Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019693 (HIV)
 170,526 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An HIV-1 strain carrying a shorter form of the transmembrane glycoprotein (TM) with a mobility of 32 kD, named KB-1, was isolated from a Japanese male hemophiliac by coculture of his peripheral blood mononuclear cells (PBMCs) with MT-2 cells and adaption to TALL-1 cells. Another HIV-1 strain, named KB-2, was isolated from his seropositive spouse by coculture of her PBMCs with MT-2 cells. The KB-2 strain carried a TM of ordinary size, with a mobility of 41 kD. The KB-1 strain carrying a truncated form of the TM could replicate in MT-2, MT-4, TALL-1 and MOLT-4 cells. The KB-1 strain is a useful HIV-1 isolate for investigating the function of the cytoplasmic domain of the TM and the significance of the presence of an in-frame stop codon in HIV env gene.
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PMID:Shorter size of transmembrane glycoprotein of an HIV-1 isolate. 238 20

An enzyme immunoassay (EIA) for serum antibodies to human immunodeficiency virus type 1 (HIV-1), based on the synthetic pentadecapeptide SGKLICT-TAVPWNAS, a segment of the transmembrane glycoprotein (gp41) of the virus, was developed and tested for sensitivity and specificity. Sera of 152 individuals at various stages of HIV-1 infection, including two prospectively and six retrospectively studied patients exposed to HIV-1 but seronegative on initial testing in whole-virus EIA and immunoblotting, were screened with the gp41 peptide antibody EIA. The reference population consisted of 1,000 healthy HIV-1 antibody-negative blood donors. In addition, five individuals with antibodies to HIV-2 were studied. Antibodies to the synthetic peptide were detected in 100% of those with asymptomatic infection. Only one patient with LAS failed to react in the peptide EIA. Patients with HIV-2 infection did not react in this test. The peptide antibodies appeared rapidly after infection, were detectable at the time when seroconversion was observed by immunoblotting, and preceded reactivity in whole-virus EIA. Sera of seven patients with verified HIV-1 infection did not react with gp41 in immunoblotting, although antibodies were readily detectable in the gp41 peptide EIA.
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PMID:Synthetic env gp41 peptide as a sensitive and specific diagnostic reagent in different stages of human immunodeficiency virus type 1 infection. 246 May 85

Human monoclonal antibodies were raised by in vitro immunization of normal human spleen cells with denatured HIV-1 and subsequent fusion to an Epstein-Barr virus (EBV) transformed cell line. Three monoclonals reacted with both gag-encoded p24 core protein and env-encoded gp41 transmembrane glycoprotein. The cross-reaction was confirmed by reactivity with p24- and gp41-derived recombinant peptides. The peptides share two amino acid sequences which may be the basis for the cross-reaction. Attempted epitope mapping using synthetic peptides was unsuccessful due to non-specific reactivity with the short linear peptides.
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PMID:Human monoclonal antibodies to HIV-1: cross-reactions with gag and env products. 248 45

Membrane fusion induced by the envelope glycoproteins of human and simian immunodeficiency viruses (HIV and SIVmac) is a necessary step for the infection of CD4 cells and for the formation of syncytia after infection. Identification of the region in these molecules that mediates the fusion events is important for understanding and possibly interfering with HIV/SIVmac infection and pathogenesis. Amino acid substitutions were made in the 15 NH2-terminal residues of the SIVmac gp32 transmembrane glycoprotein, and the mutants were expressed in recombinant vaccinia viruses, which were then used to infect CD4-expressing T cell lines. Mutations that increased the overall hydrophobicity of the gp32 NH2-terminus increased the ability of the viral envelope to induce syncytia formation, whereas introduction of polar or charged amino acids in the same region abolished the fusogenic function of the viral envelope. Hydrophobicity in the NH2-terminal region of gp32 may therefore be an important correlate of viral virulence in vivo and could perhaps be exploited to generate a more effective animal model for the study of acquired immunodeficiency syndrome.
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PMID:Identification of the fusion peptide of primate immunodeficiency viruses. 254 5

The Sabin type 1 vaccine strain of poliovirus is probably the safest and most successful live-attenuated vaccine virus used in humans. Its widespread use since the early 1960s has contributed significantly to the virtual eradication of poliomyelitis in developed countries. We have reported previously the construction of an intertypic antigen chimaera of poliovirus, based on the Sabin 1 strain, and proposed that this virus could be modified to express on its surface antigenic determinants from other pathogens. We describe here the construction and characterization of a poliovirus antigen chimaera containing an epitope from the transmembrane glycoprotein (gp41) of human immunodeficiency virus type 1 (HIV-1). In antibody absorption experiments, the virus chimaera inhibited neutralization of HIV-1 by antipeptide monoclonal antibodies specific for the gp41 epitope and significantly reduced the group specific neutralizing activity of HIV-1-positive human sera. Rabbit antisera raised by subcutaneous injection of the polio/HIV chimaera in adjuvant was shown to be specific for HIV-1 gp41 in peptide-binding assays and by western blotting. Moreover, the antisera neutralized a wide range of American and African HIV-1 isolates and also inhibited virus-induced cell fusion. Monoclonal antibodies against the HIV-1 derived regions of the chimaera also neutralized HIV-1. These results establish the potential of using poliovirus for the presentation of foreign antigens and suggest that Sabin 1 poliovirus/HIV chimaeras could offer an approach to the development of an HIV vaccine.
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PMID:An engineered poliovirus chimaera elicits broadly reactive HIV-1 neutralizing antibodies. 254 97

