scholarly journals INTERRELATIONSHIP BETWEEN THE Rh SYSTEM AND THE A B SYSTEM

Blood ◽  
1948 ◽  
Vol 3 (Special_Issue_Number_2) ◽  
pp. 66-79 ◽  
Author(s):  
ERNEST WITEBSKY ◽  
MRS. LIVIA BLUM ◽  
MISS DORIS HOWLES ◽  
MISS HELEN WARD

Abstract The isoantibodies anti-A and anti-B which are described differ in several respects from those occurring in normal human serum. This type of antibody has first been observed in the serum of an Rh negative woman who exhibited a history of erythroblastosis. Her husband belonged to the subtype Rh1 and to the blood group A. The patient’s serum completely neutralized with A and B substances still agglutinated strongly the husband’s cells provided normal human serum replaced physiological saline solution as a diluent for all dilutions. The impression was thus created that an Rh blocking antibody was responsible for the agglutination observed. It could be shown, however, that the abnormal antibody present in this patient’s serum was not an Rh antibody at all but instead, an antibody directed against the A property. This type of anti-A antibody resembles the Rh blocking antibody in many respects. It becomes manifest only if undiluted human serum is used as a diluent. Surprisingly enough this antibody agglutinated cells of group A, although the amount of AB substances added to the serum was sufficient to neutralize completely the isoagglutinin anti-A under normal conditions in which saline solution is used as a diluent. This anti-A antibody therefore cannot be neutralized as easily as the normal isoagglutinin anti-A. For its neutralization much larger amounts of the blood group specific substances are apparently necessary. The patient’s serum fixed complement when mixed with material containing water soluble A substance, in contrast to the normal isoantibody anti-A which failed to do so. The titer of isoantibodies found in the patient’s serum upon titration in saline solution was not extensively high and, as a matter of fact, was average. It is therefore felt that an extremely high titer is neither a necessary requirement nor proof of isoimmunization toward the A and B factors. Another interesting characteristic of the peculiar anti-A antibody occurring in our patient’s serum was the fact that it was essentially an anti-A1 antibody. The difference in agglutination between A1 and A2 cells respectively becomes manifest if normal serum is used as a diluent instead of saline solution. This difference becomes even more marked after neutralization of the patient’s serum with A and B substances. During the course of Mrs. Bong’s pregnancy the special anti-A antibody described did not increase but rather decreased in strength. However, even after delivery the antibody was demonstrable for at least several weeks although we had no opportunity to examine the patient’s serum further. That one must be very careful in contributing any pathological significance to isoantibodies anti-A or anti-B, even of the type described, is evident from the fact that the patient was delivered of a perfectly normal baby belonging to the blood group O and being Rh negative. Whether the difficulties experienced by the patient in previous pregnancies were due to sensitization toward the Rh factor or to the A factor cannot be decided. Antibodies anti-A and anti-B of the type reported were also found in the sera of patients who had received large amounts of pooled plasma or O blood conditioned with A and B specific substances. Again the anti-A antibody occurring in the serum of these patients was mainly directed against the A1 property. Under the experimental conditions described in this paper, such a serum can be used for the differential diagnosis of the subgroups A1 and A2 and constitutes a sensitive reagent for the recognition of the differences occurring within the A factor. With the aid of such a serum only 10 per cent of A cells were found to belong to subgroup A2, 75 per cent to A1, and 15 per cent were considered to be of the intermediate type. No subgroups were found so far in human cells of group B.

Blood ◽  
1999 ◽  
Vol 93 (12) ◽  
pp. 4418-4424 ◽  
Author(s):  
Sergio H. Spalter ◽  
Srini V. Kaveri ◽  
Emmanuelle Bonnin ◽  
Jean-Claude Mani ◽  
Jean-Pierre Cartron ◽  
...  

Abstract It is widely accepted that the serum of healthy individuals contains natural antibodies only against those blood group A or B antigens that are not expressed on the individual’s red blood cells. The mechanisms involved in tolerance to autologous blood group antigens remain unclear. In the present study, we show that IgM and IgG antibodies reactive with autologous blood group antigens are present in the immunoglobulin fraction of normal human serum. Natural IgG anti-A antibodies purified by affinity chromatography from IgG of individuals of blood group A exhibited an affinity for A trisaccharide antigen in the micromolar range and agglutinated A red cells at sixfold higher concentrations than those required for agglutination with affinity-purified anti-A IgG of individuals of blood group B. Whereas autoantibodies reactive with self A and B antigens are readily detected in purified IgG and IgM fractions, their expression is restricted in whole serum as a result of complementary interactions between variable regions of antibodies. These observations suggest that tolerance to autologous ABO blood group antigens is dependent on peripheral control of antibody autoreactivity.


Blood ◽  
1999 ◽  
Vol 93 (12) ◽  
pp. 4418-4424 ◽  
Author(s):  
Sergio H. Spalter ◽  
Srini V. Kaveri ◽  
Emmanuelle Bonnin ◽  
Jean-Claude Mani ◽  
Jean-Pierre Cartron ◽  
...  

