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Query: UMLS:C0019693 (HIV)
 170,526 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In order to delineate the molecular pathogenesis of the increased susceptibility to CMV disease in HIV infection, the patterns of antigen responsiveness in HIV-infected and non-infected individuals were investigated. CMV was fractionated by SDS-PAGE and electroblotted onto nitrocellulose. Lymphoproliferative responses of healthy HIV-, CMV+ individuals and HIV+, CMV+ asymptomatic patients to a whole CMV antigen preparation and to 20 fractions of nitrocellulose-bound CMV were then compared. Three fractions of approximate molecular weight of 130-165, 65-75, and 55-65 kD appeared to contain the major T cell stimulating antigens for HIV-, CMV+ individuals. A statistically significant depression of responses to fractions containing antigens in the ranges of 130-165 kD and 55-65 kD but not to whole CMV was seen in HIV+ individuals compared with controls. In healthy controls, the sum of the proliferative responses as measured by 3H-thymidine uptake to these three major fractions was approximately equal to the response to a whole CMV antigen preparation, whereas it was less than half of this response in five out of six HIV+ subjects. When antibody activities to CMV antigens were analysed by immunoblotting of sera from the two subject groups and also sera of ARC and AIDS patients, a selective loss of reactivity was revealed in 10 out of 19 HIV+ subjects to a band of 26-28 kD whereas all 15 HIV-, CMV+ controls recognized this band. Serum IgG and IgM values were both significantly higher in HIV+ individuals than in controls. These findings suggest that specific lesions in the repertoire of immune responsiveness to CMV antigens occur in HIV+ individuals.
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PMID:Immune responses to fractionated cytomegalovirus (CMV) antigens after HIV infection. Loss of cellular and humoral reactivity to antigens recognized by HIV-, CMV+ individuals. 217 40

1) The aspartic proteinase of the human immunodeficiency virus type 1 (HIV-1) was purified from cultures of recombinant E. coli. The enzyme preparation is homogeneous as judged by SDS-polyacrylamide gel electrophoresis and isoelectric focusing. 2) A rapid assay procedure for the proteinase was established which makes use of the cleavage of a radiolabeled decapeptide and the separation of substrate and labeled product by ion-exchange resin. 3) Activity of the enzyme is optimal at an ionic strength of 2.5-3.5M; also, the inhibitor pepstatin is a more potent inhibitor at higher ionic strength. This can be attributed to a tighter binding of both substrate and inhibitor in high-salt buffer. 4) The Km value of the decapeptide substrate is independent of the pH in the range of 3.5-7.5, while kcat shows a bell-shaped curve with a maximum at pH 5.2. The shape of the curve can be attributed to pKa values of 4.2 and 6.2 of groups on the enzyme. Pepstatin inhibition is optimal below pH 5.5, but becomes weak above pH 6.
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PMID:Purification, assay and kinetic features of HIV-1 proteinase. 218 85

An 80-kilodalton glycoprotein (gp80) was produced in human immunodeficiency virus type 2 (HIV-2)-infected cells along with three envelope glycoproteins that we have recently reported: the extracellular glycoprotein (gp125), the envelope glycoprotein precursor (gp140), and the transient dimeric form of the precursor (gp300). gp125 and gp80 were detectable after the synthesis of gp140 and the formation of gp300. Using a specific monoclonal antibody, we showed here that gp80 is a dimeric form of the transmembrane glycoprotein gp36 of HIV-2. Dimerization of the envelope glycoprotein precursor and dimeric forms of the transmembrane glycoproteins were also observed in cells infected with simian immunodeficiency virus (SIV-mac), a virus closely related to HIV-2. Under routine conditions of our experiments (i.e., extraction by 1% Triton X-100 before polyacrylamide gel electrophoresis in sodium dodecyl sulfate [SDS]), monomeric forms of the transmembrane glycoprotein of HIV-2 and SIV-mac were only seldomly observed. Dimeric forms of the envelope precursors and the transmembrane glycoproteins are probably stabilized by extraction in the nonionic detergent Triton X-100 since such dimeric forms resist dissociation during subsequent electrophoresis in the presence of the ionic detergent SDS. However, the dissociation of these dimeric forms might occur when samples are prepared by extraction directly in 1% SDS or by incubation of the purified dimers at acidic pH. Dimerization of the envelope precursor might be required for its processing to give the mature envelope proteins, whereas the transmembrane dimer might be essential for optimal structure of the virion and thus its infectivity.
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PMID:Transmembrane envelope glycoproteins of human immunodeficiency virus type 2 and simian immunodeficiency virus SIV-mac exist as homodimers. 229 88

