Academic literature on the topic 'HIV Envelope Protein gp160'

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Journal articles on the topic "HIV Envelope Protein gp160"

1

Archibald, David W., Carla A. Hebert, Kevin L. Gregory, and George K. Lewis. "Effects of Human Salivas on Recombinant HIV-1 Proteins." Critical Reviews in Oral Biology & Medicine 4, no. 3 (April 1993): 475–78. http://dx.doi.org/10.1177/10454411930040033101.

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Human saliva appears to contain factors that are inhibitory to HIV-1 infectivity in vitro. We investigated the effect of incubating human whole, parotid, labial minor salivary gland and sublingual/submandibular salivas with recombinant HIV-1 envelope protein (gpl60). Saliva/gpl60 mixtures were run on polyacrylamide gels, transferred to nitrocellulose, and assayed for the presence of gp 160 using monoclonal antibodies or HIV-1-positive sera. Incubation of the gp 160 with whole saliva reduced the intensity of gp 160 bands to 35% of control values. Minor salivary gland saliva reduced the band intensities to 65% of control values, while other saliva types diminished gp160 to 75% of control values. Protease inhibitors had no effect. Components of untreated whole human saliva prevent the detection of the HIV-1 envelope protein gp 160 by antibodies to gp120 and gp41 in immunoblots. The results suggest that complexes between whole saliva factors and certain domains of gp160 block monoclonal antibody binding or are unable to migrate through polyacrylamide gels.
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Khattar, Sunil K., Anthony L. DeVico, Celia C. LaBranche, Aruna Panda, David C. Montefiori, and Siba K. Samal. "Enhanced Immune Responses to HIV-1 Envelope Elicited by a Vaccine Regimen Consisting of Priming with Newcastle Disease Virus Expressing HIV gp160 and Boosting with gp120 and SOSIP gp140 Proteins." Journal of Virology 90, no. 3 (November 18, 2015): 1682–86. http://dx.doi.org/10.1128/jvi.02847-15.

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Newcastle disease virus (NDV) expressing HIV-1 BaL gp160 was evaluated either alone or with monomeric BaL gp120 and BaL SOSIP gp140 protein in a prime-boost combination in guinea pigs to enhance envelope (Env)-specific humoral and mucosal immune responses. We showed that a regimen consisting of an NDV prime followed by a protein boost elicited stronger serum and mucosal Th-1-biased IgG responses and neutralizing antibody responses than NDV-only immunizations. Additionally, these responses were higher after the gp120 than after the SOSIP gp140 protein boost.
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McKenna, Philip M., Roger J. Pomerantz, Bernhard Dietzschold, James P. McGettigan, and Matthias J. Schnell. "Covalently Linked Human Immunodeficiency Virus Type 1 gp120/gp41 Is Stably Anchored in Rhabdovirus Particles and Exposes Critical Neutralizing Epitopes." Journal of Virology 77, no. 23 (December 1, 2003): 12782–94. http://dx.doi.org/10.1128/jvi.77.23.12782-12794.2003.

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ABSTRACT Rabies virus (RV) vaccine strain-based vectors show significant promise as potential live-attenuated vaccines against human immunodeficiency virus type 1 (HIV-1). Here we describe a new RV construct that will also likely have applications as a live-attenuated or killed-particle immunogen. We have created a RV containing a chimeric HIV-1 Env protein, which contains introduced cysteine residues that give rise to an intermolecular disulfide bridge between gp120 and the ectodomain of gp41. This covalently linked gp140 (gp140 SOS) is fused in frame to the cytoplasmic domain of RV G glycoprotein and is efficiently incorporated into the RV virion. On the HIV-1 virion, the gp120 and gp41 moieties are noncovalently associated, which leads to extensive shedding of gp120 from virions and virus-infected cells. The ability to use HIV-1 particles as purified, inactivated immunogens has been confounded by the loss of gp120 during preparation. Additionally, monomeric gp120 and uncleaved gp160 molecules have been shown to be poor antigenic representations of virion-associated gp160. Because the gp120 and gp41 portions are covalently attached in the gp140 SOS molecule, the protein is maintained on the surface of the RV virion throughout purification. Surface immunostaining and fluorescence-activated cell sorting analysis with anti-envelope antibodies show that the gp140 SOS protein is stably expressed on the surface of infected cells and maintains CD4 binding capabilities. Furthermore, Western blot and immunoprecipitation experiments with infected-cell lysates and purified virions show that a panel of neutralizing anti-envelope antibodies efficiently recognize the gp140 SOS protein. The antigenic properties of this recombinant RV particle containing covalently attached Env, as well as the ability to present Env in a membrane-bound form, suggest that this approach could be a useful component of a HIV-1 vaccine strategy.
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Ivey-Hoyle, M., and M. Rosenberg. "Rev-dependent expression of human immunodeficiency virus type 1 gp160 in Drosophila melanogaster cells." Molecular and Cellular Biology 10, no. 12 (December 1990): 6152–59. http://dx.doi.org/10.1128/mcb.10.12.6152.

