Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0021345 (infectious mononucleosis)
 3,358 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Infectious mononucleosis may occasionally be complicated by purpura, but the mechanism of the thrombocytopenia is not known in detail. In the present study, 3 children with mononucleosis-associated purpura were found to have marked elevations of platelet-associated immunoglobulins and circulating platelet binding IgG and IgM. Employing electrophoretically (SDS-PAGE) separated normal platelet membrane proteins in an immunoblot assay, serum IgG and IgM antibodies were found to be directed to antigenic determinants situated on glycoprotein GP IIb (140 kDa) in all patients, but also on smaller proteins of molecular weights between 30 and 52 kDa. 24 control sera were negative. Positive reactions were eliminated after absorption of sera with fresh platelets. These results demonstrate autoantibodies to platelet surface membrane proteins in infectious mononucleosis-induced purpura and suggest a transient autoantibody-mediated platelet destruction as the cause of thrombocytopenia in these patients.
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PMID:Antibodies to platelet membrane glycoprotein antigens in three cases of infectious mononucleosis-induced thrombocytopenic purpura. 276 40

A vaccine derived from the high-molecular-weight glycoprotein (gp340) component of the Epstein-Barr (EB) virus membrane antigen conferred complete protection against a 100% lymphomagenic dose of EB virus in the cottontop tamarin, the animal of choice for experiments with EB virus. The membrane-antigen gene has already been cloned, and the development of a vaccine for use in man should now be possible. Such a vaccine could be tested first against infectious mononucleosis, because the effectiveness of vaccination would become evident in a relatively short time. Field trials against Burkitt's lymphoma and nasopharyngeal cancer could follow.
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PMID:Vaccination against Epstein-Barr virus: current progress and future strategies. 287 25

An enzyme immunoassay (EIA) was developed for the detection of heterophile, Hanganutziu-Deicher (H-D) antibodies in sera of patients with infectious mononucleosis (IM) and various other diseases. The EIA with a high m.w. glycoprotein (HMWGP) isolated from bovine erythrocyte stromata was shown to detect H-D antibodies directly, in spite of higher titers of Paul-Bunnell (P-B) antibodies in the IM sera. Absorption and inhibition studies of IM sera demonstrated H-D specificity of the antibodies combining with HMWGP in the EIA. The H-D antibodies were found in sera of 56% Caucasians and 27% of Japanese suffering from IM. The vast majority of the H-D antibodies in IM sera was of IgM class. Sera of patients with various other diseases also gave positive results: rheumatoid arthritis, 22%; syphilis, 19%; cancer of the gastrointestinal tract, 13%; and lepromatous leprosy 9.7%. The incidence of positive results in control sera from apparently healthy subjects was less than 4%. Results of this study confirmed our previous observation that whereas P-B antigens appear in immunogenic form in only IM, the H-D antigen is expressed as an immunogen in various diseases including IM.
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PMID:Hanganutziu-Deicher antibodies in infectious mononucleosis and other diseases. 618 36

A glycoprotein was isolated from bovine erythrocytes which has 20% carbohydrate and migrates on sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a single band. This glycoprotein carries the reactivity of bovine erythrocytes with Paul-Bunnell heterophile antibody of infectious mononucleosis. This bovine glycoprotein was coupled to carboxyl-modified latex particles with water-soluble carbodiimide. The resulting reagent was then used to develop a new test for the detection of infectious mononucleosis antibody. The bovine erythrocyte glycoprotein-latex reagent is more stable than sheep or horse erythrocytes, the traditional reagents for detection of infectious mononucleosis antibody. This new reagent is used in a direct slide test; no preabsorption of the sera is necessary. In the present study the glycoprotein-latex reagent compared favorably in terms of sensitivity and specificity with two standard tests for infectious mononucleosis antibody. Ninety-nine serum samples were tested. Agreement of the latex test with a stabilized horse erythrocyte spot test was 90%. Ten samples were weakly positive with the latex test and negative with the horse cell test. Only one of these was also positive with an enzyme-treated sheep cell test. This latter test was somewhate more sensitive than the latex test.
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PMID:Latex test for serodiagnosis of infectious mononucleosis. 624 67

