Relevant bibliographies by topics / HIV Envelope Protein gp120

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'HIV Envelope Protein gp120'

Author: Grafiati
Published: 4 June 2021
Last updated: 5 February 2022

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Journal articles on the topic "HIV Envelope Protein gp120"

1

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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2

Binley, James M., Rogier W. Sanders, Brian Clas, Norbert Schuelke, Aditi Master, Yong Guo, Francis Kajumo, et al. "A Recombinant Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Complex Stabilized by an Intermolecular Disulfide Bond between the gp120 and gp41 Subunits Is an Antigenic Mimic of the Trimeric Virion-Associated Structure." Journal of Virology 74, no. 2 (January 15, 2000): 627–43. http://dx.doi.org/10.1128/jvi.74.2.627-643.2000.

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ABSTRACT The few antibodies that can potently neutralize human immunodeficiency virus type 1 (HIV-1) recognize the limited number of envelope glycoprotein epitopes exposed on infectious virions. These native envelope glycoprotein complexes comprise three gp120 subunits noncovalently and weakly associated with three gp41 moieties. The individual subunits induce neutralizing antibodies inefficiently but raise many nonneutralizing antibodies. Consequently, recombinant envelope glycoproteins do not elicit strong antiviral antibody responses, particularly against primary HIV-1 isolates. To try to develop recombinant proteins that are better antigenic mimics of the native envelope glycoprotein complex, we have introduced a disulfide bond between the C-terminal region of gp120 and the immunodominant segment of the gp41 ectodomain. The resulting gp140 protein is processed efficiently, producing a properly folded envelope glycoprotein complex. The association of gp120 with gp41 is now stabilized by the supplementary intermolecular disulfide bond, which forms with approximately 50% efficiency. The gp140 protein has antigenic properties which resemble those of the virion-associated complex. This type of gp140 protein may be worth evaluating for immunogenicity as a component of a multivalent HIV-1 vaccine.
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3

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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4

Klinman, D. M., K. W. Higgins, and J. Conover. "Sequential immunizations with rgp120s from independent isolates of human immunodeficiency virus type 1 induce the preferential expansion of broadly crossreactive B cells." Journal of Experimental Medicine 173, no. 4 (April 1, 1991): 881–87. http://dx.doi.org/10.1084/jem.173.4.881.

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The gp120 envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) is a dominant target against which the host's humoral immune response is directed. Unfortunately, gp120 proteins from different isolates of HIV are antigenically distinct, complicating the use of the envelope glycoprotein in vaccines designed to prevent acquired immunodeficiency syndrome. Using an enzyme-linked immunosorbent spot assay (ELISA), BALB/c mice immunized and boosted with recombinant purified gp120 were studied at the single cell level for their humoral immune response to HIV-1 envelope proteins. Approximately 90% of responding B cells produced antibodies reactive with the immunizing form of gp120 but not with gp120s from other strains of HIV. A novel sandwich ELISA was then used to analyze the frequency with which individual in vivo activated B cells produced antibodies that crossreacted with heterologous gp120s. Repeated immunizations with a single gp120 or with a mixture of different gp120s resulted in the activation of primarily mono-specific (noncrossreactive) B cells. In contrast, the sequential immunization of mice with recombinant purified envelope proteins from different strains of HIV (IIIB, SF2, and Zr6) induced the selective expansion of B cells producing highly crossreactive antibodies.
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Beddows, Simon, Norbert Schülke, Marc Kirschner, Kelly Barnes, Michael Franti, Elizabeth Michael, Thomas Ketas, et al. "Evaluating the Immunogenicity of a Disulfide-Stabilized, Cleaved, Trimeric Form of the Envelope Glycoprotein Complex of Human Immunodeficiency Virus Type 1." Journal of Virology 79, no. 14 (July 2005): 8812–27. http://dx.doi.org/10.1128/jvi.79.14.8812-8827.2005.