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Expression of the human immunodeficiency virus (HIV) structural proteins in mammalian cells is regulated posttranscriptionally by the viral Rev protein. Rev has been shown to trans-activate expression by relieving the nuclear sequestration of RNAs containing viral gag or env coding regions. We have studied the effects of Rev on expression of the HIV type 1 env gene in Drosophila melanogaster cells. We demonstrated that synthesis of the gp160 envelope protein was fully Rev dependent; that is, gp160 was produced only when Rev function was coexpressed in the cell. Analysis of total cellular RNA indicated that Rev did not significantly affect the overall levels of gp160 RNA production. Instead, mRNA encoding gp160 was found in the cytoplasm only in cells expressing Rev, whereas in cells lacking Rev, this RNA was present only in the nucleus. Furthermore, comparison of these results with the previously demonstrated Rev-independent expression of gp120 envelope protein with this system indicated that information contained in the gp41 coding region appears to be critical to the selective nuclear retention of gp160 transcripts in the absence of Rev. Our results clearly demonstrate that the mechanism of Rev action is conserved in the insect cell system, and, thus, Rev must function via cellular machinery common to most, if not all, higher cell systems.
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Ivey-Hoyle, M., and M. Rosenberg. "Rev-dependent expression of human immunodeficiency virus type 1 gp160 in Drosophila melanogaster cells." Molecular and Cellular Biology 10, no. 12 (December 1990): 6152–59. http://dx.doi.org/10.1128/mcb.10.12.6152-6159.1990.

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Expression of the human immunodeficiency virus (HIV) structural proteins in mammalian cells is regulated posttranscriptionally by the viral Rev protein. Rev has been shown to trans-activate expression by relieving the nuclear sequestration of RNAs containing viral gag or env coding regions. We have studied the effects of Rev on expression of the HIV type 1 env gene in Drosophila melanogaster cells. We demonstrated that synthesis of the gp160 envelope protein was fully Rev dependent; that is, gp160 was produced only when Rev function was coexpressed in the cell. Analysis of total cellular RNA indicated that Rev did not significantly affect the overall levels of gp160 RNA production. Instead, mRNA encoding gp160 was found in the cytoplasm only in cells expressing Rev, whereas in cells lacking Rev, this RNA was present only in the nucleus. Furthermore, comparison of these results with the previously demonstrated Rev-independent expression of gp120 envelope protein with this system indicated that information contained in the gp41 coding region appears to be critical to the selective nuclear retention of gp160 transcripts in the absence of Rev. Our results clearly demonstrate that the mechanism of Rev action is conserved in the insect cell system, and, thus, Rev must function via cellular machinery common to most, if not all, higher cell systems.
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Tamma, Seetha M. Lakshmi, Narendra Chirmule, Hirosuka Yagura, Naoki Oyaizu, Vaniambadi Kalyanaraman, and Savita Pahwa. "CD4 Cross-Linking (CD4XL) Induces RAS Activation and Tumor Necrosis Factor-α Secretion in CD4+ T Cells." Blood 90, no. 4 (August 15, 1997): 1588–93. http://dx.doi.org/10.1182/blood.v90.4.1588.

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Abstract CD4 molecules are the primary receptors for human immunodeficiency virus (HIV) and bind the envelope glycoprotein gp120 of HIV with high-affinity. We have previously shown that cross-linking of CD4 molecules (CD4XL) in normal peripheral blood mononuclear cells (PBMC) results in secretion of cytokines tumor necrosis factor-α (TNF-α) and interferon-γ (IFN-γ), but not of interleukin-2 (IL-2) or IL-4. To investigate the intracellular signaling events associated with CD4-gp120 interaction, we incubated CD4+ T cells from peripheral blood of HIV-negative healthy donors with HIV envelope protein gp160 alone or performed CD4XL with gp160 and anti-gp160 antibody. This procedure resulted in tyrosine phosphorylation of intracellular substrates p59fyn, zap 70, and p95vav and also led to ras activation, as assessed by conversion of rasGDP to rasGTP. The role of ras in CD4 signaling was further investigated using CD4+ Jurkat cells transfected with a dominant negative ras mutant. CD4+ T cells expressing dn-ras secreted significantly reduced levels of TNF-α in response to CD4XL. These studies indicate that interaction of HIV gp160 with CD4 molecules activates the ras pathway in T cells, which may result in the cells becoming unresponsive to subsequent stimulation.
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Tamma, Seetha M. Lakshmi, Narendra Chirmule, Hirosuka Yagura, Naoki Oyaizu, Vaniambadi Kalyanaraman, and Savita Pahwa. "CD4 Cross-Linking (CD4XL) Induces RAS Activation and Tumor Necrosis Factor-α Secretion in CD4+ T Cells." Blood 90, no. 4 (August 15, 1997): 1588–93. http://dx.doi.org/10.1182/blood.v90.4.1588.1588_1588_1593.

