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)

In an attempt to qualitatively identify the membrane antigen (MA) complex induced by Epstein-Barr virus (EBV) infection of lymphoblastoid cells, superinfected Raji cells were surface labelled with 125I by the lactoperoxidase method and solubilized with Triton X-100, then the 125I-labelled membrane proteins were precipitated by sera containing high antibody titers to MA. Analysis of these immune precipitates on sodium dodecyl sulfate polyacrylamide gel eletrophoresis identified four major EBV-specific membrane proteins with molecular weights (mol. wt) of 280,000, 250,000, 170,000 and 90,000. Sera from patients with Burkitt's lymphoma (BL), nasopharyngeal carcinoma (NPC) and infectious mononucleosis (IM) and from EBV-infected disease-free individuals showed differential patterns of reactivity to these antigens with some sera only recognizing three or less of the antigens. The results from invesigations with these sera also indicated that these major proteins were not related to EBV-induced viral capsid antigens (VCA) or the virus-associated early antigen (EA) complexes as defined by immunofluorescence. Metabolic labelling of EBV-infected Raji cells with [14C]glucosamine, followed by Triton X-100 solubilization and radioimmune precipitation, identified the 280,000, 250,000 and 90,000 components as glycoproteins. The lactoperoxidase-labelled 170,000 molecular weight component was not significantly glycosylated and, therefore, could not be categorized as a glycoprotein on the basis of this study. In addition, a glycoprotein with a mol. wt of 130,000 was identified by this approach which also appeared to be specified by EBV. The results from these investigations, therefore, indicated that the EBV-induced MA complex was composed of four major glycoproteins and one nonglycosylated high mol. wt protein.
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PMID:Epstein-Barr virus-induced membrane antigens: immunochemical characterization of Triton X-100 solubilized viral membrane antigens from EBV-superinfected Raji cells. 8 99

The coated-tube method of solid-phase radioimmunoassay has been adapted to the detection of heterophile antibodies and antigens of infectious mononucleosis. Disposable plastic hemagglutination trays were coated with purified glycoprotein from horse erythrocytes and the subsequent uptake of antibody from test sera was detected by radio-iodinated horse erythrocyte glycoprotein. In a preliminary survey of sera from patients with infectious mononucleosis and sera from controls, the assay proved highly sensitive and specific. The test system was also useful in a competitive binding assay for immunochemical studies of glycoproteins from other heterophile antigen-positive species.
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PMID:Immunochemical studies of infectious mononucleosis. VI. a radioimmunoassay for the detection of infectious mononucleosis heterophile antibody and antigen. 29 65

The heterophile antigen (Paul-Bunnell antigen, PBA) of infectious mononucleosis was isolated by extraction of an aqueous suspension of bovine erythrocyte stromata with chloroform-methanol (2:1). The upper aqueous layer contained gangliosides, PBA, and a high-molecular-weight glycoprotein. PBA and gangliosides were separated from the high-molecular-weight glycoprotein by extraction of lyophilized upper layer with chloroform-methanol solvents. Separation of PBA from gangliosides was carried out by chromatography on DEAE-cellulose with chloroform-methanol solvents. PBA appeared to be a minor glycoprotein component of the erythrocyte membrane and had both hydrophobic and hydrophilic properties. It was soluble in either organic or aqueous solvents. On SDS-polyacrylamide gel electrophoresis, it migrated as a single component that stained for protein with Coomassie blue, for carbohydrate with periodic acid-Schiff reagent, and for lipid with oil red 0; it had an apparent molecular weight of 26,000. It was composed of 62% protein with major amino acids; glutamic acid, proline, glycine, isoleucine, leucine, and threonine (158, 116, 98, 90, 85, and 82 residues per 1,000 residues, respectively). Carbohydrate content was 9.2% with major sugar constituents: sialic acid, galactosamine, and galactose. Serologic activity of PBA was destroyed by pronase but not by trypsin.
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PMID:Isolation and partial characterization of the heterophile antigen of infectious mononucleosis from bovine erythrocytes. 40 89

The major sialoglycopeptide released from bovine erythrocytes by papain has been purified and characterized. The glycopeptide contains 82% by weight carbohydrate in molar ratios of galactose - 5.5:N-acetylglucosamine - 3.6:sialic acid - 2.6:N-acetylgalactosamine - 1.0. The carbohydrate and amino acid composition is quite different from the glycoprotein extracted from bovine erythrocyte stroma with hot 75% ethanol. The glycopeptide is devoid of reactivity with Paul-Bunnell heterophile antibody of infectious mononucleosis - an activity expressed to high degree on the bovine erythrocyte and associated with glycoprotein. The glycopeptide does react, however, with another antibody found in infectious mononucleosis as well as most normal human sera tested.
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PMID:Immunochemical studies of infectious mononucleosis. VII. Isolation and partial characterization of a glycopeptide from bovine erythrocytes. 89 34