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ABSTRACT The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) complex comprises three gp120 exterior glycoproteins each noncovalently linked to a gp41 transmembrane glycoprotein. Monomeric gp120 proteins can elicit antibodies capable of neutralizing atypically sensitive test viruses in vitro, but these antibodies are ineffective against representative primary isolates and the gp120 vaccines failed to provide protection against HIV-1 transmission in vivo. Alternative approaches to raising neutralizing antibodies are therefore being pursued. Here we report on the antibody responses generated in rabbits against a soluble, cleaved, trimeric form of HIV-1JR-FL Env. In this construct, the gp120 and gp41 moieties are covalently linked by an intermolecular disulfide bond (SOS gp140), and an I559P substitution has been added to stabilize gp41-gp41 interactions (SOSIP gp140). We investigated the value of DNA priming and compared the use of membrane-bound and soluble priming antigens and of repeat boosting with soluble and particulate protein antigen. Compared to monomeric gp120, SOSIP gp140 trimers elicited approximately threefold lower titers of anti-gp120 antibodies. Priming with DNA encoding a membrane-bound form of the SOS gp140 protein, followed by several immunizations with soluble SOSIP gp140 trimers, resulted in antibodies capable of neutralizing sensitive strains at high titers. A subset of these sera also neutralized, at lower titers, HIV-1JR-FL and some other primary isolates in pseudovirus and/or whole-virus assays. Neutralization of these viruses was immunoglobulin mediated and was predominantly caused by antibodies to gp120 epitopes, but not the V3 region.
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Schülke, Norbert, Mika S. Vesanen, Rogier W. Sanders, Ping Zhu, Min Lu, Deborah J. Anselma, Anthony R. Villa, et al. "Oligomeric and Conformational Properties of a Proteolytically Mature, Disulfide-Stabilized Human Immunodeficiency Virus Type 1 gp140 Envelope Glycoprotein." Journal of Virology 76, no. 15 (August 1, 2002): 7760–76. http://dx.doi.org/10.1128/jvi.76.15.7760-7776.2002.

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ABSTRACT We describe the further properties of a protein, designated SOS gp140, wherein the association of the gp120 and gp41 subunits of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein is stabilized by an intersubunit disulfide bond. HIV-1JR-FL SOS gp140, proteolytically uncleaved gp140 (gp140UNC), and gp120 were expressed in stably transfected Chinese hamster ovary cells and analyzed for antigenic and structural properties before and after purification. Compared with gp140UNC, SOS gp140 reacted more strongly in surface plasmon resonance and radioimmunoprecipitation assays with the neutralizing monoclonal antibodies (MAbs) 2G12 (anti-gp120), 2F5 (anti-gp41), and 17b (to a CD4-induced epitope that overlaps the CCR5-binding site). In contrast, gp140UNC displayed the greater reactivity with nonneutralizing anti-gp120 and anti-gp41 MAbs. Immunoelectron microscopy studies suggested a model for SOS gp140 wherein the gp41 ectodomain (gp41ECTO) occludes the “nonneutralizing” face of gp120, consistent with the antigenic properties of this protein. We also report the application of Blue Native polyacrylamide gel electrophoresis (BN-PAGE), a high-resolution molecular sizing method, to the study of viral envelope proteins. BN-PAGE and other biophysical studies demonstrated that SOS gp140 was monomeric, whereas gp140UNC comprised a mixture of noncovalently associated and disulfide-linked dimers, trimers, and tetramers. The oligomeric and conformational properties of SOS gp140 and gp140UNC were largely unaffected by purification. An uncleaved gp140 protein containing the SOS cysteine mutations (SOS gp140UNC) was also oligomeric. Surprisingly, variable-loop-deleted SOS gp140 proteins were expressed (although not yet purified) as cleaved, noncovalently associated oligomers that were significantly more stable than the full-length protein. Overall, our findings have relevance for rational vaccine design.
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Christina Nilofer and Arumugam Mohanapriya. "Insights from the interfaces of HIV-1 envelope (ENV) trimer viral protein GP160 (GP120-GP41)." International Journal of Research in Pharmaceutical Sciences 12, no. 1 (January 6, 2021): 513–22. http://dx.doi.org/10.26452/ijrps.v12i1.4111.

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The Human Immunodeficiency Virus (HIV-1) type 1 viral protein is a life threatening virus causing HIV/AIDS in infected humans. The HIV-1 envelope (ENV) trimer glycoprotein GP160 (GP120-GP41) is gaining attention in recent years as a potential vaccine candidate for HIV-1/AIDS. However, the sequence variation and charge polarity at the interacting sites across clades is a shortcoming faced in the development of an effective HIV-1 vaccine. We analyzed the interfaces in terms of its interface area, interface size, and interface energies (van der Waals, hydrogen bonds, and electrostatics). The interfaces were divided as dominant (≥60%) and subdominant (<60%) based on van der Waals contribution to total energies. 88% of GP120 and 74% of GP41 interfaces are highly pronounced with van der Waals energy having large interfaces with interface size (98±65 (GP120) and 73±65 (GP41)) and interface area (882±1166Å2 (GP120) and 921±1288Å2 (GP41)). Nevertheless, 12% of GP120 and 26% of GP41 interfaces have subdominant van der Waals energies having small interfaces with interface size (58±20 (GP120) and 27±9 (GP41)) and interface area (581±1605Å2 (GP120) and 483±896Å2 (GP41)). It was interesting to observe GP41 small interfaces with subdominant van der Waals are stabilized by electrostatics (r2=0.63) without hydrogen bonds (r2=0). However, GP120 small interfaces were found to have two fold more hydrogen bonds (r2=0.59) than electrostatics (r2=0.20). Therefore, our previous finding stating that small protein-protein interfaces rich in electrostatics holds true in case of GP41 whereas not with GP120 protein interfaces.
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Stansell, Elizabeth, and Ronald C. Desrosiers. "Fundamental Difference in the Content of High-Mannose Carbohydrate in the HIV-1 and HIV-2 Lineages." Journal of Virology 84, no. 18 (July 7, 2010): 8998–9009. http://dx.doi.org/10.1128/jvi.00996-10.