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CD4 molecules are the primary receptors for human immunodeficiency virus (HIV) and bind the envelope glycoprotein gp120 of HIV with high-affinity. We have previously shown that cross-linking of CD4 molecules (CD4XL) in normal peripheral blood mononuclear cells (PBMC) results in secretion of cytokines tumor necrosis factor-α (TNF-α) and interferon-γ (IFN-γ), but not of interleukin-2 (IL-2) or IL-4. To investigate the intracellular signaling events associated with CD4-gp120 interaction, we incubated CD4+ T cells from peripheral blood of HIV-negative healthy donors with HIV envelope protein gp160 alone or performed CD4XL with gp160 and anti-gp160 antibody. This procedure resulted in tyrosine phosphorylation of intracellular substrates p59fyn, zap 70, and p95vav and also led to ras activation, as assessed by conversion of rasGDP to rasGTP. The role of ras in CD4 signaling was further investigated using CD4+ Jurkat cells transfected with a dominant negative ras mutant. CD4+ T cells expressing dn-ras secreted significantly reduced levels of TNF-α in response to CD4XL. These studies indicate that interaction of HIV gp160 with CD4 molecules activates the ras pathway in T cells, which may result in the cells becoming unresponsive to subsequent stimulation.
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Lin, P. F., H. Samanta, C. M. Bechtold, C. A. Deminie, A. K. Patick, M. Alam, K. Riccardi, R. E. Rose, R. J. White, and R. J. Colonno. "Characterization of siamycin I, a human immunodeficiency virus fusion inhibitor." Antimicrobial Agents and Chemotherapy 40, no. 1 (January 1996): 133–38. http://dx.doi.org/10.1128/aac.40.1.133.

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The human immunodeficiency virus (HIV) fusion inhibitor siamycin I, a 21-residue tricyclic peptide, was identified from a Streptomyces culture by using a cell fusion assay involving cocultivation of HeLa-CD4+ cells and monkey kidney (BSC-1) cells expressing the HIV envelope gp160. Siamycin I is effective against acute HIV type 1 (HIV-1) and HIV-2 infections, with 50% effective doses ranging from 0.05 to 5.7 microM, and the concentration resulting in a 50% decrease in cell viability in the absence of viral infection is 150 microM in CEM-SS cells. Siamycin I inhibits fusion between C8166 cells and CEM-SS cells chronically infected with HIV (50% effective dose of 0.08 microM) but has no effect on Sendai virus-induced fusion or murine myoblast fusion. Siamycin I does not inhibit gp120 binding to CD4 in either gp120- or CD4-based capture enzyme-linked immunosorbent assays. Inhibition of HIV-induced fusion by this compound is reversible, suggesting that siamycin I binds noncovalently. An HIV-1 resistant variant was selected by in vitro passage of virus in the presence of increasing concentrations of siamycin I. Drug susceptibility studies on a chimeric virus containing the envelope gene from the siamycin I-resistant variant indicate that resistance maps to the gp160 gene. Envelope-deficient HIV complemented with gp160 from siamycin I-resistant HIV also displayed a resistant phenotype upon infection of HeLa-CD4-LTR-beta-gal cells. A comparison of the DNA sequences of the envelope genes from the resistant and parent viruses revealed a total of six amino acid changes. Together these results indicate that siamycin I interacts with the HIV envelope protein.
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McGettigan, James P., Heather D. Foley, Igor M. Belyakov, Jay A. Berzofsky, Roger J. Pomerantz, and Matthias J. Schnell. "Rabies Virus-Based Vectors Expressing Human Immunodeficiency Virus Type 1 (HIV-1) Envelope Protein Induce a Strong, Cross-Reactive Cytotoxic T-Lymphocyte Response against Envelope Proteins from Different HIV-1 Isolates." Journal of Virology 75, no. 9 (May 1, 2001): 4430–34. http://dx.doi.org/10.1128/jvi.75.9.4430-4434.2001.

