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

The interaction of the peptide fragment 828-848, called P828, from the carboxy-terminal region of the envelope glycoprotein gp41 of HIV-I with model membranes composed of phosphatidylcholine (PC) and phosphatidylglycerol (PG) was investigated using microelectrophoretic mobility of liposomes, fluorescence polarization of labeled lipids, NMR, and differential scanning calorimetry. The peptide binds to negatively charged lipid surfaces. No interaction between P828 and neutral PC surfaces is observed. The interaction between the peptide and the lipid is exclusively electrostatic with the six positively charged arginines of P828 acting as binding sites for PG. Circular dichroism measurements of P828 indicate that the peptide undergoes a transition from a random coil to an ordered conformation upon binding to negatively charged PG bilayers or SDS micelles, but not in the presence of neutral PC bilayers. The ordered structure has an apparent helical content of 60%. IN DOPG/DOPC mixtures containing 20 mol % DOPG, the peptide causes the formation of lipid domains enriched in DOPG, as assessed by measurement of fluorescence energy transfer between labeled PG and PC. The formation of these domains requires energy and therefore reduces the strength of peptide binding to the lipid matrix. Our data support and quantitate the results from antibody binding studies [Haffar, O.K., Dowbenko, D. J., & Berman, P. W. (1988) J. Cell Biol. 107, 1677-1687] that the carboxy-terminal segment of the envelope glycoprotein gp41 interacts with microsomal membranes.
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PMID:Interaction of peptide fragment 828-848 of the envelope glycoprotein of human immunodeficiency virus type I with lipid bilayers. 845 72

The ability of HTLV-I to infect cells is presumed to be dependent, in some part, on the attachment of the virus to a target cell via a specific cell surface receptor which is, as yet, unknown. Here we present evidence that a monoclonal antibody, Mab 34-23, inhibits the binding of HTLV-I to IL-2 and phytohemagglutinin-activated peripheral blood mononuclear cells and also inhibits virus entry into these cells. Analysis of a variety of target cells, including a human:mouse somatic hybrid which contains only human chromosome 17q, indicates that the binding of Mab 34-23 correlates with HTLV-I adsorption and entry. SDS-PAGE and Western blot analysis show that Mab 34-23 binds to four major proteins of MW 31, 45, 55, and 70 kDa and this binding can be inhibited by HTLV-I and not HIV proteins. HTLV-I virions bind to proteins of similar molecular weight and virus-binding to these proteins can be inhibited by preincubation with Mab 34-23. These data suggest that Mab 34-23 may identify a specific cell surface receptor(s) for HTLV-I.
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PMID:Identification of a putative cellular receptor for HTLV-I by a monoclonal antibody, Mab 34-23. 848 Apr 13

A principal neutralizing determinant of human immunodeficiency virus type 1 (HIV-1) lies within the V3 loop of gp120, the external major envelope glycoprotein. V3 loop peptides derived from two HIV-1 strains, HTLV-III BH-10 (V3-BH10) and LAVELI (V3-ELI), were synthesized and biotinylated. The binding of both biotinylated V3-BH10 and V3-ELI to the surfaces of MOLT-4 clone 8 cells was demonstrated by flow cytometric analyses. Both the peptides (more than 2 microM) bound to the cells (2 x 10(5) in a dose-dependent manner. The binding of biotinylated V3-BH10 was specifically inhibited by a neutralizing monoclonal antibody (0.5 beta). The binding of both of the biotinylated V3 loop peptides was enhanced by the addition of unlabeled V3-BH10. In addition, the peptides were employed as ligands on affinity columns. A major V3 loop binding protein (V3BP) was purified from the membrane soluble fraction of MOLT-4 cells by successive application to two different V3 loop columns. V3BP consisted of two major polypeptides (32 and 33 kDa). The SDS-PAGE profile of V3BP did not change under non-reducing conditions, but only a single band was observed after analysis on native PAGE. The major peak of the eluate as determined by size exclusion chromatography was broad and the estimated relative molecular mass was much larger than 33 kDa, suggesting that V3BP comprises several subunits. Taken together, we confirmed that the V3 loop peptides are useful in the characterization of V3BP(s) of which they are conformational ligands.
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PMID:Applications of biotinylated V3 loop peptides of human immunodeficiency virus type 1 to flow cytometric analyses and affinity chromatographic techniques. 848 4

