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19. Terminology for Red Cell Surface Antigens. Makuhari Report

Author

Daniels, G.L., primary, Anstee, D.J., additional, Cartron, J. P., additional, Dahr, W., additional, Henry, S., additional, Issitt, P.D., additional, Jorgensen, J., additional, Judd, W.J., additional, Kornstad, L., additional, Levene, C., additional, Lomas-Francis, C., additional, Lubenko, A., additional, Mallory, D., additional, Moulds, J. M., additional, Moulds, J. J., additional, Okubo, Y., additional, Overbeeke, M., additional, Reid, M. E., additional, Rouger, P., additional, Seidl, S., additional, Sistonen, P., additional, Wendel, S., additional, and Zelinski, T., additional

Published
1996
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20. Blood Group Terminology 1995: ISBT Working Party on Terminology for Red Cell Surface Antigens

Author

Daniels, G. L., primary, Anstee, D. J., additional, Cartron, J. P., additional, Dahr, W., additional, Jørgensen, J., additional, Kornstad, L., additional, Levene, C., additional, Lomas-Francis, C., additional, Lubenko, A., additional, Mallory, D., additional, Moulds, J. J., additional, Okubo, Y., additional, Overbeeke, M., additional, Reid, M. E., additional, Rouger, P., additional, Seidl, S., additional, Sistonen, P., additional, Wendel, S., additional, Woodfield, G., additional, and Zelinski, T., additional

Published
1995
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21. ISBT Working Party on Terminology for Red Cell Surface Antigens: São Paulo Report

Author

Daniels, G. L., primary, Moulds, J. J., additional, Anstee, D. J., additional, Bird, G. W. G., additional, Brodheim, E., additional, Cartron, J.-P., additional, Dahr, W., additional, Engelfriet, C. P., additional, Issitt, P. D., additional, Jørgensen, J., additional, Kornstad, L., additional, Lewis, M., additional, Levene, C., additional, Lubenko, A., additional, Mallory, D., additional, Morel, P., additional, Nordhagen, R., additional, Okubo, Y., additional, Reid, M., additional, Rouger, Ph., additional, Salmon, Ch., additional, Seidl, S., additional, Sistonen, P., additional, Wendel, S., additional, Woodfield, G., additional, and Zelinski, T., additional

Published
1993
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24. INTERNATIONAL SOCIETY OF BLOOD TRANSFUSION SOCIÉTÉ INTERNATIONALE DE TRANSFUSION SANGUINE: ISBT Working Party on Terminology for Red Cell Surface Antigens: Los Angeles Report

Author

Lewis, M., primary, Anstee, D.J., additional, Bird, G. W. G., additional, Brodheim, E., additional, Cartron, J.-P., additional, Contreras, M., additional, Dahr, W., additional, Daniels, G. L., additional, Engelfriet, C. P., additional, Issitt, P. D., additional, Jørgensen, J., additional, Kornstad, L., additional, Lubenko, A., additional, McCreary, J., additional, Morel, P., additional, Moulds, J. J., additional, Nevanlinna, H., additional, Nordhagen, R., additional, Okubo, Y., additional, Pehta, J., additional, Rouger, Ph., additional, Rubinstein, P., additional, Salmon, Ch., additional, Seidl, S., additional, Sistonen, P., additional, Tippett, P., additional, Walker, R. H., additional, Woodfield, G., additional, Young, S., additional, and Zelinski, T., additional

Published
1991
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36. N-acetylneuraminyllactose-binding fibrillar hemagglutinin of Campylobacter pylori: a putative colonization factor antigen

