Molecular basis of two novel high‐prevalence antigens in the Kell blood group system, KALT and KTIM

Lee, Soohee; Debnath, Asim K.; Wu, Xu; Scofield, Terry L.; George, Terry J.; Kakaiya, Ram; Yogore, Mariano G.; Sausais, Laima; Yacob, Michelle; Lomas‐Francis, Christine; Reid, Marion E.

doi:10.1111/j.1537-2995.2006.00899.x

Cited by 19 publications

(21 citation statements)

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“…[38] showed an equal level of activity for KEL1 and KEL2, and the authors noted that this was consistent with the predicted location of residue 193. In addition to these enzymatic studies, novel antigens have been mapped onto the Kell model as they have been discovered [39].…”

Section: Modelling Studies Of Blood Group Active Proteinsmentioning

confidence: 99%

“…However, the results of Sha et al [38] showed an equal level of activity for KEL1 and KEL2, and the authors noted that this was consistent with the predicted location of residue 193. In addition to these enzymatic studies, novel antigens have been mapped onto the Kell model as they have been discovered [39]. The crystal structure of endothelin-converting enzyme 1 (ECE-1) ectodomain has been solved recently [40].…”

Section: Kellmentioning

confidence: 99%

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Structural modelling of red cell surface proteins

Burton

Daniels

2010

Vox Sanguinis

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The red cell surface membranes contain a large variety of proteins, many of which express blood group activity as a result of variation in their oligosaccharide or amino acid sequences. To understand the nature of the blood group epitopes, the functions of the proteins that express them and their relationship to each other, computer modelling has been employed to provide predictions of their structures. Modelling is an excellent method of first resort when experimental structural data for the protein of interest are absent or incomplete. The model can then be used to explain previous experimental data and to direct future experiments. In this review, examples of protein modelling are taken from the Rh, RHAG, Kell, LW, Lutheran, Duffy, Dombrock and RAPH blood group systems.

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Section: Modelling Studies Of Blood Group Active Proteinsmentioning

confidence: 99%

Section: Kellmentioning

confidence: 99%

Structural modelling of red cell surface proteins

Burton

Daniels

2010

Vox Sanguinis

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“…EcoRI-/+ † KEL28-(VONG-)/KEL28+(VONG +) 53 8 862C>T R248W KEL29+ (KALT+)/KEL29-(KALT-) 10 17 1988G>A R623K TfiI+/- † KEL30+ (KTIM+)/KEL30-(KTIM-) 10 baby is at risk during pregnancies in mothers with anti-K. However, because the procedure, although commonly used, is invasive, it should be withheld until the father is typed to determine the potential for a baby with K antigen.…”

Section: R130w R130qmentioning

confidence: 99%

The value of DNA analysis for antigens of the Kell and Kx blood group systems

Lee

2007

Transfusion

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“…Consisting of more than 30 antigens, the Kell blood group system is one of the most polymorphic of the protein blood group systems . Antibodies to antigens in the Kell blood group system are often clinically significant and have caused transfusion reactions and hemolytic disease and anemia of the fetus and newborn .…”

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confidence: 99%

Molecular basis of two novel and related high‐prevalence antigens in the Kell blood group system, KUCI and KANT, and their serologic and spatial association with K11 and KETI

et al. 2013

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Background The numerous antigens in the Kell blood group system result from missense nucleotide changes in KEL. Antibodies to antigens in this system can be clinically important. We describe six probands whose plasma contained antibodies to high-prevalence Kell antigens, and discuss their relationship. Study design and methods PCR amplification, direct sequencing, RFLP assays, hemagglutination, flow cytometry, and protein modeling were performed by standard methods. Results Proband 1 (KUCI), and her serologically-compatible sister, were heterozygous for a nucleotide change in exon 11 (KEL*1271C/T; Ala424Val). Proband 2 (KANT) was heterozygous for KEL*1283G/T (Arg428Leu) and KEL*1216C/T (Arg406Stop) in exon 11. RBCs from Proband 1 and her sister were not agglutinated by plasma from Proband 2; however, RBCs from Proband 2 were agglutinated by plasma from Proband 1. Probands 3, 4, 5, and 6 had the KEL*1391C>T change associated with the previously reported KETI− phenotype. Proband 5 was also homozygous for KEL*905T>C encoding the K11−K17+ phenotype. Hemagglutination studies revealed an association between KUCI, KANT, KETI and K11. Protein modeling indicated that whereas Ala424 and Arg428 are clustered, Val302 and Thr464 are not. Conclusion Ala424 in the Kell glycoprotein is associated with the high-prevalence Kell antigen, KUCI (ISBT 006032), which is detected by the antibody of Proband 1. Arg428 is associated with the high-prevalence Kell antigen, KANT (ISBT 006033). The association between KUCI, KANT, KETI, and K11, and the results of protein modeling are discussed.

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Molecular basis of two novel high‐prevalence antigens in the Kell blood group system, KALT and KTIM

Abstract: The identified KEL mutations of the two probands are novel and inherited. The antigen absent from the red blood cells (RBCs) of Probands 1 and 2 are named KALT and KTIM, respectively. KALT is unique in that it is the only Kell antigen sensitive to treatment of RBCs by trypsin.

Cited by 19 publications

References 20 publications

Structural modelling of red cell surface proteins

Structural modelling of red cell surface proteins

The value of DNA analysis for antigens of the Kell and Kx blood group systems

Molecular basis of two novel and related high‐prevalence antigens in the Kell blood group system, KUCI and KANT, and their serologic and spatial association with K11 and KETI

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