Two mouse monoclonal antibodies (VIC5 and VIC6; referred to as Ab1) reacting with the p24 core antigen of HIV-1 were used to produce mouse monoclonal anti-idiotypic antibodies (Ab2). Six anti-idiotypic antibodies were characterized. The five anti-idiotypic antibodies directed against VIC6 partly competed which each other and thus defined a set of overlapping idiotypes on Ab1. All 6 Ab2s inhibited the binding of the corresponding anti-p24 antibody to antigen, although four (W1, Y16, Y6, X14) were markedly more inhibitory than the remaining two (G6, Y11). All six Ab2s were antigen-inhibitable; however the interaction of G6 and Y11 with Ab1 was blocked with considerably less soluble p24 antigen than the remaining four. Correspondingly, G6 and Y11 had lower affinities for Ab1 than did W1, Y6 and X14; the affinity index of Y16 was equivalent to that of Y11. None of the Ab2s reacted with H or L chains of Ab1 after reduction on SDS-gels. Similarly, both Ab1s failed to react with the H or L chains of Ab2. These criteria appeared to define at least four of these Ab2s as internal image antibodies whose image is composed of both H and L chains. The anti-idiotypic antibodies were injected either individually or as a combined preparation of all 6 into syngeneic mice and Porton rats. Despite the presence of anti-anti-idiotypic antibodies (Ab3) in these animals, when used individually no antigen-specific antibodies were found. A small response to p24 antigen was induced in 3 of 6 mice using preparations containing all 6 anti-idiotypes.
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PMID:Mouse monoclonal anti-idiotypic antibodies to HIV p24: immunochemical properties and internal imagery. 848 75

A recombinant HIV-1 gp120 (rgp120) was expressed in a permanent Chinese Hamster Ovary (CHO) cell line (L761h) that constitutively secretes the product of clone p4 derived from the env gene of HIV-1 isolate GB8. The rgp120 was isolated from cell culture supernatants by a simple, rapid, non-denaturing and efficient purification procedure based on a novel combination of lectin affinity and FPLC ion-exchange chromatography. The purity of the isolated glycoprotein was rigorously confirmed by SDS-PAGE, capillary electrophoresis, laser desorption mass spectrometry, total amino acid analysis and N-terminal amino acid sequencing. The retention of biological activity by the purified rgp120 was assessed by determining the dissociation constant of rgp120 binding to sCD4. After formulation of this highly purified and biologically active rgp120 with "conventional" adjuvants, including types already used in clinical trials of candidate gp120-based HIV vaccines, antibody responses in immunised rabbits were analysed using panels of overlapping synthetic peptides. The consequences of using currently available adjuvants to deliver highly specialised and perhaps conformation-dependent molecules, like HIV gp120, are presented and discussed in the context of HIV vaccine development.
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PMID:Efficient purification and rigorous characterisation of a recombinant gp120 for HIV vaccine studies. 852 94

Previous reports have shown that cyclophilin A (CyPA) is found to be specifically associated with human immunodeficiency virus type-1 (HIV-1) virions and is required for infectivity (Franke et al. Nature 372:359; Thali et al. Nature 372:363). We have examined CyPA associated with HIV-1MN virions. Virions from infected human lymphoid cells were analyzed by high-pressure liquid chromatography (HPLC), protein sequence, and immunoblot analysis. At least three forms of CyPA were found: an unmodified form, an N-terminally modified form, and an N-terminally modified form that migrates as a larger isoform on a reducing-SDS polyacrylamide gel. Using a protease digestion procedure, CyPA that is associated with virions was found to be located inside the viral membrane. Similar examination of SIVMne produced by HUT-78 human T cells did not detect specific incorporation of CyPA into SIV virions. Our results are consistent with the role of CyPA acting early in the infectious process of HIV-1.
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PMID:Analysis and localization of cyclophilin A found in the virions of human immunodeficiency virus type 1 MN strain. 855 96

Matrix-associated laser desorption ionization/mass spectrometry (MALDI/MS) has been used to examine whole bacteria for the presence of a recombinant HIV p26 fusion protein. MALDI/MS, combined with affinity-purification techniques, is also shown to be very useful in monitoring the enzymatic cleavage of both affinity-bound fusion protein and fusion protein in solution. The combination of mass resolution, sensitivity, and speed of analysis makes MALDI/MS an attractive alternative to SDS-PAGE.
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PMID:Monitoring cleavage of fusion proteins by matrix-assisted laser desorption ionization/mass spectrometry: recombinant HIV-1IIIB p26. 866 Jun 21

