Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0021051 (immunodeficiency)
 71,517 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The extent of suppression of antibody response by bursectomy (Bx) was examined as a measure of the seeding sequence of different clones from the bursa to peripheral lymphoid tissues. Chickens were bursectomized surgically 1, 4 or 7 days after hatching and immunized later with four antigens: sheep red blood cells (SRBC); Bordetella pertussis (Bp); human serum albumin (HSA); influenza virus (IV). The kinetics of the antibody responses were delayed in bursectomized birds when compared with the control groups. The following order in the degree of immunosuppression was established: Bp greater than HSA greater than SRBC greater than IV. This is discussed in relation to the 'sequential maturation' theory of ontogenesis of immunocyte differentiation. The data also stress the limitation of non-specific markers for assessing partial immunodeficiency states.
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PMID:Immunodeficiency in the chicken. I. Disparity in suppression of antibody responses to various antigens following surgical bursectomy. 16 36

Chickens inoculated orally with infectious bursal disease virus (IBDV) 1 day after hatching subsequently showed a 50% incidence of immunodeficiency but little mortality. Antibody responses against IBDV and to immunization with sheep red blood cells (SRBC) or human serum albumin (HSA) were suppressed. Serum IgG concentration was decreased while IgM occurred exclusively in its 7S monomeric form (mIgM). An allotypic marker of chicken IgM (Mla) was lacking in mIgM derived from IBDV-infected birds. The loss of Mla occurred gradually in several birds between 3 and 12 weeks after perinatal infection. Inoculation of IBDV into chickens 3 weeks after hatching resulted in 50% mortality level but little immunodeficiency. Paradoxically, the serum IgG concentration was elevated, in comparison with normal birds. Histology of the bursa showed permanent hypo- or aplasia of follicles irrespective of the age of infection. The results suggest that bursal but not peripheral B cells are targets for IBDV, and immunodeficiency results from impaired peripheral seeding of B cells in infected juvenile chickens.
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PMID:Immunodeficiency in the chicken. IV. An immunological study of infectious bursal disease. 17 36

We have recently demonstrated that human immunodeficiency virus type 1 (HIV-1) recombinant envelope glycoprotein precursor gp160 (rgp160) behaves as a mannosyl/N-acetylglucosaminyl (GlcNAc) binding protein. If such a carbohydrate-binding property were of biological relevance it should be shared by other related primate immunodeficiency viruses such as HIV-2. The present study confirms this hypothesis and extends these findings by showing that HIV-2 recombinant gp140 (rgp140) specifically interacts with three affinity matrices substituted by synthetic or natural carbohydrate structures: D-mannose-divinylsulphone-agarose, para-aminophenyl-beta-D-GlcNAc-agarose and the natural glycoprotein, bovine fetuin, also coupled to agarose. Binding of rpg140 to the matrices was inhibited by alpha-D-Man17-BSA (where BSA is bovine serum albumin), beta-D-GlcNAc47-BSA and fetuin, and by glycopeptides derived from pronase-treated porcine thyroglobulin. Glycopeptides obtained after endoglycosidase H treatment of thyroglobulin had a limited inhibitory effect, whereas beta-D-Gal17-BSA and beta-D-glucan had no effect. These results indicate that, like HIV-1 envelope glycoprotein, HIV-2 rgp140 interacts with high-mannose and with the mannosyl core of complex-type N-linked glycans, as well as with the N-acetylglucosaminyl core of oligosaccharidic structures.
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PMID:Mannosyl/N-acetyl-beta-D-glucosaminyl binding properties of the envelope glycoprotein of human immunodeficiency virus type 2. 128 Oct 21

Maleylated-human serum albumin (Mal-HSA) inhibited human immunodeficiency virus type-1 (HIV-1) infection of MT-4 cells in vitro. It was also found to inhibit the fusion between uninfected CD4+ cells (Molt-4 clone 8 cells) and HIV-1 infected cells (Molt-4/HIV-1) to form syncytia. To investigate the mechanism of the inhibition, a study was designed to determine whether Mal-HSA could bind to CD4+ cells. Mal-HSA could bind to both MT-4 cells and Molt-4 clone 8 cells with high affinity, Kd = 2.0 nM and Kd = 5.8 nM, respectively. However, Mal-HSA could neither inhibit anti CD4 antibody Leu 3a binding to Molt-4 clone 8 cells nor modulate the expression of CD4 molecules on the surface of the cells. Mal-HSA binding to Molt-4 clone 8 cells was completely inhibited by sulfated polysaccharides bearing anti-HIV activity, such as dextran sulfate, fucoidan and carrageenan. Other HIV-1 susceptible human T-cell lines, such as Molt-4, CEM-5, H-9 and HuT-78 cells, also have Mal-HSA binding sites showing a high affinity, Kd = 0.9 +/- 0.4 nM. Mal-HSA binding proteins of Molt-4 clone 8 cells were identified by ligand blotting as 155 and 220 kDa proteins. Unlike dextran sulfate, Mal-HSA could not inhibit reverse transcriptase activity of HIV-1. These results indicate that Mal-HSA inhibits HIV-1 infection and syncytia formation, and suggest that 155 and/or 220 kDa proteins of target cells are involved in HIV-1 adsorption and/or the membrane fusion between HIV-1 and target cells.
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PMID:Maleylated human serum albumin inhibits HIV-1 infection in vitro. 128 31