The expression of a molecule recognized by CD4 monoclonal antibodies was investigated on human sperm using immunolabelling, biochemical and immunochemical methods. Flow cytometry detected a significant fluorescence signal. SDS-PAGE analysis and Western blotting identified a molecule of 60 kDa, consistent with a CD4-like structure as confirmed after selective immunoseparation. Additional bands reacting with anti-CD4 were found in sperm extracts (73 kDa) and seminal fluid (90 kDa). These data indicate that sperm express a molecule similar to the receptor for HIV described on mononuclear cells.
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PMID:CD4-like molecules in human sperm. 231 62

As a contribution to the noninvasive diagnosis of kidney damage, polyclonal antisera specifically directed against brush border surface glycoproteins of the proximal tubule of the human kidney were used in radioimmunoblotting studies for the assessment of kidney-tissue proteinuria. Urine specimens from healthy controls, from patients (n = 41) with various forms of renal involvement and from those suffering from symptomatic HIV-infection (AIDS) but having normal kidney function, were investigated for the excretion of kidney-derived membrane proteins. After SDS-polyacrylamide gel electrophoresis of urine samples and electroblotting of protein bands on nitrocellulose sheets, followed by incubation with the antibody and subsequently with 125I-labelled protein A, 3 major tubular glycoproteins (Mr 240 000, 160 000, 120 000) were revealed by autoradiography. The results indicate and increased shedding of epithelial membrane glycoproteins in the urine of patients with kidney lesions, and they also demonstrate the suitability of radioimmunoblotting for the determination of such tissue-antigens ("brush border-histuria").
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PMID:Tubule-derived membrane glycoproteins in the urine of patients (including those with AIDS) as analysed by radioimmunoblotting. 231 34

Two cases of wild-born chimpanzees which were positive for HIV-1 antibodies were observed in Gabon. These animals were never experimentally exposed to HIV-1 and had no history of inoculation with human blood products. A retrovirus was isolated from one of these chimpanzees. Several of the viral proteins from this virus, designated SIVcpz-GAB-1 (simian immunodeficiency virus from chimpanzee), differed in molecular weight from the known corresponding HIV/SIV proteins. The major gag protein of SIVcpz migrated on SDS-PAGE with a relative molecular mass of 25.5 and the outer membrane proteins were 110, 155 and 185 kD, respectively. SIVcpz did not induce severe cytopathic effects in human and chimpanzee lymphocytes. Antigenically, SIVcpz seems to be closer to HIV-1 than to HIV-2 and the other SIVs. Nucleic acid hybridization experiments appear to indicate that the virus is different from HIV-1 and HIV-2.
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PMID:Isolation and partial characterization of an HIV-related virus occurring naturally in chimpanzees in Gabon. 251 55

gp120 and CD4 are two glycoproteins that are considered to interact together to allow the binding of HIV to CD4+ cells. We have utilized enzymatic digestion by endoglycosidases in order to analyze N-linked carbohydrate chains of these proteins and their possible role in the interaction of gp120 or gp160 with CD4. SDS denaturation was not necessary to obtain optimal deglycosylation of either molecule, but deglycosylation of CD4, nonetheless, depended on the presence of 1% Triton X-100. Endo H and Endo F that cleave high mannose type and biantennary glycans diminish the molecular mass of the glycoproteins from 120 or 160 Kd to 90 or 130 Kd, respectively; but these enzymes had no action on CD4 glycans. Endo F N-glycanase mixture, which acts on all glycan species, including triantennary chains, led to complete deglycosylation of gp120/160 and of CD4. Therefore, probably half of the glycan moieties of gp120/160 are composed of high mannose and biantennary chains, the other half being triantennary species. The carbohydrate structures of CD4 seems to be triantennary chains. To analyze the binding of gp120/160 to CD4, we used a molecular assay in which an mAb (110-4) coupled to Sepharose CL4B allowed the attachment of soluble gp120/160 to the beads; 125I-sCD4 was then added to measure the binding of CD4 to different amounts of gp120/160. Binding to gp160 was not modified when using completely deglycosylated 125I-sCD4, while deglycosylation of gp120 or of gp160 resulted in the decrease of the binding to native CD4 by two- and fivefold, respectively. Native and deglycosylated gp120/160 bound to CD4+ cells with comparable affinities. In addition, deglycosylated gp120 displaced 125I-gp160 binding to CD4+ cells and inhibited fusion of fresh Molt-T4 cells with CEM HIV1- or HIV2-infected cells to the same extent. Taken together, these results indicate that carbohydrates of CD4 and of gp120/160 do not play a significant role in the in vitro interaction between these two molecules.
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PMID:Role of N-linked glycans in the interaction between the envelope glycoprotein of human immunodeficiency virus and its CD4 cellular receptor. Structural enzymatic analysis. 253 47