It is widely accepted that the serum of healthy individuals contains natural antibodies only against those blood group A or B antigens that are not expressed on the individual’s red blood cells. The mechanisms involved in tolerance to autologous blood group antigens remain unclear. In the present study, we show that IgM and IgG antibodies reactive with autologous blood group antigens are present in the immunoglobulin fraction of normal human serum. Natural IgG anti-A antibodies purified by affinity chromatography from IgG of individuals of blood group A exhibited an affinity for A trisaccharide antigen in the micromolar range and agglutinated A red cells at sixfold higher concentrations than those required for agglutination with affinity-purified anti-A IgG of individuals of blood group B. Whereas autoantibodies reactive with self A and B antigens are readily detected in purified IgG and IgM fractions, their expression is restricted in whole serum as a result of complementary interactions between variable regions of antibodies. These observations suggest that tolerance to autologous ABO blood group antigens is dependent on peripheral control of antibody autoreactivity.


2001 ◽  
Vol 69 (6) ◽  
pp. 3597-3604 ◽  
Author(s):  
Charlene M. Kahler ◽  
Larry E. Martin ◽  
Yih-Ling Tzeng ◽  
Yoon K. Miller ◽  
Kerith Sharkey ◽  
...  

ABSTRACT We have located a locus, pgl, in Neisseria meningitidis strain NMB required for the glycosylation of class II pili. Between five and eight open reading frames (ORFs) (pglF, pglB, pglC, pglB2, orf2, orf3, orf8, and avtA) were present in the pgl clusters of different meningococcal isolates. The Class I pilus-expressing strains Neisseria gonorrhoeae MS11 and N. meningitidis MC58 each contain a pgl cluster in which orf2 andorf3 have been deleted. Strain NMB and other meningococcal isolates which express class II type IV pili contained pglclusters in which pglB had been replaced bypglB2 and an additional novel ORF, orf8, had been inserted between pglB2 and pglC. Insertional inactivation of the eight ORFs of the pglcluster of strain NMB showed that pglF, pglB2, pglC, andpglD, but not orf2, orf3, orf8, andavtA, were necessary for pilin glycosylation. Pilin glycosylation was not essential for resistance to normal human serum, as pglF and pglD mutants retained wild-type levels of serum resistance. Although pglB2 andpglC mutants were significantly sensitive to normal human serum under the experimental conditions used, subsequent examination of the encapsulation phenotypes revealed that pglB2 andpglC mutants expressed almost 50% less capsule than wild-type NMB. A mutation in orf3, which did not affect pilin glycosylation, also resulted in a 10% reduction in capsule expression and a moderately serum sensitive phenotype. On the basis of these results we suggest that pilin glycosylation may proceed via a lipid-linked oligosaccharide intermediate and that blockages in this pathway may interfere with capsular transport or assembly.


1921 ◽  
Vol 34 (2) ◽  
pp. 201-205 ◽  
Author(s):  
Frederick T. Lord ◽  
Robert N. Nye

The purulent sputum obtained during life and the exudate at autopsy from the later stages of lobar pneumonia commonly erode the surface of Löoffler's blood serum. Cellular material obtained from the pneumonic lung in an early stage of lobar pneumonia failed to erode the surface until washed with normal saline solution. Mixtures of washed pneumonic cellular material and normal human serum fail to erode Löffler's blood serum when the amount of cellular material is less than one part of cells to approximately three parts of serum. Erosion occurs when the cellular material exceeds this amount in the ratio.


Blood ◽  
1950 ◽  
Vol 5 (6) ◽  
pp. 553-567 ◽  
Author(s):  
DONALD M. ERVIN ◽  
RICHARD M. CHRISTIAN ◽  
LAWRENCE E. YOUNG

Abstract 1. Severe hemolytic reactions were observed in 3 group A (subgroup A1) recipients transfused with group O whole blood or plasma. In one case, 10 ml. of a commerical preparation of soluble A and B factors had been added to 500 ml. of whole blood prior to the transfusion and it is believed that the reaction might have been even more serious had not this material been added. 2. The anti-A antibodies in the serum of the dangerous universal donors causing the hemolytic reactions fixed complement, acted as hemolysins, were difficult to neutralize with soluble A and B factors, were capable of giving positive Coombs tests and their ability to agglutinate A cells was enhanced by the presence of normal human serum. These characteristics were similar to those observed in serum from donors known to be actively immunized against the A factor, but the stimulus for development of "immune" anti-A antibodies in the dangerous group O donors was not apparent. 3. Small amounts of immune A antibody were consistently demonstrated in 12 of 100 random group O sera which, after neutralization, produced indirect Coombs tests with A1 cells and agglutinated A1 cells suspended in compatible normal human serum. 4. Screening procedures for elimination of dangerous group O donors are discussed.


1982 ◽  
Vol 28 (1) ◽  
pp. 119-121 ◽  
Author(s):  
E Piall ◽  
G W Aherne ◽  
V Marks

Abstract We evaluated a commercially available (Diagnostic Biochemistry Inc.) doxorubicin 125I radioimmunoassay kit. This kit gave a high apparent doxorubicin concentration (greater than 12 micrograms/L), which was not linearly related to dilution, for two pools of normal human serum and plasma and also for samples collected from patients before they received the drug. In contrast, a doxorubicin 3H radioimmunoassay developed by us gave a low blank (2 micrograms/L), which was linearly related to dilution, for the same pools and patients' samples. Doxorubicin concentrations in the plasma of patients receiving the drug were compared by the two methods; the kit gave results five- to 10-fold those obtained with our assay. High nonspecific interference by serum and plasma as measured by the 125I radioimmunoassay must therefore be borne in mind by users of the kit, and we suggest that results should be corrected for these nonspecific effects.


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