Catechin derivatives including (-)-epicatechin gallate (ECG), (-)-epigallocatechin gallate (EGCG), (-)-epigallocatechin (EGC) and green tea extract (GTE) were found to inhibit the activities of cloned human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT), duck hepatitis B virus replication complexes reverse transcriptase (DHBV RCs RT), herpes simplex virus 1 DNA polymerase (HSV-1 DNAP) and cow thymus DNA polymerase alpha (CT DNAP alpha). EGCG and ECG were shown to be very potent inhibitors of HIV-1 RT. According to the IC50 values for HIV-1 RT, these compounds can be ordered as EGCG 0.0066 mumol/L > ECG 0.084 mumol/L > GTE 0.1 microgram/ml > EGC 7.2 mumol/L. DHBV RCs RT was the least sensitive to these compounds. Kinetic study showed that EGCG exerts a mixed inhibition with respect to external template inducer poly (rA).oligo (dT) 12-18 and a noncompetitive inhibition with respect to substrate dTTP for HIV-1 RT. Bovine serum albumin significantly reduced the inhibitory effects of catechin analogues and GTE on HIV-1 RT. In tissue culture GTE inhibited the cytopathic effect of coxsackie B3 virus, but did not inhibit the cytopathic effects of HSV-1, HSV-2, influenza A or influenza B viruses.
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PMID:[The inhibitory effects of catechin derivatives on the activities of human immunodeficiency virus reverse transcriptase and DNA polymerases]. 128 89

Cerebrospinal fluid (CSF) analytes were evaluated in 59 human immunodeficiency virus (HIV+) individuals to assess neurological involvement. Glucose, total protein, cell counts, p24 antigen, CSF: serum albumin/IgG ratios, and oligoclonal bands were measured. Eighty percent of samples showed abnormalities in one or more analyte. In some patients samples, these abnormalities could mimic those of secondary opportunistic infection when none was present. The presence of oligoclonal banding in CSF (31 percent) and disturbances in CSF: serum albumin/IgG ratio (30 percent) were related to decreases in serum CD4+ lymphocytes. Disturbances in CSF: Serum albumin/IgG ratio were also related to severity of non-neurological HIV disease staging. Cerebrospinal fluid oligoclonal bands were distinct from that found in serum in the same subjects. Since immune complexes between immunoglobulins and enzymes are observed in these same patients, these oligoclonal bands may result in artifactually elevated enzyme results secondary to decreased clearance leading to erroneous clinical decisions. There was no significant relationship between any abnormalities and the presence of neurologic disease as established by a wide variety of other studies. It is important to recognize the limits of CSF interpretation in this patient group.
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PMID:Cerebrospinal fluid analysis in human immunodeficiency virus infection. 135 27

The activity of human immunodeficiency virus 1 (HIV-1) protease has been examined as a function of solvent composition, incubation time, and enzyme concentration at 37 degrees C in the pH 4.5-5.5 range. Glycerol and dimethyl sulfoxide inhibit the enzyme, while polyethylene glycol and bovine serum albumin activate the enzyme. When incubated at a concentration of 50-200 nM, the activity of the protease decreases irreversibly with an apparent first-order rate constant of 4-9 x 10(-3) min-1. The presence of 0.1% (w/v) polyethylene glycol or bovine serum albumin in the reaction buffer dramatically stabilizes enzyme activity. In the absence of prolonged incubation of the enzyme at submicromolar concentration, the specific activity of HIV-1 protease in buffers of either high or low ionic strength is constant over the enzyme concentration range of 0.25-5 nM, indicating that dissociation of the dimeric protease, if occurring, can only be governed by a picomolar dissociation constant. Similarly, the variation of the specific activity of HIV-2 protease over the enzyme concentration of 4-85 nM is consistent only with a dimer dissociation constant of less than 10 nM. We conclude that: 1) the assumption of a nondissociating HIV-1 protease is a valid one for kinetic studies of tight-binding inhibitors where nanomolar concentrations of the enzymes are employed; 2) stock protease solutions of submicromolar concentration in the absence of activity-stabilizing compounds may lead to erroneous kinetic data and complicate mechanistic interpretations.
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PMID:Activity and dimerization of human immunodeficiency virus protease as a function of solvent composition and enzyme concentration. 140 Mar 18