Author

Evans, D G, Evans, D J, Moulds, J J, and Graham, D Y

Abstract

Campylobacter pylori is the causative agent of gastritis and possibly of peptic and duodenal ulcers in adults. Histological observations show C. pylori attached to gastric epithelium as well as in the mucus layer of the stomach. We found that clinical isolates of C. pylori possess a cell-bound hemagglutinin detectable with human erythrocytes (all phenotypes tested) and those of a variety of animal species. The C. pylori hemagglutinin is antigenic, heat sensitive, and destroyed by pronase and papain but resistant to pepsin and trypsin. The hemagglutinin has fibrillar morphology; C. pylori-erythrocyte interaction displays very intimate contact, which is typical of fibrillae-mediated attachment. Fibrillae were removed from C. pylori by solubilization with N-octylglucose. After partial purification and removal of N-octylglucose by dialysis, the protein reaggregated, with the assembly of fibrillar structures. Hemagglutination inhibition was observed with the sialoproteins fetuin, alpha 2-macroglobulin, and glycophorin A but not with asialofetuin or asialoglycophorin A. The erythrocyte receptor was more sensitive to destruction by a neuraminidase specific for the N-acetylneuraminyl-alpha(2-3)-galactopyranosyl [NeuAc(2-3)Gal] sequence than one specific for NeuAc(2-6)Gal. Hemagglutination-inhibition assays with N-acetylneuraminyl-alpha(2-3)-lactose [NeuAc(2-3)-lactose] and NeuAc(2-6)-lactose confirmed that the C. pylori hemagglutinin preferentially binds to the NeuAc(2-3)Gal isomer of NeuAc-lactose. Based upon the above-described properties of the C. pylori fibrillar hemagglutinin, we conclude that this antigen should be designated as a putative colonization factor antigen.

Published
1988
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37. Membrane glycophorins of Dantu blood group erythrocytes.

Author

Blumenfeld, O O, Smith, A J, and Moulds, J J

Abstract

Glycophorins of erythrocytes of two unrelated individuals who exhibit the Dantu blood group phenotype were studied. Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin. delta-Glycophorin (glycophorin B) was present in one donor's cells but not the other's; the s and N phenotypes of the latter's erythrocytes may derive from the variant glycophorin. The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins. All these properties are characteristic of delta-glycophorin. The variant is related to alpha-glycophorin in the carboxyl-terminal region as shown by reaction with a specific antiserum. Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin. Sequence analysis of a mixture of CNBr fragments allowed us to conclude that the variant originates from delta-s- rather than delta-S-glycophorin. The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's. This may reflect that the two donors belong to different varieties of Dantu phenotypes. Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins. The results suggest that the unique junction region may be characteristic of the Dantu phenotype.

Published
1987
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46. Molecular identification of Knops blood group polymorphisms found in long homologous region D of complement receptor 1.

Author

Moulds JM, Zimmerman PA, Doumbo OK, Kassambara L, Sagara I, Diallo DA, Atkinson JP, Krych-Goldberg M, Hauhart RE, Hourcade DE, McNamara DT, Birmingham DJ, Rowe JA, Moulds JJ, and Miller LH

Subjects
Animals, Blood Group Antigens immunology, Blood Grouping and Crossmatching, Erythrocytes immunology, Humans, Plasmodium falciparum, Polymorphism, Genetic, Receptors, Complement 3b immunology, Blood Group Antigens genetics, Receptors, Complement 3b genetics
Abstract

Complement receptor 1 (CR1) has been implicated in rosetting of uninfected red blood cells to Plasmodium falciparum-infected cells, and rosette formation is associated with severe malaria. The Knops blood group (KN) is located on CR1 and some of these antigens, ie, McCoy (McC) and Swain-Langley (Sl(a)), show marked frequency differences between Caucasians and Africans. Thus, defining the molecular basis of these antigens may provide new insight into the mechanisms of P falciparum malaria. Monoclonal antibody epitope mapping and serologic inhibition studies using CR1 deletion constructs localized McC and Sl(a) to long homologous repeat D of CR1. Direct DNA sequencing of selected donors identified several single nucleotide polymorphisms in exon 29 coding for complement control protein modules 24 and 25. Two of these appeared to be blood group specific: McC associated with K1590E and Sl(a) with R1601G. These associations were confirmed by inhibition studies using allele-specific mutants. A sequence-specific oligonucleotide probe hybridization assay was developed to genotype several African populations and perform family inheritance studies. Concordance between the 1590 mutation and McC was 94%; that between Sl(a) and 1601 was 88%. All but 2 samples exhibiting discrepancies between the genotype and phenotype were found to be due to low red cell CR1 copy numbers, low or absent expression of some alleles, or heterozygosity combined with low normal levels of CR1. These data further explain the variability observed in previous serologic studies of CR1 and show that DNA and protein-based genetic studies will be needed to clarify the role of the KN antigens in malaria.