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ABSTRACT The virus-encoded envelope proteins of human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) typically contain 26 to 30 sites for N-linked carbohydrate attachment. N-linked carbohydrate can be of three major types: high mannose, complex, or hybrid. The lectin proteins from Galanthus nivalis (GNA) and Hippeastrum hybrid (HHA), which specifically bind high-mannose carbohydrate, were found to potently inhibit the replication of a pathogenic cloned SIV from rhesus macaques, SIVmac239. Passage of SIVmac239 in the presence of escalating concentrations of GNA and HHA yielded a lectin-resistant virus population that uniformly eliminated three sites (of 26 total) for N-linked carbohydrate attachment (Asn-X-Ser or Asn-X-Thr) in the envelope protein. Two of these sites were in the gp120 surface subunit of the envelope protein (Asn244 and Asn460), and one site was in the envelope gp41 transmembrane protein (Asn625). Maximal resistance to GNA and HHA in a spreading infection was conferred to cloned variants that lacked all three sites in combination. Variant SIV gp120s exhibited dramatically decreased capacity for binding GNA compared to SIVmac239 gp120 in an enzyme-linked immunosorbent assay (ELISA). Purified gp120s from six independent HIV type 1 (HIV-1) isolates and two SIV isolates from chimpanzees (SIVcpz) consistently bound GNA in ELISA at 3- to 10-fold-higher levels than gp120s from five SIV isolates from rhesus macaques or sooty mangabeys (SIVmac/sm) and four HIV-2 isolates. Thus, our data indicate that characteristic high-mannose carbohydrate contents have been retained in the cross-species transmission lineages for SIVcpz-HIV-1 (high), SIVsm-SIVmac (low), and SIVsm-HIV-2 (low).
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Balasubramanian, Anuradha, Ramesh K. Ganju, and Jerome E. Groopman. "HCV and HIV Envelope Proteins Co-Operatively Induce Fas-Mediated Apoptosis Via a Novel Stat1 Signaling Pathway." Blood 104, no. 11 (November 16, 2004): 604. http://dx.doi.org/10.1182/blood.v104.11.604.604.

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Abstract Hepatitis C virus (HCV) co-infects approximately 40% of patients with human immunodeficiency virus (HIV). HCV/HIV co-infected patients often have progressive liver disease that can lead to cirrhosis and death. We observed that hepatocytes exposed to HCV and HIV envelope proteins undergo apoptosis via an ‘innocent bystander’ mechanism due to cell surface binding of viral proteins independent of direct viral infection. HCV envelope protein E2 (1.5 nM) and HIV envelope protein gp120 (0.8 nM) derived from M-tropic and T-tropic viruses induce significant apoptosis in both hepatocytic cell lines and primary hepatocytes, while either of these viral proteins alone does not. Now, we have elucidated the signaling mechanisms that mediate this effect. HCV-E2 and HIV-gp120 were found to significantly upregulate Fas ligand (FasL). We then examined the Stat family of proteins known to participate in FasL and apoptotic pathways. We observed an increased DNA binding activity of Stat1 upon HCV-E2 and HIV-gp120 stimulation. Furthermore, overexpression of wild type Stat1αincreased apoptosis and FasL expression in HepG2 cells, whereas a C-terminal domain deleted mutant, Stat1β, decreased HCV-E2 and HIV-gp120 mediated apoptosis and FasL upregulation. Overexpression of Stat1αand Stat1β in primary hepatocytes confirmed that Stat1αenhanced apoptosis upon HCV-E2 and HIV-gp120 treatment. We observed a tyrosine dependent activation of Stat1 and a subsequent serine phosphorylation of Stat1. TYK2, lyn kinase, RAFTK and MAP kinases were activated upstream of Stat1. In addition, Stat1 associated with the death domain-containing adapter protein TRADD. TRADD is known to induce inflammatory signaling through the NFκB pathway. Here, the association of Stat1 with TRADD would reduce the availability of TRADD to induce NFκB. Thus, Stat1 sequestration of downstream apoptotic signaling molecules would block the host inflammatory response. Further characterization of Fas-mediated apoptosis revealed that caspase 3 and caspase 7 were activated following HCV-E2 and HIV-gp120 stimulation. However, we were not able to detect significant activity of either caspase 8 or caspase 9. We also found a loss in mitochondrial membrane potential upon HCV-E2 and HIV-gp120 stimulation, which leads to the release of cytochrome C and AIF into the cytosol. Taken together, these studies indicate that the viral proteins of HCV and HIV co-operate in causing the apoptosis of hepatocytes, independent of direct infection, by induction of novel Stat1 downstream signaling pathways at the expense of a normal host inflammatory response.
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Anand, Appakkudal R., Anil Prasad, Ritu R. Bradley, Yadwinder S. Deol, Tirumuru Nagaraja, Xianghui Ren, Ernest F. Terwilliger, and Ramesh K. Ganju. "HIV-1 gp120-induced migration of dendritic cells is regulated by a novel kinase cascade involving Pyk2, p38 MAP kinase, and LSP1." Blood 114, no. 17 (October 22, 2009): 3588–600. http://dx.doi.org/10.1182/blood-2009-02-206342.