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ABSTRACT Novel viral vectors that are able to induce both strong and long-lasting immune responses may be required as effective vaccines for human immunodeficiency virus type 1 (HIV-1) infection. Our previous experiments with a replication-competent vaccine strain-based rabies virus (RV) expressing HIV-1 envelope protein from a laboratory-adapted HIV-1 strain (NL4–3) and a primary HIV-1 isolate (89.6) showed that RV-based vectors are excellent for B-cell priming. Here we report that cytotoxic T-lymphocyte (CTL) responses against HIV-1 gp160 are induced by recombinant RVs. Our results indicated that a single inoculation of mice with an RV expressing HIV-1 gp160 induced a solid and long-lasting memory CTL response specific for HIV-1 envelope protein. Moreover, CTLs from immunized mice were not restricted to the homologous HIV-1 envelope protein and were able to cross-kill target cells expressing HIV-1 gp160 from heterologous HIV-1 strains. These studies further suggest promise for RV-based vectors to elicit a persistent immune response against HIV-1 and their potential utility as efficacious anti-HIV-1 vaccines.
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Casini, Antonio, Michele Olivieri, Lara Vecchi, Oscar R. Burrone, and Anna Cereseto. "Reduction of HIV-1 Infectivity through Endoplasmic Reticulum-Associated Degradation-Mediated Env Depletion." Journal of Virology 89, no. 5 (December 24, 2014): 2966–71. http://dx.doi.org/10.1128/jvi.02634-14.

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During the HIV-1 replicative cycle, the gp160 envelope is processed in the secretory pathway to mature into the gp41 and gp120 subunits. Misfolded proteins located within the endoplasmic reticulum (ER) are proteasomally degraded through the ER-associated degradation (ERAD) pathway, a quality control system operating in this compartment. Here, we exploited the ERAD pathway to induce the degradation of gp160 during viral production, thus leading to the release of gp120-depleted viral particles.
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Dissertations / Theses on the topic "HIV Envelope Protein gp160"

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Chen, Yuxin. "Characterization of Envelope-Specific Antibody Response Elicited by HIV-1 Vaccines: A Dissertation." eScholarship@UMMS, 2001. http://escholarship.umassmed.edu/gsbs_diss/760.

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Despite 30 years of intensive research,an effective human immunodeficiency virus (HIV) vaccine still remains elusive. The desirable immune response capable of providing protection against HIV acquisition is still not clear. The accumulating evidence learned from a recent vaccine efficacy correlate study not only confirmed the importance of antibody responses, but also highlighted potential protective functions of antibodies with a broad repertoire of HIV-1 epitope specificities and a wide range of different antiviral mechanisms. This necessitates a deep understanding of the complexity and diversity of antibody responses elicited by HIV-1 vaccines. My dissertation characterizes antibody response profiles of HIV-1 Env antibodies elicited by several novel immunogens or different immunization regimens, in terms of magnitude, persistence, epitope specificity, binding affinity, and biological function. First, to overcome the challenge of studying polyclonal sera without established assays, we expanded a novel platform to isolate Env-specific Rabbit mAbs (RmAb) elicited by DNA prime-protein boost immunization. These RmAbs revealed diverse epitope specificity and cross-reactivity against multiple gp120 antigens from more than one subtype, and several had potent and broad neutralizing activities against sensitive Tier 1 viruses. Further, structural analysis of two V3 mAbs demonstrated that a slight shift of the V3 epitope might have a dramatic impact on their neutralization activity. All of these observations provide a useful tool to study the induction of a desired type of antibody by different immunogens or different immunization regimens. Since heavily glycosylated HIV Env protein is a critical component of an HIV vaccine, we wanted to determine the impact of the HIV Env-associated glycan shield on antibody responses. We were able to produce Env proteins with a selective and homogeneous pattern of N-glycosylation using a glycoengineered yeast cell line. Antigenicity of these novel Env proteins was examined by well-characterized human mAbs. Immunogenicity studies showed that they were immunogenic and elicited gp120- specific antibody responses. More significantly, sera elicited by glycan-modified gp120 protein immunogens revealed better neutralizing activities and increased diversity of epitopes compared to sera elicited by traditional gp120 produced in Chinese Hamster Ovary (CHO) cells. Further, we examined the impact of the delivery order of DNA and protein immunization on antibody responses. We found that DNA prime-protein boost induced a comparable level of Env-specific binding Abs at the peak immunogenicity point to codelivery of DNA. However, antibody responses from DNA prime-protein boost had high avidity and diverse specificities, which improved potency and breadth of neutralizing Abs against Tier 1 viruses. Our data indicate that DNA vaccine priming of the immune system is essential for generation of high-quality antibodies. Additionally, we determined the relative immunogenicity of gp120 and gp160 Env in the context of DNA prime-protein boost vaccination to induce high-quality antibody responses. Immunized sera from gp120 DNA primed animals, but not those primed with gp160 DNA, presented with distinct antibody repertoire specificities, a high magnitude of CD4 binding site-directed binding capabilities as well as neutralizing activities. We confirmed the importance of using the gp120 Env form at the DNA priming phase, which directly determined the quality of antibody response.
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Chen, Yuxin. "Characterization of Envelope-Specific Antibody Response Elicited by HIV-1 Vaccines: A Dissertation." eScholarship@UMMS, 2015. https://escholarship.umassmed.edu/gsbs_diss/760.