Published
2001
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47. Blood group associations with parasites, bacteria, and viruses.

Author

Moulds JM and Moulds JJ

Subjects
Animals, Bacteria, Communicable Diseases microbiology, Humans, Membrane Proteins metabolism, Parasites, Parasitic Diseases parasitology, Viruses, Blood Group Antigens, Communicable Diseases blood, Parasitic Diseases blood
Abstract

Although recent investigations into the human blood groups have proceeded mainly at the molecular level, the RBC remains an exquisite model to study the expression of various genes and their related proteins. Although DNA may be informative, it may not always give meaningful information regarding protein expression on cell surfaces, which is where binding occurs. Because of their easy accessibility, RBCs will continue to be used as a major tool in the investigation of the causative agents for disease, whether they be viral, bacterial, or parasitic in nature.

Published
2000
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49. Membrane dynamics of the water transport protein aquaporin-1 in intact human red cells.

Author

Cho MR, Knowles DW, Smith BL, Moulds JJ, Agre P, Mohandas N, and Golan DE

Subjects
Actins metabolism, Anion Exchange Protein 1, Erythrocyte metabolism, Antibodies immunology, Aquaporin 1, Aquaporins chemistry, Blood Group Antigens, Cell Membrane metabolism, Diffusion, Fluorescein-5-isothiocyanate analogs & derivatives, Fluorescent Dyes, Humans, Membrane Proteins metabolism, Microscopy, Fluorescence, Aquaporins metabolism, Erythrocytes metabolism, Water metabolism
Abstract

Aquaporin-1 (AQP1) is the prototype integral membrane protein water channel. Although the three-dimensional structure and water transport function of the molecule have been described, the physical interactions between AQP1 and other membrane components have not been characterized. Using fluorescein isothiocyanate-anti-Co3 (FITC-anti-Co3), a reagent specific for an extracellular epitope on AQP1, the fluorescence photobleaching recovery (FPR) and fluorescence imaged microdeformation (FIMD) techniques were performed on intact human red cells. By FPR, the fractional mobility of fluorescently labeled AQP1 (F-alphaAQP1) in the undeformed red cell membrane is 66 +/- 10% and the average lateral diffusion coefficient is (3.1 +/- 0.5) x 10(-11) cm2/s. F-alphaAQP1 fractional mobility is not significantly affected by antibody-induced immobilization of the major integral proteins band 3 or glycophorin A, indicating that AQP1 does not exist as a complex with these proteins. FIMD uses pipette aspiration of individual red cells to create a constant but reversible skeletal density gradient. F-alphaAQP1 distribution, like that of lipid-anchored proteins, is not at equilibrium after microdeformation. Over time, approximately 50% of the aspirated F-alphaAQP1 molecules migrate toward the membrane portion that had been maximally dilated, the aspirated cap. Based on the kinetics of migration, the F-alphaAQP1 lateral diffusion coefficient in the membrane projection is estimated to be 6 x 10(-10) cm2/s. These results suggest that AQP1 lateral mobility is regulated in the unperturbed membrane by passive steric hindrance imposed by the spectrin-based membrane skeleton and/or by skeleton-linked membrane components, and that release of these constraints by dilatation of the skeleton allows AQP1 to diffuse much more rapidly in the plane of the membrane.

Published
1999
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50. Terminology for red cell surface antigens. ISBT Working Party Oslo Report. International Society of Blood Transfusion.

Author

Daniels GL, Anstee DJ, Cartron JP, Dahr W, Garratty G, Henry S, Jørgensen J, Judd WJ, Kornstad L, Levene C, Lomas-Francis C, Lubenko A, Moulds JJ, Moulds JM, Moulds M, Overbeeke M, Reid ME, Rouger P, Scott M, Seidl S, Sistonen P, Tani Y, Wendel S, and Zelinski T

Subjects
ABO Blood-Group System immunology, Glycoproteins immunology, Humans, Kell Blood-Group System immunology, Lewis Blood Group Antigens immunology, MNSs Blood-Group System immunology, Phenotype, Rh-Hr Blood-Group System immunology, Serologic Tests, Sweden, Blood Group Antigens immunology, Erythrocyte Membrane immunology, Isoantigens blood, Terminology as Topic
Published
1999
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