A glycoprotein was isolated from goat erythrocyte membranes by extraction with hot 75% ethanol. The glycoprotein was purified by ethanol precipitation, phosphocellulose chromatography gel filtration, ethyl:ether and chloroform:methanol extraction. In aqueous phosphate-buffered saline, pH 7, the glycoprotein was in an aggregated state with a sedimentation coefficient (S(obs)) to 1.5. Electrophoresis of the glycoprotein on polyacrylamide gels containing phosphate-buffered 0.1% SDS gave a single band, staining with both periodic acid Schiff (PAS) and Coomassie Blue (CB). The apparent m.w., calculated from retardation coefficient, was 25,000. Electrophoresis of the glycoprotein on 1% SDS gels buffered with Tris-acetate (pH 7.4) showed a major band of similar (23,500) apparent m.w. plus four other PAS- and CB-staining bands of lower mobility. With 131I-labeled glycoprotein, recovery of bands from gels, sialic acid analysis, heterophile antigen activity, and re-electrophoresis, it was shown that these additional bands were aggregated forms of a single or closely related glycoprotein species. The purified glycoprotein contained 50% carbohydrate with molar ratios of sialic acid:galactose:mannose:galactosamine:glucosamine of 3.1:2.1:0.1:1.6:1. The glycoprotein was highly reactive with the Paul-Bunnell heterophile antibody in the sera of patients with infectious mononucleosis, with Limulus polyphemus lectin and weakly ractive with wheat germ agglutinin. These reactivities were destroyed by neuraminidase treatment or by alkaline sodium borohydride. The native glycoprotein did not react with lectins from Canavalia enisformis, Phaseolus vulgaris, Ricinus communis, or Vicia graminea although it was reactive with the latter two after neuraminidase treatment.
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PMID:Immunochemical studies of infectious mononucleosis. V. Isolation and characterization of a glycoprotein from goat erythrocyte membranes. 95 50

A method is described for the isolation and purification of infectious mononucleosis receptor (IMR) in high yield from sheep erythrocyte stroma. The procedure involves extraction of the stroma successively with boiling acetone, 100, 75 and 50% ethanol which removes approximately 40% non-infectious mononucleosis-active material. Subsequent phenol/buffered saline extraction of the residue from the organic extraction yields a highly active IMR preparation in the aqueous phases. This material was further purified by ethanol precipitation and gel filtration chromatography. The yield was 0.2% of the stroma. Approximately 0.1 mug/ml of the purified IMR inhibits 4 agglutinating units of infectious mononucleosis (IM) serum. The material is a glycoprotein containing N-acetyl- and N-glycolylneuraminic acids, hexose, hexosamine and approximately 46% protein. It gives one band in immunoelectrophoresis with IM serum and loses IM specificity upon treatment with neuraminidase.
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PMID:Preparation of an infectious mononucleosis receptor from sheep erythrocyte stroma. 100 12

The major glycoproteins of horse and swine erythrocyte membranes were isolated and examined chemically and immunologically. The major glycoprotein of horse erythrocyte membranes had a molecular weight of 33 000 and consisted of 46.2% protein and 53.8% carbohydrate, of which 9.4% was hexose, 10.1% hexosamine and 33.7% sialic acid. This glycoprotein was associated with activity for the infectious mononucleosis heterophile antigen. There were two different major glycoproteins in swine erythrocyte membranes. One major glycoprotein had a molecular weight of 46 200 and consisted of 34.2% protein and 65.8% carbohydrate, of which 18% was hexose, 19% hexosamine and 27.2% sialic acid. This glycoprotein had phytohemagglutinin (Phaseolus vulgaris) binding activity. The other glycoprotein had a molecular weight of 29 000 and consisted of 50.4% protein and 49.6% carbohydrate, of which 6.4% was hexose, 7.0% hexosamine and 36.3% sialic acid. This glycoprotein had weak or absent phytohemagglutinin binding activity.
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PMID:Isolation and partial characterization of the major glycoproteins of horse and swine erythrocyte membranes. 123 14