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AbstractTargeting dendritic cell (DC) functions such as migration is a pivotal mechanism used by HIV-1 to disseminate within the host. The HIV-1 envelope protein is the most important of the virally encoded proteins that exploits the migratory capacity of DCs. In the present study, we elucidated the signaling machinery involved in migration of immature DCs (iDCs) in response to HIV-1 envelope protein. We observed that M-tropic HIV-1 glycoprotein 120 (gp120) induces phosphorylation of the nonreceptor tyrosine kinase, Pyk2. Inhibition of Pyk2 activity using a pharmacologic inhibitor, kinase-inactive Pyk2 mutant, and Pyk2-specific small interfering RNA blocked gp120-induced chemotaxis, confirming the role of Pyk2 in iDC migration. In addition, we also illustrated the importance of Pyk2 in iDC migration induced by virion-associated envelope protein, using aldithriol-2–inactivated M-tropic HIV-1 virus. Further analysis of the downstream signaling mechanisms involved in gp120-induced migration revealed that Pyk2 activates p38 mitogen-activated protein kinase, which in turn activates the F-actin–binding protein, leukocyte-specific protein 1, and enhances its association with actin. Taken together, our studies provide an insight into a novel gp120-mediated pathway that regulates DC chemotaxis and contributes to the dissemination of HIV-1 within an infected person.
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Dissertations / Theses on the topic "HIV Envelope Protein gp120"

1

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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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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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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5

Jones, Adam. "The biological characteristics of gp120 envelope proteins derived from laboratory adapted HIV-1←I←I←I←B←/←L←A←I, and HIV-1 infected brain and lymphoid tissues." Thesis, University of Reading, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.388583.

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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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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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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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Books on the topic "HIV Envelope Protein gp120"

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Sjolander, Sigrid. Studies on immune responses to the HIV envelope glycoprotein gp120. Uppsala: Sveriges Lantbruksuniversitet, 1995.

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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 gp120"

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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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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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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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Valenzuela, Agustin, Julià Blanco, Christian Callebaut, Etienne Jacotot, Carmen Lluis, Ara G. Hovanessian, and Rafael Franco. "HIV-1 Envelope gp120 and Viral Particles Block Adenosine Deaminase Binding to Human CD26." In Advances in Experimental Medicine and Biology, 185–92. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-9613-1_24.

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Bennett, Barbara A., Daniel E. Rusyniak, and Charlotte K. Hollingsworth. "HIV-1 Coat Protein GP120 Induces Neuronal Injury to Cultured Dopamine Cells." In Neurodegenerative Diseases, 55–62. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4899-0209-2_8.

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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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Ray, Sujay, and Arundhati Banerjee. "Interactions with Human CD4 Protein Leads to Helix-to-Coil Transition in HIV-gp120 Aiding CCR5 Attachment and Viral Entry: An In Silico Structural Biology Approach for AIDS." In Lecture Notes in Electrical Engineering, 3–11. New Delhi: Springer India, 2016. http://dx.doi.org/10.1007/978-81-322-3589-7_1.

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Conference papers on the topic "HIV Envelope Protein gp120"

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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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Valentin-Guillama, Gabriel, Sheila Lopez, Jose Perez, Luis Cubano, Natalia Chorna, Jeffrey Harrison, Nawal Boukli, and Lilia Kucheryavykh. "Abstract 5343: The HIV shell protein Gp120 stimulates U87 glioma cell proliferation through the activation of glycolysis." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-5343.

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Pandey, Vishnudatt, Gargi Tiwari, Vijaya Shri Mall, Rakesh Kumar Tiwari, and Rajendra Prasad Ojha. "Interaction between gp120 and ligand in HIV-1 env protein: Molecular dynamics simulations and binding free energy calculations." In ADVANCES IN BASIC SCIENCE (ICABS 2019). AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5122491.

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