The angiotensin I-based peptide Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Glu-Glu-Ser yields angiotensin I (Ang I) and Leu-Glu-Glu-Ser upon hydrolysis by the human immunodeficiency virus type 1 (HIV-1) protease, but not by human renin. N-terminal sequencing of the reaction products showed that the HIV-1 protease cleaved exclusively at the Leu-Leu bond. The rate of Ang I formation can be measured by a radioimmunoassay, since the parent peptide has minimal cross reactivity in this assay. The rate of enzymatic hydrolysis is maximal at pH 4.5-5.0 and at an ionic strength of 1 M. At 37 degrees C, 0.1 M Na acetate buffer, pH 5.0, 1 M NaCl, 10% glycerol, 5% ethylene glycol, 1 mg/ml bovine serum albumin, and 3 mM EDTA, the reaction obeys Michaelis-Menten type kinetics with Km = 17.2 +/- 3.5 microM and kcat = 2.30 +/- 0.33 min-1. The activity assay readily quantitates as little as 0.25 nM of HIV-1 protease. The production of Ang I by the HIV-1 protease is inhibited in the presence of a HIV-1 protease inhibitor. The newly discovered substrate is relatively insensitive to human or monkey serum. Therefore, the effect of sera from 20 patients with advanced acquired immunodeficiency disease syndrome (AIDS) on Ang I production in the above assay system was examined. Results of this study indicate that it may be possible to adapt the above Ang I-based system to determine blood levels of HIV-1 protease inhibitors in AIDS patients during clinical trials.
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PMID:An ultrasensitive human immunodeficiency virus type 1 protease radioimmuno rate assay with a potential for monitoring blood levels of protease inhibitors in acquired immunodeficiency disease syndrome patients. 144 99

In 37 intravenous drug users (IVDUs) in the first stages of HIV-infection (17 in stage II and 20 in stage III according to CDC), compared with 32 IVDUs HIV-negatives, we found a significant decrease in circulating leucocytes (p less than 0.01), lymphocytes (p less than 0.005), platelets (p less than 0.005), serum albumin (p less than 0.005), and C3 (p less than 0.02) and significant increase in serum gammaglobulins (p less than 0.0005) and IgG (p less than 0.0005). On the other hand no difference was observed in hemoglobin and in IgA levels; nevertheless an inverse relationship between serum IgA and CD4+ lymphocytes was present in HIV-positive (HIV+) patients (r = -0.34; p = 0.04). This observation agrees with that is observed in the advanced stages of HIV-infection, which presents an increase in IgA serum levels. In these stages this fact could be due to a decrease of secretory IgA, with a deficient barrier effect; the consequent recirculation of intestinal antigens should enhance the antibody production, as well as serum IgA. In the IVDUs HIV-infected a reverse correlation between albumin serum levels and the length of HIV-positivity (r = -0.44; p = 0.008) and a direct correlation between albumin serum levels and circulating CD4+ lymphocytes (r = 0.37; p = 0.05) were present. There was no direct linear relationship between albumin serum levels and creatinine, on the contrary to what was observed in the control group. The decrease of albumin levels could have a prognostic value as in other clinical conditions, in which it is associated with a higher mortality risk. Many factors could act to decrease albumin levels, but the most important one is perhaps the malnutrition of HIV-infected patients that can also be present in the first stages of infection, negatively influencing the associated immunodeficiency.
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PMID:Serum albumin and others parameters in intravenous drug users HIV-infected. 149 83

Recombinant human migration inhibitory factor (MIF), isolated through functional expression cloning in COS-1 cells, up-regulates expression of genes encoding HLA-DR and interleukin 1 beta (IL-1 beta) and elaboration of IL-1 beta by human monocyte-derived macrophages. Administration of soluble bovine serum albumin or human immunodeficiency virus 120-kDa glycoprotein (HIV gp120) to mice in the presence of recombinant MIF together with incomplete Freund's adjuvant induced a strong T-cell proliferative response comparable to that of complete Freund's adjuvant. Recombinant MIF also increased antibody production, especially of IgG1 and IgM, in mice. Taken together, these results indicate that recombinant MIF may be useful as an adjuvant in the development of vaccines.
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PMID:Recombinant human migration inhibitory factor has adjuvant activity. 901 81


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