By using a fluorescence sandwich ELISA, elevated IL-2R levels were detected in the sera from both HIV-infected hemophiliacs and other HIV-infected patients. The serum IL-2R levels were reflective of the classification of HIV-induced diseases by the Centers for Disease Control. Moreover, the IL-2R levels were negatively correlated most prominently with CD4 cell counts, with lymphocyte counts, and with a decrease in the CD4-CD8 ratio but not with either WBC counts or B cell counts. As striking elevations of serum IL-2R were noted in AIDS patients with group IVD infection, the serum IL-2R was purified sequentially by using size-exclusion HPLC, high-pressure chromatofocusing, and H48 affinity HPLC. The isoelectric point values of IL-2R were separated into 4.2 and 3.8, whereas the Mr was determined to be only 45 kDa by immunoprecipitation with H48 antibody followed by SDS-PAGE. However, production of cellular and supernatant IL-2R was not elevated in PBMC of patients with AIDS or in any of the 19 HIV-I- or HIV-II-infected cell line cells. In contrast, PBMC from patients with adult T cell leukemia and cell line cells that expressed human T cell lymphotropic virus -I or -II produced soluble IL-2R, constitutively. The mechanisms by which serum levels of IL-2R might be elevated in HIV-infected patients are discussed in comparison with that in adult T cell leukemia patients.
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PMID:Soluble IL-2 receptor in AIDS. Correlation of its serum level with the classification of HIV-induced diseases and its characterization. 256 34

A type D retrovirus isolated from a permanent human cell line (PMFV) was employed as diagnostic reagent both in Southern transfer hybridization experiments using the cloned genome as a probe and in immunoblot analysis using SDS disrupted virus particles. Hybridization experiments performed under conditions of different stringencies revealed a close homology of PMFV to SAIDS type D retroviruses of serotype 1 (SRV-1, SAIDS retrovirus D/NE), a related homology to the prototype type D virus (MPMV) and to viruses of serotype 2 (SRV-2), but no homology to the endogenous type D retrovirus of squirrel monkeys (SMRV) and the human AIDS virus (HIV-1). Antigens of PMFV showed cross-reactivity only to antibodies of a SAIDS infected macaque, but no reaction to anti HIV-antibodies of seropositive patients. Thus, the type D virus isolated from a human cell line and closely related to SAIDS type D viruses of macaques is not related to the AIDS virus in humans.
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PMID:Evaluation of type D retroviruses as diagnostic tools in HIV infections. 261 25

A recombinant plasmid encompassing the human immunodeficiency virus type 1 (HIV 1) protease coding sequence and flanking regions (Ala-13 to Gly-185 of the pol open reading frame) has been expressed in two distinct strains of Escherichia coli, AR58 and AR68. In the first strain, AR58, the primary translation product, a 25 kilodalton (kDa) precursor protein, is short-lived and rapidly processes itself to the 11 kDa mature protease in vivo. In the second strain, AR68, the 25 kDa species is only partially processed, and it, a 13 kDa intermediate, and the mature 11 kDa enzyme accumulate at a ratio of 3:4.5:2.5, respectively. The 11 kDa mature protease from AR58 and the 25 kDa precursor from AR68 have been purified to homogeneity. The yield of 11 kDa enzyme from AR58 is approximately 0.02 mg/g wet weight of E. coli cell pellet. The protease has both the expected NH2- and COOH-terminal sequences. The yield of 25 kDa enzyme from AR68 is approximately 0.1 mg/g wet weight of E. coli cell pellet. In vitro, the 25 kDa precursor enzyme rapidly (t1/2 approximately equal to 9 min) processes itself into a species with a mass of approximately 13 kDa and a species with a mass of approximately 11 kDa. Both of these latter species can be separated by RP-HPLC, have the NH2-terminal sequence expected for the mature protease, and are active. The 11 kDa enzyme from AR58 comigrates with the 11 kDa enzyme from AR68 on RP-HPLC and SDS polyacrylamide gel electrophoresis. On extended incubation at 4 degrees C at either neutral or acidic pH all species of the protein exhibit further autodegradation at defined sequences. The availability of the mature, 11 kDa enzyme and the 25 kDa precursor will allow biochemical and physical studies on this critical viral enzyme.
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PMID:Characterization and autoprocessing of precursor and mature forms of human immunodeficiency virus type 1 (HIV 1) protease purified from Escherichia coli. 269 27


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