An Antibody, in the Serum of a Wr(a+) Individual, Reacting with an Antigen of Very High Frequency

Adams, John H.; Broviac, M.; Brooks, Wiley H.; Johnson, Natalie R.; Issitt, Peter D.

doi:10.1111/j.1537-2995.1971.tb04416.x

Cited by 54 publications

(14 citation statements)

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“…Positions of the amino acid substitutions associated with the Diego system antigens are shown. The name anti -Wr b was provisionally used in 1971 for an antibody, in the serum of a Wr(a + ) woman, that detected a high frequency antigen [6] . The large cytoplasmic N -terminal domain is not shown.…”

Section: Anti-di a And -Di Bmentioning

confidence: 99%

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Diego Blood Group System

Daniels

2013

Human Blood Groups

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Section: Anti-di a And -Di Bmentioning

confidence: 99%

“…Alloanti -Wr b has been found in the sera of the three Wr(a + b -) patients [6,99,100] , plus some Wr(a -b -) individuals with certain rare MNS phenotypes (Sections 3.5 and 3.10). Wr b is generally considered resistant to treatment of red cells with proteases, but one anti -Wr b did not react with fi cin -or papain -treated red cells [100] .…”

Section: Anti-wr Bmentioning

confidence: 99%

Diego Blood Group System

Daniels

2013

Human Blood Groups

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“…Data obtained with Wr(a+b+) membranes from donor S.Z 5. Data obtained with Wr(a-b+) and Wr(a+b+) membranes were similar 6. A^-(3-Dimethylaminopropyl)W-ethylcarbodiimide/glycine ethyl ester.…”

mentioning

confidence: 98%

High Frequency Antigens of Human Erythrocyte Membrane Sialoglycoproteins, III. Studies on the EnFR, Wr and Wr Antigens

Dahr¹,

Wilkinson²,

Issitt³

et al. 1986

Biological Chemistry Hoppe-Seyler

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The nature of the common erythrocyte antigens En a FR and Wr b , that are both absent from En(a-) cells, and the rare Wr a receptor, apparently encoded by an allele of Wr b 9 was investigated. Various modification, fractionation or cleavage products of erythrocyte membranes were used in hemagglutination inhibition assays. The En a FR and Wr b antigens were shown to represent labile structures within the residues approx. 62-72 of the major (MN) sialoglycoprotein that require lipids, at least for complete expression of antigenic activity. During the course of these experiments, the arrangement of the MN glycoprotein's peptide chain with respect to the lipid bi-layer was also studied, using various proteinases. Furthermore, the MN glycoprotein was found to aggregate with the major membrane protein (band 3) in the presence of Triton X-100. The Wr a antigen was shown to exhibit properties that differ considerably from those of the Wr b receptor. Analyses on the MN glycoprotein, isolated from the red cells of the only known Wr° homozygote and two Wr*Wr b individuals, did not reveal any amino-acid exchange within the residues 40-96 of the molecule. Therefore, the Wr locus that determines the presence or absence of the Wr b antigen on the MN glycoprotein might influence the posttranslational modification of amino-acid residues, the structure of tightly bound lipids or the aggregation of the MN glycoprotein with a different protein such as band 3. Hochfrequente Antigene auf menschlichen Erythrozytenmembran-Sialoglycoproteinen, III. Untersuchungen an den En a FR-, Wr b -und Wi*-AntigenenZusammenfassung: Die Eigenschaften der häu-figen Erythrozytenantigene En a FR and Wr b , die beide in En(a-) Zellen fehlen, und des seltenen Wr a Rezeptors, der offensichtlich durch ein Allel von Wr b kodiert wird, wurden untersucht. Diverse Modifizierungs-, Fraktionierungs-und

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“…[2], The high level of expression of Wra antigen on the red cells of this patient compared with that of her Wr(a+) relatives suggested that she might be a Wr"Wra homozygote. Family studies were inconclusive because only a few members were available for testing.…”

Section: Introductionmentioning

confidence: 99%

Comparative Immunochemical Analysis of Wr^a and Wr^b Red Cell Antigens

Ring¹,

Tippett²,

Swallow³

1994

Vox Sanguinis

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This paper describes immunoblotting and immunoprecipitation studies using monoclonal anti-Wr^a and anti-Wr^b antibodies to investigate the nature of the low- incidence blood group antigen, Wr^a and its high-incidence allelic antigen Wr^b. No membrane components were identified by the immunoblotting experiments. Immunoprecipitation studies confirmed that the Wr^b antigen involves both gly- cophorin A and band 3. The monoclonal anti-Wr ', BGU1-WR^a, failed to immu- noprecipitate these or any other red cell membrane component. The significance of these findings is discussed.

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An Antibody, in the Serum of a Wr(a+) Individual, Reacting with an Antigen of Very High Frequency

Cited by 54 publications

References 0 publications

Diego Blood Group System

Diego Blood Group System

High Frequency Antigens of Human Erythrocyte Membrane Sialoglycoproteins, III. Studies on the EnFR, Wr and Wr Antigens

Comparative Immunochemical Analysis of Wr^a and Wr^b Red Cell Antigens

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