare subgroup A3 blood group

To investigate the serological phenotypic characteristics and possible mechanism of subgroup A₃, a blood donor's ABO phenotypes were detected by the conventional microcolumn gel method and classic tube method. N-acetylgalactosaminyl transferase activity was detected by the non-radioactive phosphate coupling method. ABO subtype genotyping was determined by PCR-SSP and exons 1-7 of ABO gene were analyzed by Sanger sequencing. The donor's blood type was subgroup A₃ as evaluated by serological test. There was no N-acetylgalactosaminyl transferase activity in the red blood cells and weak N-acetylgalactosaminyl transferase activity in the plasma. The ABO blood group genotyping result was ABO*AO1, and the gene sequencing result was confirmed as A221/O01. Sequencing results showed two mutations, 467C>T and 607G>A in exon 7 in ABO*A allele. In conclusion, it is suggested that the ABO blood group of the donor be subgroup A₃, which may be induced by mutations 467C>T and 607G>A, and led to a decrease in N-acetylgalactosaminyl transferase activity and resulted in weakened A antigen.     

ABO blood group and secretor status in the spondyloarthropathies

Abstract The postulated role of infectious agents, genetic susceptibility of the host to infection and their interaction in the pathogenesis of ankylosing spondylitis, other spondyloarthropathies, and the associated primary (non-arthritic) diseases are reviewed.
Compared with a local control population there is a significantly increased prevalence of non-secretors amongst different groups of patients with spondyloarthropathy: ankylosing spondylitis, reactive arthritis and psoriatic arthropathy. No differences between secretor and non-secretor patients with respect to serum and salivary IgA levels, the occurrence of eye lesions or peripheral joint disease have been found. There is no evidence that ankylosing spondylitis or other spondyloarthropathies are associated with any particular ABO blood group.
The association between non-secretion and ankylosing spondylitis strengthens the hypothesis that ankylosing spondylitis has an infective aetiology. It also suggests several pathogenetic mechanisms which may be relevant to the initial host-parasite interactions in the spondyloarthropathies.     

Apparent destruction of bovine blood group determinants by chymotrypsin

Although chymotrypsin treatment eliminated the reactivity of many antigenic determinants on the bovine red cell, haemolytic inhibition tests, double diffusion in agar tests, and immunizations provided no conclusive evidence of any of the affected determinants in the soluble digest. Chymotryptic digestion unmasked an apparent cryptantigen, rendering Q-positive cells reactive with a previously Q-negative antiserum.     

The occurrence of the feline A blood group antigen on lymphocytes

Sera from 300 cats were tested for the presence of anti-lymphocytic antibodies. One hundred and nineteen sera showed some activity with the majority (79) reacting only with lymphocytes from blood group A cats. Absorption of two such sera with A, AB and B erythrocytes and absorption of AB system reagents with lymphocytes from A and B blood group cats demonstrated that the A antigen is expressed on both erythrocytes and lymphocytes. Blood group and lymphocyte typing tests of foetuses indicated that the A antigen is present on these tissues as early as 46 days gestation. The erythrocytic B antigen could not be demonstrated on lymphocytes although a single antiserum, which reacted against lymphocytes from group B cats, was found. Several sera containing anti-lymphocytic antibodies which were not related to the AB type were also detected.