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Despite 30 years of intensive research,an effective human immunodeficiency virus (HIV) vaccine still remains elusive. The desirable immune response capable of providing protection against HIV acquisition is still not clear. The accumulating evidence learned from a recent vaccine efficacy correlate study not only confirmed the importance of antibody responses, but also highlighted potential protective functions of antibodies with a broad repertoire of HIV-1 epitope specificities and a wide range of different antiviral mechanisms. This necessitates a deep understanding of the complexity and diversity of antibody responses elicited by HIV-1 vaccines. My dissertation characterizes antibody response profiles of HIV-1 Env antibodies elicited by several novel immunogens or different immunization regimens, in terms of magnitude, persistence, epitope specificity, binding affinity, and biological function. First, to overcome the challenge of studying polyclonal sera without established assays, we expanded a novel platform to isolate Env-specific Rabbit mAbs (RmAb) elicited by DNA prime-protein boost immunization. These RmAbs revealed diverse epitope specificity and cross-reactivity against multiple gp120 antigens from more than one subtype, and several had potent and broad neutralizing activities against sensitive Tier 1 viruses. Further, structural analysis of two V3 mAbs demonstrated that a slight shift of the V3 epitope might have a dramatic impact on their neutralization activity. All of these observations provide a useful tool to study the induction of a desired type of antibody by different immunogens or different immunization regimens. Since heavily glycosylated HIV Env protein is a critical component of an HIV vaccine, we wanted to determine the impact of the HIV Env-associated glycan shield on antibody responses. We were able to produce Env proteins with a selective and homogeneous pattern of N-glycosylation using a glycoengineered yeast cell line. Antigenicity of these novel Env proteins was examined by well-characterized human mAbs. Immunogenicity studies showed that they were immunogenic and elicited gp120- specific antibody responses. More significantly, sera elicited by glycan-modified gp120 protein immunogens revealed better neutralizing activities and increased diversity of epitopes compared to sera elicited by traditional gp120 produced in Chinese Hamster Ovary (CHO) cells. Further, we examined the impact of the delivery order of DNA and protein immunization on antibody responses. We found that DNA prime-protein boost induced a comparable level of Env-specific binding Abs at the peak immunogenicity point to codelivery of DNA. However, antibody responses from DNA prime-protein boost had high avidity and diverse specificities, which improved potency and breadth of neutralizing Abs against Tier 1 viruses. Our data indicate that DNA vaccine priming of the immune system is essential for generation of high-quality antibodies. Additionally, we determined the relative immunogenicity of gp120 and gp160 Env in the context of DNA prime-protein boost vaccination to induce high-quality antibody responses. Immunized sera from gp120 DNA primed animals, but not those primed with gp160 DNA, presented with distinct antibody repertoire specificities, a high magnitude of CD4 binding site-directed binding capabilities as well as neutralizing activities. We confirmed the importance of using the gp120 Env form at the DNA priming phase, which directly determined the quality of antibody response.
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Davis, Katie L. "Analysis of HIV-1 variable loop 3-specific neutralizing antibody responses by HIV-2/HIV-1 envelope chimeras." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2008. https://www.mhsl.uab.edu/dt/2009r/davis.pdf.

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Bernhard, Oliver. "Proteomic investigation of the HIV receptors CD4 and DC-SIGN/CD209 membrane protein interactions." Saarbrücken VDM Verlag Dr. Müller, 2004. http://d-nb.info/989278026/04.

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Costa, Matthew R. "FC Receptor-Mediated Activities of Env-Specific Monoclonal Antibodies Generated from Human Volunteers Receiving a DNA Prime-Protein Boost HIV Vaccine: A Dissertation." eScholarship@UMMS, 2010. http://escholarship.umassmed.edu/gsbs_diss/866.