Immunochemical comparisons were made of the reactivity of membrane glycoproteins from horse, bovine, sheep and goat erythrocytes with heterophile antibodies of infectious mononucleosis. The four receptors were tested as competitive inhibitors of a sandwich-type solid-phase radioimmunoassay and of agglutination of glycoprotein-latex reagents by infectious mononucleosis serum. The results of this study showed that the bovine glycoprotein had a superior reactivity with this heterophile antibody system and sheep erythrocyte glycoprotein was the least reactive. The latter had negligible ability to displace 125I-bovine glycoprotein and was a very poor inhibitor of the agglutination of a bovine glycoprotein-latex reagent by infectious mononucleosis serum. Horse and goat glycoproteins were more efficient inhibitors than sheep glycoprotein but less active than the preparation from bovine red cells. All of the inhibitory activity of sheep, horse and goat glycoproteins, and a major portion of that of the bovine glycoprotein was destroyed by neuraminidase treatment. We have termed this receptor--shared by all four species--the Paul-Bunnell receptor, since by definition Paul-Bunnell antibody is a sheep erythrocyte agglutinin which is also reactive with horse, bovine and goat erythrocytes. The neuraminidase (and alkaline borohydride) resistant receptor of bovine glycoprotein has been designated the Bo receptor because it is not common to the other three species.
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PMID:Immunochemical studies of infectious mononucleosis--XI. comparison of heterophile antibody inhibitors from the erythrocyte membranes of four mammalian species. 640 39

Mixed agglutination (MA) test with sediments of guinea pig kidney (GPK) homogenates and indicator red blood cells of bovine (BRBC) or sheep (SRBC) origin was established for detection of human heterophile antibodies. By means of MA test with BRBC indicator cells, heterophile antibodies of Hanganutziu-Deicher (H-D) specificity were demonstrated in sera of patients with syphilis (20%), lepromatous leprosy (57%), infectious mononucleosis (45%), Chediak-Higashi syndrome (73%), Kawasaki disease (58%), multiple sclerosis (58%), and leukemias (13%), as well as in sera of subjects who received injections of foreign species sera (20%). Some but not all BRBC-positive sera gave positive MA tests when SRBC were employed as indicator cells. None of 13 multiple myeloma sera tested gave positive results. The incidence of positive reactions in normal human sera was 3%. Neutralization of H-D antibodies in representative pathologic sera by purified heterophile antigens showed that the antibodies under investigation were mostly directed against antigen(s) of high molecular weight glycoprotein, but not N-glycolyl-neuraminic acid (NGNA) ganglioside fraction of BRBC.
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PMID:Mixed agglutination with guinea pig tissue sediments for detection of heterophile antibodies. 643 28

Monoclonal antibody T305, prepared by immunizing mice with the T-ALL derived cell line RPMI-8402, immunoprecipitates a single chain glycoprotein with m.w. 160,000 daltons (under reducing conditions) or 180,000 daltons (under nonreducing conditions). In immunofluorescence assays, antibody T305 reacted with a subpopulation of T cells in normal blood (22 +/- 6%), thymus (28 +/- 11%), and lymph node (24 +/- 6%). Increased frequency of T cells reactive with antibody T305 was found in peripheral blood of patients with infectious mononucleosis (greater than 80%), graft-vs-host disease after bone marrow transplantation (65 +/- 11%), acquired immunodeficiency syndrome (53 +/- 12%). The T cells in synovial fluid of patients with rheumatoid arthritis had increased frequency of antibody T305 reactive cells (59 +/- 8%) as compared to their peripheral blood (18 +/- 7%). Two color immunofluorescent studies demonstrated that the T305+ T cells predominantly co-stained with antibody Leu 2a (suppressor/cytotoxic subset) in both normals and disease state blood. After cell sorting to obtain T305+ and T305- subpopulations, we demonstrated that a) natural killer and antibody-dependent cellular cytotoxicity activity in normal blood was in the T305+ but not T305- T cells; b) cytotoxic T cells induced by mixed lymphocyte reaction were predominantly T305+; c) T305- T cells could be induced in vitro to express T305 antigen by mitogens or allogeneic B cells; d) the DNA content of T305+ and T305- T cells in normal blood was similar (greater 95% of cells with G0/G1 level); e) after mitogen stimulation, T305 antigen induction on previously T305- cells occurs before S-phase; and f) significantly more [3H]-thymidine after mitogen stimulation was incorporated by originally T305- cells than by originally T305+ cells (p less than 0.001). The T305 antigen was not restricted to T cells because it was also found on myeloid precursors in bone marrow but was not present on polymorphonuclear leukocytes, red blood cells, platelets, muscle, liver, skin, kidney, lung, or brain. Antibody T305 was found on 24/25 cases of acute leukemia (6 T-ALL, 10/11 cALL, 7 AML, and 1 AMOL) but not on 18 cases of chronic leukemia (B-CLL, T-CLL, null CLL, CML). The importance of the T305 antigen is that it is present on a high number of T cells in certain autoimmune diseases and on virtually all acute leukemia cells. Its distribution on immature and in vitro activated cells suggests that it may represent a receptor for signals related to cellular replication or differentiation.
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PMID:A novel cell surface antigen (T305) found in increased frequency on acute leukemia cells and in autoimmune disease states. 660 45