The Epstein-Barr Virus (EBV) causes infectious mononucleosis, and has been strongly associated with certain human cancers. The virus is thought to exclusively bind to B lymphocytes and epithelial cells via receptors (CR2/CD21) that also interact with fragments of the third component of complement (C3). Recent evidence, however, has challenged this belief. We have used two-color immunofluorescence analysis using biotin-conjugated EBV and streptavidin-phycoerythrin along with fluorescein-conjugated anti-T cell antibodies and demonstrated that CD1-positive, CD3-dull (immature) human thymocytes express functional EBV receptors. In four replicate experiments, the binding of EBV to thymocytes ranged between 8 and 18%. This interaction is specific as evidenced by inhibition with nonconjugated virus, anti-CR2 antibodies, aggregated C3, and an antibody to the gp350 viral glycoprotein that the virus uses to bind to CR2. EBV can infect the thymocytes as evaluated by the presence of episomal EBV-DNA in thymocytes that had been incubated with the virus as short as 12 days or as long as 6 weeks. Episomal DNA analysis was performed by Southern blotting with a EBV-DNA probe that hybridizes to the first internal reiteration of the viral DNA. The presence of the EBV genome is also supported by the detection of EBV nuclear antigen 1 in infected thymocytes, assessed by Western blotting with EBV-immune sera. The EBV infection is specific as determined by blocking experiments using anti-CR2 and anti-gp350 antibodies. Finally, virus infection of thymocytes can act synergistically along with interleukin 2 and induce a lymphokine-dependent cellular proliferation. In view of previously reported cases of EBV-positive human T cell lymphomas, the possibility is raised that EBV may be involved in cancers of T lymphocytes that have not been previously appreciated.
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PMID:Infection of human thymocytes by Epstein-Barr virus. 170 54

The soluble form of the CD30 antigen (sCD30), an 88-kd glycoprotein that is released by Hodgkin's-derived cell lines in vitro, can be detected in patients with Hodgkin's lymphoma, adult (HTLV-1+) T-cell leukemia, rare cases of non-Hodgkin's lymphoma, and acute infectious mononucleosis (anti-EBV-IgM+). In a prospective study of 90 consecutive untreated patients with newly diagnosed Hodgkin's disease who were treated according to the protocols of the German Hodgkin Study group, 22% had detectable levels of sCD30 in their serum. sCD30 was only detected in patients with B symptoms (20 of 44 or 45%), and maximum sCD30 levels (88 U/mL) were found in stage IVB. Of 87 patients evaluable for response, sCD30+ patients had significantly lower rates of complete remission (9 of 20 or 45% v 60 of 67 or 90%; P less than .001) and higher rates of progressive disease (9 of 20 or 45% v 6 of 67 or 9%; P less than .001) than CD30+ patients. Similarly, freedom from treatment failure curves were significantly worse for CD30+ patients (P = .0003). sCD30 disappeared after successful treatment, but increased in patients with progressive disease. It was never detected in patients in complete remission or in healthy controls. We conclude that sCD30 is a valuable marker for disease activity and has prognostic significance in Hodgkin's disease.
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PMID:Clinical significance of soluble CD30 antigen in the sera of patients with untreated Hodgkin's disease. 185 Mar 8

Human antibody responses to the Epstein-Barr virus (EBV) glycoprotein gp340 have been measured using purified preparations of the native molecule as the substrate in ELISAs. This glycoprotein is the dominant component of the EBV envelope and a major target for the virus-neutralizing antibody response. Healthy virus carriers (both Caucasian and Chinese) regularly show detectable anti-gp340 IgG in serum and, unexpectedly, 21-30% of these individuals are also serum anti-gp340 IgA positive. Chinese patients with the EBV-genome-positive malignancy nasopharyngeal carcinoma (NPC) show elevated serum IgA antibodies to gp340 but, given the background of responses amongst healthy virus carriers, anti-gp340 IgA titres are a poorer diagnostic indicator of NPC than serum IgA antibodies detectable by immunofluorescence against the multicomponent EBV early antigen (EA). Salivary IgA antibody responses to gp340 are potentially important as a means of neutralizing orally-transmitted virus. We detected salivary IgA (but not IgG) to gp340 in a minority (12-19%) of healthy virus carriers and in a higher proportion (49%) of NPC patients. Even saliva samples chosen for their relatively high anti-gp340 IgA titres showed only weak neutralizing activity against transforming EBV preparations whether from B95.8 cell culture supernatant or from the throat washing of an infectious mononucleosis patient. We conclude that in healthy virus carriers, salivary IgA responses to gp340 are unlikely to provide effective local immunity against re-infection with a second EBV strain.
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PMID:Salivary and serum IgA antibodies to the Epstein-Barr virus glycoprotein gp340: incidence and potential for virus neutralization. 185 Mar 82


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