The humoral immune response of patients infected with Cryptococcus neoformans var. neoformans and C. neoformans var. gattii to cytoplasmic (non-capsular) antigens from the two varieties of Cryptococcus has been investigated. Cytoplasmic antigens from C. neoformans (one clinical isolate and one acapsular mutant of var. neoformans and two clinical isolates from var. gattii) were subject to isoelectric focusing, SDS-PAGE and Western blotting; patients sera was then used in the immunoenzyme development of the Western blots. The humoral response from the 20 patients (all HIV+) infected with var. neoformans against the var. neoformans antigens was predominantly IgG based, with a large number of bands recognised: the most commonly recognised bands were at 26, 52, 74, 100, 115 and 144 kDa. The IgM response was less pronounced and the IgA response was practically non-existent. The humoral response of the sera from the 15 patients (all but one HIV-) infected with var. gattii against var. gattii antigens was also predominantly IgG based with bands at 37, 55, 65, 74, 94 and 115 kDa being most commonly recognised. Periodate treatment of cytoplasmic antigens reduced the intensity of antigen recognition, though it did not absolutely destroy reactivity to any individual antigen. Comparison of immunodevelopment of cytoplasmic antigens from both varieties grown at 25 degrees C and 37 degrees C revealed that culture temperature made no differences in the number of bands recognised although there were differences in the intensity of recognition. This is the first report on the pattern of serological recognition of the non-capsular antigens from the two varieties of Cryptococcus and it identifies a number of major antigenic components.
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PMID:Recognition of cytoplasmic yeast antigens of Cryptococcus neoformans var. neoformans and Cryptococcus neoformans var. gattii by immune human sera. 906 57

In the course of investigating effective biological active substances, we detected a substance in an extract of silkworm faeces that markedly suppresses viral production. The extract, prepared with hot phosphate-buffered saline and purified with ammonium sulfate precipitation, inhibited HVJ (Sendai virus), HSV (herpes simplex virus type-1), and HIV (human immunodeficiency virus type-1), but not poliovirus, suggesting that it is effective on enveloped virus production but not on non-enveloped ones. In the case of HVJ, indirect immunofluorescent staining using anti-HVJ antibody and Northern blotting analysis showed that, while viral adsorption and entry into the host cells were not affected, the synthesis of viral specific gene was inhibited by pretreatment of the virions with the extract. The extract affected more effectively aged virion, which losses membrane function as barrier and its envelope is leaky, than young virion that maintains barrier function. The active substance was partially purified by gel filtration after treatment of the extract with 1 N NaOH solution. From analysis with SDS-PAGE (SDS-polyacrylamide gel electrophoresis), protein bands were detected with molecular masses of about 25 kDa and near 14 kDa, while sugars were also detected with lectin blotting.
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PMID:Suppression of enveloped virus production with a substance from silkworm faeces. 907 8

The fusion domain of human immunodeficiency virus (HIV-1) envelope glycoprotein (gp120-gp41) is a conserved hydrophobic region located at the N terminus of the transmembrane glycoprotein (gp41). A V2E mutant has been shown to dominantly interfere with wild-type envelope-mediated syncytium formation and virus infectivity. To understand this phenomenon, a 33-residue peptide (wild type, WT) identical to the N-terminal segment of gp41 and its V2E mutant were synthesized, fluorescently labeled, and characterized. Both peptides inhibited HIV-1 envelope-mediated cell-cell fusion and had similar alpha-helical content in membrane mimetic environments. Studies with fluorescently labeled peptide analogues revealed that both peptides have high affinity for phospholipid membranes, are susceptible to digestion by proteinase-K in their membrane-bound state, and tend to self- and coassemble in the membranes. In SDS-polyacrylamide gel electrophoresis the WT peptide formed dimers as well as higher order oligomers, whereas the V2E mutant only formed dimers. The WT, but not the V2E mutant, induced liposome aggregation, destabilization, and fusion. Moreover, the V2E mutant inhibited vesicle fusion induced by the WT peptide, probably by forming inactive heteroaggregates. These data form the basis for an explanation of the mechanism by which the gp41 V2E mutant inhibits HIV-1 infectivity in cells when co-expressed with WT gp41.
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PMID:Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell Fusion. Structure-function study. 915 94


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