Fy3 antigenicity of blood of newborns.
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Biomedical subjects
Publications and source records attributed to W L Marsh.
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Anti-A and anti-K have been found in the serum of a 20-day-old child who had not been transfused but who was acutely ill with E. coli enterocolitis. Both antibodies are IgM proteins. The mother's serum does not contain either antibody and the anti-A and anti-K in the infant's serum are not of maternal origin. Both parents and the child are of the Kell phenotype K-k+. Stool cultures made from the child yielded E. coli O 125:B15, an uncommon B-variant pathogenic coliform. Cell-free preparations made from broth cultures of this organism have strong specific inhibitory activity against IgM anti-A and anti-K, and both antigens have been identified on the bacterial cells. At age 3 months the child had made a clinical recovery, stool cultures showed no pathogenic coliforms, and anti-A and anti-K were no longer detectable in her serum. These data indicate that absorption of metabolites with A-like and K-like activity produced by a pathogenic coliform in the intestinal tract were responsible for the appearance of apparent naturally occurring anti-A and anti-K in the child's serum.
The high-incidence erythrocyte antigens Dib and Scl have been demonstrated on leukocytes, using an antibody absorption technique. Tests with separated platelets, lymphocytes and neutrophils indicate that these antigens are restricted to the phagocytic leukocytes. Studies using the same methodology do not show Lan or Coa antigens on leukocytes.
We have investigated a new source of commercial Lewis and P1 soluble blood group substances produced for use in immunohematology. Our tests show them to be potent, specific, stable and suitable for use in antibody inhibition procedures. They should make a useful contribution to antibody identification studies in hospital blood bank laboratories.
An 84-year-old woman with intestinal bleeding had marked reduction of red blood cell antigenicity in the Kell system, and a positive direct antiglobulin test caused by auto-anti-Kpb. KX antigen activity of her cell was increased, an observation which supports the belief that KX marks a precursor structure utilized in the normal Kell biosynthetic pathway. It is postulated that reduced Kell antigenicity was an acquired change that resulted from enzymatic degradation, possibly of bacterial origin.
A second example of anti-K19 has been identified in the serum of a black patient immunized by blood transfusions. The antibody was responsible for delayed hemolysis of transfused incompatible red blood cells. The patient's red blood cells are K:--19 but are otherwise of common Kell phenotype. The K19 antigen is closely associated with the Kell blood group although there is, as yet, no pedigree information to confirm that it is produced by the Kell gene. Tests on 10,757 group O blood donors have not revealed any further examples of the K:--19 phenotype.
Two examples of a "new" IgM saline-agglutinating auto-antibody are described. The antibodies bind complement, have the ability to cause in vivo hemolysis, and are most active at room temperature at a pH of about 6.5. Despite tests on more than 5,000 people, no nonreactive cell sample has been found. The reactive antigen is not denatured by neuraminidase, papain, or ficin, and is present on i adult red blood cells. The antibodies appear to be slightly inhibited by human saliva and milk, and more convincingly inhibited by urine from Sd(a+) persons. They are not inhibited by urine from Sd(a-) persons, but are strongly inhibited by guinea pig urine. The serologic characteristics indicate a relationship to the Sda blood group and the auto-antibody has been named antiSdx. Sdx antigen is present on red blood cells from some higher primates and is absent from rabbit, rhesus monkey, dog and sheep cells.
Red blood cells stored in saline solution for two weeks at 12 C lose some of their Fya, Fyb, and Fy3 antigenicity. At the same time substances with specific inhibitory activity against appropriate Duffy antibodies appear in the saline. Similar changes could not be recognized in time-expired commercial reagent red blood cell samples.
A case of hemolytic disease in a newborn infant caused by anti-Dia is described. The parents are Japanese. The antibody was an IgG of subclasses IgG1 and IgG3, did not bind complement, and gave a 27 percent phagocytosis rate when used to sensitize red blood cells for a macrophage binding assay. The antibody was not detected during antenatal serologic testing. This case suggests the need for reagent red blood cell panels selected to match antibody specificities likely to be encountered in a particular population.
An association in inheritance of the i adult phenotype and congenital cataract in people from Japan has been reported. We found six Caucasians of i adult type from New York who do not have cataracts. The relationship recognized in Japan probably arises through close linkage between independent genes.
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Red cells from a Mexican blood donor had depressed H, IF, ID, i, Sda, Sdx, D, LW, Dib, Vel and JMH antigens. A wide range of other blood group antigens had normal activity. The unusual red cell phenotype may be caused by a membrane anomaly that alters orientation of certain cell surface components. The specificities of the depressed red cell antigens in this phenomenon differ from those affected in Melanesians with ovalocytosis or in individuals with the In(Lu) inhibitor gene.
An IgG autoantibody, named anti-Wj, reacts with all random and most selected red cell samples. It does not agglutinate cells of Lu(a-b-) type caused by the In(Lu) dominant inhibitor gene, but cells of recessive Lu(a-b-) type are reactive. These data establish that synthesis of the Wj antigen is suppressed by the In(Lu) gene, but it is not a part of the Lutheran blood group system. The Wj antigen is not well developed on fetal red cells. This example of auto anti-Wj is a non-complement-binding IgGl protein that did not appear to cause accelerated in vivo destruction of the patient's red cells.
McLeod syndrome is an X-linked condition in which individuals of McLeod blood group phenotype have weak Kell antigens, acanthocytic red cells, and a muscular disorder. We now report a family in which two brothers have McLeod syndrome. One is K:-1, while the other is the first known K:1 person with McLeod syndrome. The K1 gene in the latter is expressed weakly and was inherited from the father, in whom it is expressed normally. The brothers have the same clinical and laboratory manifestations of McLeod syndrome but have different Kell genes. Therefore, the Kell gene is unlikely to have any positive input into development of McLeod syndrome; its role is one of passive involvement in which its expression is modified.
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A healthy 38-year-old white woman had two abortions and three live children. Red cells from each of her living children at birth had a strongly positive direct antiglobulin test. Detailed studies on the third child showed that the cells were sensitized by IgG. Maternal serum, tested by a range of techniques against reagent red cells and the husband's cells, showed no unusual antibody. Maternal serum and eluates prepared from red cells of the third child did not react with fresh cells from the older siblings (aged 7 and 10 years). Follow-up on the third child showed that the direct antiglobulin test was positive at 2 months, weakly positive at 4 months, and negative at 8 months. Red cells collected at 8 months of age did not react with the stored eluate prepared from the baby's sensitized red cells at birth. The most likely explanation of these data is that the children inherited a paternal antigen that is only present as a red cell surface-active structure during fetal development.
Kell blood-group-active protein has been isolated by labeling red cell surface proteins with 125I, sensitizing intact cells with anti-K1, anti-K2, anti-K7, or anti-K22, solubilizing the cell membranes, isolating immune complexes, and separating their components by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Each antibody separated a protein of approximately 93,000 daltons. Periodic-acid Schiff (PAS) staining of Kell protein showed that it was glycosylated. When separated under non-reducing conditions, Kell protein had different SDS-PAGE characteristics with protein bands of approximately 85,000 daltons and 115,000 daltons. This suggests that in the red cell membrane Kell protein is complexed with other proteins. Quantitative experiments made with anti-K7, anti-K22, and a mixture of anti-K7 and anti-K22 indicate that both antigen specificities are present in the same molecule. These biochemical data support serological studies which indicate that K22 is part of the Kell system.
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