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Human immunodeficiency type 1 (HIV-1) is able to elicit broadly potent neutralizing antibodies in a very small subset of individuals only after several years’ infection and as a result, vaccines that elicit these types of antibodies have been difficult to design. The RV144 trial showed that a moderate protection is possible, which may correlate with antibody dependent cellular cytotoxicity (ADCC) activity. Previous studies in the Lu lab demonstrated that in an HIV-1 vaccine phase I trial, DP6-001, a polyvalent Env DNA prime-protein boost formulation, could elicit potent and broadly reactive, gp120-specific antibodies with positive neutralization activities along with multiple Fc mediated effector functions. I developed a protocol for the production and analysis of HIV-1 Env-specific human monoclonal antibodies (mAbs) isolated from these DP6-001 vaccinees. By utilizing a labeled gp120 bait to isolate Env specific B cells, paired heavy and light chain immunoglobulin (Ig) genes were cloned and allowed for the production of monoclonal antibodies with specificity for gp120. By using this protocol, 13 isolated mAbs from four DP6-001 vaccinees showed broad binding activities to gp120 proteins of diverse subtypes, both autologous and heterologous to vaccine immunogens, with mostly conformational epitopes and a few V3 and C5 specific mAbs. Equally cross-reactive Fc-mediated functional activities, including ADCC and antibody dependent cellular phagocytosis (ADCP), were present with both immune sera and isolated mAbs, confirming the induction of non-neutralizing functional antibodies by the DNA prime- protein boost vaccination. Elicitation of broadly reactive mAbs by vaccination in healthy human volunteers confirms the value of the polyvalent formulation in this HIV-1 vaccine design.
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Costa, Matthew R. "FC Receptor-Mediated Activities of Env-Specific Monoclonal Antibodies Generated from Human Volunteers Receiving a DNA Prime-Protein Boost HIV Vaccine: A Dissertation." eScholarship@UMMS, 2016. https://escholarship.umassmed.edu/gsbs_diss/866.

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Human immunodeficiency type 1 (HIV-1) is able to elicit broadly potent neutralizing antibodies in a very small subset of individuals only after several years’ infection and as a result, vaccines that elicit these types of antibodies have been difficult to design. The RV144 trial showed that a moderate protection is possible, which may correlate with antibody dependent cellular cytotoxicity (ADCC) activity. Previous studies in the Lu lab demonstrated that in an HIV-1 vaccine phase I trial, DP6-001, a polyvalent Env DNA prime-protein boost formulation, could elicit potent and broadly reactive, gp120-specific antibodies with positive neutralization activities along with multiple Fc mediated effector functions. I developed a protocol for the production and analysis of HIV-1 Env-specific human monoclonal antibodies (mAbs) isolated from these DP6-001 vaccinees. By utilizing a labeled gp120 bait to isolate Env specific B cells, paired heavy and light chain immunoglobulin (Ig) genes were cloned and allowed for the production of monoclonal antibodies with specificity for gp120. By using this protocol, 13 isolated mAbs from four DP6-001 vaccinees showed broad binding activities to gp120 proteins of diverse subtypes, both autologous and heterologous to vaccine immunogens, with mostly conformational epitopes and a few V3 and C5 specific mAbs. Equally cross-reactive Fc-mediated functional activities, including ADCC and antibody dependent cellular phagocytosis (ADCP), were present with both immune sera and isolated mAbs, confirming the induction of non-neutralizing functional antibodies by the DNA prime- protein boost vaccination. Elicitation of broadly reactive mAbs by vaccination in healthy human volunteers confirms the value of the polyvalent formulation in this HIV-1 vaccine design.
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Connell, Bridgette Janine. "Development of a binding assay between the HIV-1 envelope protein (gp120) and coreceptors CCR5/CXCR4 by Surface Plasmon Resonance: Screening and optimization of viral entry inhibitors." Phd thesis, Université de Grenoble, 2012. http://tel.archives-ouvertes.fr/tel-01063128.