A serum panel obtained from male homosexuals (n = 278); i.v. drug abusers (n = 99), patients attending a VD clinic (n = 390), blood donors who visited Central or West Africa (n = 573), blood donors who had sexual contact with natives from Central or West Africa (n = 38), blood donors from Surinam, South America (n = 481), individuals positive for anti-HIV-1 (n = 94), individuals with indeterminate HIV-1 western blot (WB) reactions (n = 73), African patients with AIDS or AIDS-related symptoms (n = 30), and random Dutch blood donors (n = 555), was tested with HIV-2 ELISA (ELAVIA-2). Of these 2,611 samples, 32 (1.2%) were repeatedly reactive. Antibodies to gp140/105env were found in 4/32 by HIV-2 WB, and in 1/4 by radioimmunoprecipitation (RIPA). These 4 HIV-2 WB-positive samples were also reactive with gp160/120env in HIV-1 WB, suggesting cross-reactivity. In a spot test with synthetic peptides of the transmembrane glycoprotein of both HIV types, 3/4 were only HIV-1 positive and 1/4 was strongly HIV-2 positive and weakly HIV-1 positive. In inhibition assays with soluble HIV-1 or HIV-2 synthetic peptides in HIV-1 and HIV-2 peptide ELISA, cross-reactivity was excluded, which indicates an HIV variant or HIV-1/HIV-2 double infection. It is concluded that for the moment HIV-2 infection is at low prevalence in risk groups in The Netherlands, and that in addition to WB and RIPA, synthetic peptide assays are useful for differentiation between HIV-1 and HIV-2 antibodies.
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PMID:Diagnosis and prevalence of HIV-2 antibodies in different population subsets in The Netherlands. 257 26

The human immunodeficiency virus type 1 (HIV-1) envelope protein is synthesized as a gp160 precursor that is cleaved to a 120 kDa exterior glycoprotein (gp120) and a 41 kDa transmembrane glycoprotein (gp41). The HIV-1 envelope protein was stably expressed under the control of the transactivator proteins tat and rev, in wild-type and mutant Chinese hamster ovary (CHO) cells. The mutant, ldlD, is conditionally defective for the addition of galactose and N-acetylgalactosamine to oligosaccharide chains. The effects of glycosylation modification on the HIV-1 envelope's structure and function were examined. The effects of galactosylation on the structure of the envelope proteins suggest that cleavage of the gp160 precursor into gp120 and gp41 occurs intracellularly, apparently concurrent with the addition of galactose to N-linked oligosaccharides of the envelope proteins. No evidence for O-linked glycosylation of the envelope proteins in CHO cells was observed. The envelope protein in the transfected hamster cells mediated the fusion of these cells with CD4-positive lymphocytes, and this fusogenic activity was independent of the addition of either galactose or N-acetylgalactosamine to oligosaccharides in the transfected cells.
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PMID:Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. 264 53

The transmembrane glycoprotein (gp41) of human immunodeficiency virus type-1 (HIV-1) has a long cytoplasmic domain of unknown functional significance. To investigate the role of the carboxy-terminal (C-terminal) portion of the HIV-1 envelope protein in viral replication, infectivity, and cytopathogenicity, we examined the properties of a panel of mutants with variable deletions in the 3'-env region. Deletion of the C-terminal 76 amino acids did not abolish production of reverse transcriptase upon transfection of COS-1 cells. Deletion of the C-terminal 6-14 amino acids appeared sufficient to alter the replication pattern, infectivity, and cytopathogenicity of some clones. The data suggest that conformational determinants or specific sequences are responsible for the observed changes, rather than simply the length of the gp41 cytoplasmic tail.
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PMID:Role of the carboxy-terminal portion of the HIV-1 transmembrane protein in viral transmission and cytopathogenicity. 278 44

A series of synthetic peptides corresponding to segments of HIV encoded proteins were selected using criteria described by Welling et al. [(1985) FEBS Lett. 188, 215]. Synthetic peptide analogs to gp120 (2-13), (55-65), gp41 (582-596) (659-670) and tatIII (71-83) were recognized by 41-67% of sera or plasma from individuals known to be infected with HIV on the basis of virus isolation or Western blot screening. The peptide which reacted with most sera or plasma was gp41 (582-596), a conserved region in the transmembrane glycoprotein. An extended peptide analog, gp41 (579-599), tested against the same samples showed almost 100% reactivity, confirming independent studies identifying a highly immunodominant region of gp41. There was an unexpected high prevalence of antibodies (25%) to the tatIII peptide.
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PMID:Recognition of envelope and tat protein synthetic peptide analogs by HIV positive sera or plasma. 283 37

Based on the finding that cells producing antibodies to human immunodeficiency virus (HIV) circulate in the peripheral blood of HIV-infected individuals, attempts were made to immortalize such B cells with Epstein-Barr virus. Mononuclear cells from 58 HIV-seropositive subjects at various stages of HIV infection were transformed, and anti-HIV cell lines were derived from 4 subjects, all of whom were in early stages of infection. Seven of these cell lines have been stable with respect to antibody production for up to 15 months. Three lines are producing IgG antibody to the 41-kDa HIV transmembrane glycoprotein gp41 and 4 produce IgG antibodies to the 24-kDa HIV core protein p24, its precursors and a breakdown product. The antibodies are reactive by ELISA, by radioimmunoprecipitation, and by Western blot, demonstrating the feasibility of producing multiple stable cell lines synthesizing human monoclonal antibodies to HIV by immortalization of peripheral blood cells with Epstein-Barr virus.
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PMID:Generation of human monoclonal antibodies to human immunodeficiency virus. 292 1


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