A glycoprotein from bovine erythrocyte membrane was evaluated in two immunoassays as a reagent for the serodiagnosis of infectious mononucleosis (IM). We previously reported that a partially purified preparation of this glycoprotein, when attached to latex beads, agglutinated in the presence of IM heterophile antibody. In the present study, we used a highly purified form of the glycoprotein both as an agglutinating reagent, covalently bound to latex, and in a solid-phase sandwich-type radioimmunoassay (RIA) for IM antibody detection in a larger population of patients. We tested serum samples from college students with symptoms suggestive of IM with the latex reagent (143 samples) and with the RIA (245 samples). Correlation of these two tests, both with each other and with the classical differentially absorbed, agglutination tests for Paul-Bunnell antibody in IM sera, using fresh sheep or horse cells, was excellent (greater than 97% agreement). The new tests also corresponded in most cases with a rapid, unabsorbed preserved horse erythrocyte slide test. However, in this study of 245 samples, both apparent false-positives (5 samples) and apparent false-negatives (3 samples) were observed with this slide test. In conclusion, we found that the bovine glycoprotein as a reagent can facilitate the diagnosis of IM, giving results comparable to those with erythrocyte agglutination tests on differentially absorbed sera. The advantages are ease and speed of performance (latex test), potential for automation (RIA test), stability and uniformity of the glycoprotein reagent (latex and RIA tests), and most importantly, the ability to use unabsorbed sera (latex and RIA tests).
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PMID:Serodiagnosis of infectious mononucleosis with a bovine erythrocyte glycoprotein. 663 Apr 40

A highly purified preparation of horse erythrocyte glycoprotein was prepared from an aqueous ethanolic extract of hemoglobin-free membranes. The subunit apparent mol. wt was 30,000. In aqueous solution the glycoprotein formed globular aggregates of 93 +/- 16 A diameter. The glycoprotein had a receptor for the Paul-Bunnell antibody of infectious mononucleosis which was associated with an O-glycosidically linked oligosaccharide and dependent on the presence of N-glycolylneuraminic acid. In addition the glycoprotein had a neuraminidase-sensitive receptor for human peripheral blood lymphocytes. Fifty per cent inhibition of the rosetting of sheep red cells by 4 x 10(5) lymphocytes was caused by 30 microgram of glycoprotein.
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PMID:Immunochemical studies of infectious mononucleosis--X. Characterization of a glycoprotein from horse erythrocytes which reacts with Paul-Bunnell antibody. 681 Jan 2

A glycoprotein was isolated from the membrane of the bovine erythrocyte by refluxing the acetone- and ethanol-extracted stroma residue with 75% ethanol. The glycoprotein was purified by phosphocellulose chromatography, ethanol precipitation, lipidsolvent extraction and DEAE chromatography. The glycoprotein appeared to have two serological determinants, both reactive with antibodies present in the sera of patients with infectious mononucleosis. One of the determinants is similar to the Paul-Bunnell heterophile antigen found on sheep erythrocytes. It is dependent on carbohydrate, including sialic acid residues. Another specificity, seemingly not shared by sheep erythrocytes to any great extent, is resistance to neuraminidase and to alkaline borohydride treatment and thus it may be located either on the polypeptide portion of the molecule or on an alkali-stable oligosaccharide. The purified glycoprotein comprises 73% amino acids. Carbohydrate components and their molar ratios were sialic acid (1.0): galactose (1.5): N-acetylglucosamine (1.1): N-acetylgalactosamine (0.5): mannose (0.1).
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PMID:Immunochemical studies of infectious mononucleosis. IX. Heterophile antigen associated with a glycoprotein from the bovine erythrocyte membrane. 681 86


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