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La gp120 du VIH-1 se fixe aux héparane sulfate (HS) cellulaires, par le biais de la boucle V3 ce qui favorise l'infectivité virale. Cependant, une polyanion solubles (HS12), conjugués à CD4 (mCD4-HS12) a des propriétés antivirales et a montré in vitro une activité contre le VIH-1 à de concentrations nM. En raison de la complexité structurale des HS, le criblage d'oligosaccharides différenciellement sulfatés pour améliorer l'activité de la molécule serait trop difficile. En vue d'obtenir une molécule plus spécifique, de plus haute affinité et plus facile à produire, des peptides mimant les HS ont été synthétisés par nos collaborateurs. Notre but était de cribler ces peptides pour leur capacité à inhiber l'entrée de VIH-1. Nous avons mis en place une plateforme permettant d'immobiliser CCR5 et CXCR4 solubilisés sur des biocapteurs pour cribler des molécules qui inhibent la liaison de gp120-CD4 aux corécepteurs. Pour contrôler le processus de solubilisation, CXCL12, le ligand naturel de CXCR4, a été injecté sur CXCR4 immobilisé. Les affinités des isoformes CXCL12 (α et γ) pour CXCR4 ont été calculées dans les fourchettes de valeurs précédemment décrites avec des techniques différentes prouvant la fonctionnalité de notre système. Nous montrons pour la première fois que les HS régulent différemment les mécanismes de liaison de ces deux isoformes et nous proposons un nouveau mode d'action pour le domaine C-terminal particulièrement basique de CXCL12 γ vis-à-vis de CXCR4. Le système a ensuite été utilisé pour cribler la capacité d'inhibition des peptides mimétiques du HS. Chaque peptide, [S(XDXS)n] contient des acides aminés qui imitent les groupes hydroxyles, carboxyles et sulfates des HS. Le peptide contenant des résidus sulphotyrosines, une fois conjugué à mCD4 (mCD4-P3YSO3), montre un IC50 de l'ordre du nM, pour l'inhibition simultanée de la liaison de gp120 aux HS, à CD4, aux anticorps, aux corécepteurs ainsi que l'infection par VIH-1 in cellulo. Il constitue le premier inhibiteur bivalent de l'entrée qui cible à la fois les virus R5 et X4 et le concept d'un peptide mimétique des HS se prête à une analyse structurale et fonctionnelle de la liaison des chaînes HS aux protéines, une nouvelle technique dans ce domaine.
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Chagas, Kélem de Nardi. ""Avaliação do gene estrutural da proteína de ligação à lectina (MBL) e sua relação com a transmissão materno-fetal do HIV"." Universidade de São Paulo, 2005. http://www.teses.usp.br/teses/disponiveis/5/5144/tde-16112005-114946/.

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Avaliou-se a expressão do gene mbl2 em 79 crianças e suas mães HIV positivas com o objetivo de avaliar a sua influência na transmissão vertical. Os pacientes divididos em dois grupos: crianças HIV positivas e suas mães (n=18) e crianças HIV negativas e suas mães (n=61) foram avaliados pelo CH50 e AP50 (ensaios hemolíticos), dosagem e avaliação funcional da MBL, ativação da cascata terminal do complemento (ELISA) e o gene mbl2 (PCR). Os resultados não mostraram diferença significante entre os níveis séricos, atividade funcional e o gene da MBL entre os grupos, excluindo a sua influência sobre a transmissão materno-fetal do HIV
It was evaluated the mbl2 gene expression in 79 children and their HIV positive mothers with the aim to evaluate its influence on mother-to-child HIV. The patients were divided in two groups: HIV positive children and their mothers (n=18) and HIV negative children and their mothers (n=61) were evaluated by CH50 and AP50 (hemolytic assays); levels and functional MBL and terminal complement cascade (ELISA) and mbl2 gene (PCR). The results didn't show significant difference amons serum levels, functional activities and MBL gene between the groups, excluding the influence in the mother-to child HIV transmission.
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Diop, Amadou Gallo. "Mort neuronale et proteine-enveloppe (gp120) du virus de l'immunodeficience humaine." Limoges, 1988. http://www.theses.fr/1998LIMO306B.

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Xu, Xiaodong. "Expression and characterization of HIV-1 envelope protein." Thesis, University of Reading, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.500515.

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We postulated that gp120 and CD4 interaction might expose cryptic epitopes on gp120 that could be immunogenic and so widen the immunogenic response. A fusion protein of a C clade strain of HIV-1 (HIVCN54) gp120 and full-length human CD4 was constructed and expressed using a recombinant baculovirus system. The protein was purified, characterized and used to immunize rabbits. The antiserum generated had an expected anti-gp120 activity and demonstrated a higher capacity than a control serum raised to gp120 alone to block b12 binding, a marker of neutralization. A formal neutralization assay however did not detect neutralizing activity in the CD4-gp120CN54 antiserum. To enhance overall immunogenicity, a gp120CN54-FPV168 fusion protein was also expressed. FPV168 is a fowlpox virus protein. Although designed to elicit a stronger host immune response, the antiserum generated to gp120CN54-FPV168 had a weaker binding activity to gp120 than the antiserum generated to non-fused gp120CN54. A possible reason was protein instability associated with fusion to the N-terminus of FPV168. To ameliorate this problem, three gp120 fusion proteins with N-terminal truncated FPV168 were also constructed. The stability of these proteins was vastly improved but their performance as immunogens continued to be poorer than immunization with gp120 alone. Lastly, experiments describing an alternative strategy of immune enhancement based on targeting of gp120 or fragments of gp120 to antigen presenting cells via use of the human immunoglobulin Fc domain are presented. These were more successful and indicate a future direction that could yet produce an HIV-1 gp120 based immunogen capable of raising the antibody responses required as part of a successful vaccine.
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Books on the topic "HIV Envelope Protein gp160"

