Mary H. McGinniss

Febrile, Nonhemolytic Transfusion Reactions and the Limited Role of Leukoagglutinins in Their Etiology

In more than ten thousand transfusions given over a four‐year period to 1,649 patients, the incidence of urticarial reactions was 1.1 per cent. There were no hemolytic transfusion reactions and none due to bacterial contamination or to bacterial pyrogens. There were 276 “Febrile Nonhemolytic” reactions for an incidence of 2.5 per cent.

Thrombocytopenia with Sodium Cephalothin Therapy

Abstract Thrombocytopenia occurred on two separate occasions in a patient while she was receiving sodium cephalothin. After recovery, a test dose of cephalothin (1 g) produced a 50% drop in the pla...

Two monoclonal antibodies highly specific for the blood group N determinant

Two monoclonal IgM antibodies, 179K and 35/5F, obtained following immunization of mice with A2,MN or O,MN human erythrocytes, agglutinate NN and MN red cells strongly, and MM erythrocytes weakly. As shown by hemagglutination inhibition and solid phase ELISA, both antibodies are highly specific for the blood group N determinant. They react with N glycoprotein, its amino-terminal glycopeptides and with Ss glycoprotein (glycophorin B), which carries the blood group N determinant. They fail to react with M glycoprotein, M glycoprotein-derived glycopeptides, or with internal glycopeptides derived from N glycoprotein. Reaction of the antibodies with N glycoprotein is abolished by desialylation, periodate oxidation/borohydride reduction, orN-acetylation of the glycoprotein. Thus, the antibodies are specific for an epitope which includes sialylated oligosaccharide chain(s) and is located in the region of the amino-terminal leucine residue of N glycoprotein. MMU− erythrocytes, lacking both blood group N and Ss glycophorin are non-reactive. Agglutination of MMU+ erythrocytes by the anti-N antibodies occursvia interaction with glycophorin B and correlates with the Ss phenotype of red cells MM,S erythrocytes are usually more strongly, agglutinated than MM,ss cells. The agglutination of MM erythrocytes decreases markedly as the pH is increased from 6 to 8, while agglutination of NN red cells is much less affected by shifts in pH over this range. As a result, both monoclonal antibodies are highly anti-N specific typing reagents when the agglutination assay is carried out at pH 8.

Immune cross-reactivity of penicillin and cephalothin.

WE recently described positive direct Coombs tests in patients receiving sodium cephalothin1. Because most normal sera caused the in vitro agglutination of red cells coated with cephalothin, we concluded that some of the positive direct Coombs tests must be related to non-immune binding of a serum protein–cephalothin complex to the red cell surface. We also suggested the possibility that some of these test sera contained anti-penicillin agglutinins.

Mechanism of the albumin agglutination phenomenon.

Summary. The albumin agglutination phenomenon is due to antibodies which cause agglutination of all human red cells when these cells are suspended in an albumin medium. Two sera with this property were studied. We suggest that the reaction is due to non‐specific adsorption of antigen‐antibody complex onto red cells. The antibody is a gamma globulin directed at albumin which has been altered by the addition of acetyl tryptophanate or caprylate. These chemicals are added as stabilizers in the manufacture of albumin to prevent denaturation when the albumin is heated.

Expression of red cell antigens by K562 human leukemia cells before and after induction of hemoglobin synthesis by hemin.

We studied the red cell antigens present on K562 human leukemia cells before and after induction of hemoglobin synthesis by hemin. The fetal antigens i, IF, and IT were detected on uninduced cells. While expression of both i and IT antigens increased after hemin induction, expression of IT was closely related to fetal hemoglobin synthesis as determined in experiments in which the induction was reversed. The EnaFR, NVg, and T antigens of glycophorin A were also present on uninduced cells. In contrast, the M and Pra antigens of glycophorin A, the Kell system antigens, and the P1 antigen became detectable only after hemin induction. Antigens of other major red cell systems were not detected.

Further Evidence for the Serologic Association of the O (H) and I Blood Groups

Summary. Natural occurring agglutinins in eel sera display a spectrum of specificities against O (H) and I determinants: anti‐O, anti‐H, anti‐OI, anti‐HI, anti‐IO and anti‐I. These findings suggest that the H and I determinants are probably in close proximity to each other resulting in various degrees of specificity at the antibody combining site.

DIFFERENCES BETWEEN ANTI-H AND ANTI-OI RED CELL ANTIBODIES.

Both anti-0 and anti-H reagents preferentially agglutinate human group 0 red cells. When this activity is inhibited by H substance (secretor saliva) the serum is said t o contain anti-H; conversely, if not inhibited the serum is said to be anti-0 [7]. The recognition of anti-0 as separate from anti-H sera is of considerable theoretical importance in the search for the determinants of blood group specificity. Also, we have commented on this difference as being of practical importance in blood transfusion [4]. There is evidence that anti-0 destroys group 0 red cells in vivo and anti-H does not. The I blood group system has bearing on specificity in the ABO system. GOLD has described parallels between anti-0, anti-A,, and anti-I [2]. We have examined the relationship between anti-H and anti-I and contrasted this with anti-0 by serologic and in vivo compatibility studies.

Duffy phenotypes in Malaysian populations: correction of previous unusual findings

Duffy phenotypes were determined for 314 Malaysian Orang Asli. The most common gene, Fya, was present in 313; there were no Duffy negative individuals. A previous study found evidence of Plasmodium vivax infection in 5 of 7 Orang Asli reported to be of the Duffy negative genotype. In this study, 5 of the 7 previously tested Orang Asli were retested in triplicate, and each of the 5 was found to be Duffy positive, having the Fya gene and a phenotype of Fy (a + b-).

An erythrocyte Pr auto‐antibody with sialoglycoprotein specificity in a patient with purine nucleoside phosphorylase deficiency

A warm auto‐antibody with specificity in the Pr blood group system was demonstrated in the serum and red cell eluate of a patient with purine nucleoside phosphorylase (NP) deficiency. The antibody reacted with all cells tested except En(a‐) red cells which lack glycophorin A, the major erythrocyte sialoglycoprotein. However, anti‐Ena was ruled out by absorption of the antibody with En(a‐) red cells. The antibody demonstrated similar serologic characteristics to Pra antibodies, except that those previously described were inactive with protease‐ treated red cells, while in this case, reactivity was destroyed by papain and ficin but maintained in the presence of trypsin. Inhibition analysis with purified glycoprotein fragments localized the predominant reactive antigen on the MN sialoglycoprotein between amino acid residues 40 and 61. Serologic tests demonstrated its presence in decreased amount on at least one other erythrocyte membrane structure. The serum from another patient with NP deficiency contained an autoantibody similar to the one described here. It may be of interest to explore the association of auto‐antibodies to erythrocyte sialoglycoprotein antigens in NP and other immune deficiency states.