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Apatoff, Brian Richard. Trophic effects of neuroleukin on central neurons and antagonism by HIV envelope protein. 1988.

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Book chapters on the topic "HIV Envelope Protein gp160"

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Nilofer, Christina, Arumugam Mohanapriya, and Pandjassarame Kangueane. "HIV-1 Envelope (ENV) GP160 Trimer Protein Complex SPIKE as a Recombinant Macromolecular Assembly Vaccine Component Candidate: Current Opinion." In Global Virology II - HIV and NeuroAIDS, 939–51. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7290-6_36.

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Su, S. B., H. Ueda, O. M. Z. Howard, M. C. Grimm, W. Gong, F. W. Ruscetti, J. J. Oppenheim, and J. M. Wang. "Inhibition of the Expression and Function of Chemokine Receptors on Human CD4+ Leukocytes by HIV-1 Envelope Protein gp120." In Chemical Immunology and Allergy, 141–60. Basel: KARGER, 1999. http://dx.doi.org/10.1159/000058731.

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Kangueane, Pandjassarame. "HIV-1 GP160 (GP120/GP40) Trimer ENV Spike Protein." In Bioinformation Discovery, 173–81. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-95327-4_9.

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Jöbstl, B., M. Barcova, C. Speth, L. Kacani, and M. P. Dierich. "Role of Adenylate Cyclase and p70S6-Kinase in the Regulation of gp41 Envelope Protein-Induced IL-10 Expression in Human Monocytes." In HIV-Infekt, 40–43. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-642-59683-4_7.

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Mattiacio, Jonelle L., Matt Brewer, and Stephen Dewhurst. "Display of HIV-1 Envelope Protein on Lambda Phage Scaffold as a Vaccine Platform." In Methods in Molecular Biology, 245–53. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6869-5_14.

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Brenneman, D. E. "Peptide Intervention in Neuronal Death Caused by the HIV External Envelope Protein: Clinical Implications." In Neuropsychopharmacology, 722–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-74034-3_71.

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Lu, Xiaobin, Nancy Lewis, David Rekosh, and Marie-Louise Hammarskjöld. "A 5’ Splice Site is Essential for REV and REX Regulation of HIV Envelope Protein mRNA Expression." In Advances in Molecular Biology and Targeted Treatment for AIDS, 183–88. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-5928-9_16.

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Soulika, Athena. "Hiv Envelope Protein gp120." In xPharm: The Comprehensive Pharmacology Reference, 1. Elsevier, 2007. http://dx.doi.org/10.1016/b978-008055232-3.63892-9.

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"Studies Regarding the Interaction of the T4 (CD4) Molecule with the Envelope Protein gp120 of the Human Immunodeficiency Virus (HIV)." In Lymphocyte Activation and Differentiation, 445–48. De Gruyter, 1988. http://dx.doi.org/10.1515/9783110850253-064.

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"Modification of HIV-1 Envelope Glycoprotein to Enhance Immunogenicity." In Medicinal Protein Engineering, 161–86. CRC Press, 2008. http://dx.doi.org/10.1201/9781420007305-13.

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Conference papers on the topic "HIV Envelope Protein gp160"

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Valentin-Guillama, Gabriel, Yuriy Kucheryavykh, and Lilia Kucheryavykh. "Abstract 3454: HIV-1 envelope protein gp120 promotes glioma tumor growth through the Akt and MAP kinase pathways." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3454.

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Martin, Helen, Sebastian Reuter, Nina Dehzad, Iris Bellinghausen, Ina Haasler, Stephanie Korn, Joachim Saloga, Christian Becker, Roland Buhl, and Christian Taube. "Reduction Of Pulmonary Inflammation Through HIV-1 Envelope Protein GP120 In A Humanized Mouse Model Of Allergic Asthma Depends On Regulatory T Cells." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2772.

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