Relevant bibliographies by topics / Env ectodomain gp140

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  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'Env ectodomain gp140'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

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Journal articles on the topic "Env ectodomain gp140"

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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 (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 glycopr
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Earl, Patricia L., Wataru Sugiura, David C. Montefiori, et al. "Immunogenicity and Protective Efficacy of Oligomeric Human Immunodeficiency Virus Type 1 gp140." Journal of Virology 75, no. 2 (2001): 645–53. http://dx.doi.org/10.1128/jvi.75.2.645-653.2001.

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ABSTRACT The biologically active form of the human immunodeficiency virus type 1 (HIV-1) envelope (Env) glycoprotein is oligomeric. We previously described a soluble HIV-1 IIIB Env protein, gp140, with a stable oligomeric structure composed of uncleaved gp120 linked to the ectodomain of gp41 (P. L. Earl, C. C. Broder, D. Long, S. A. Lee, J. Peterson, S. Chakrabarti, R. W. Doms, and B. Moss, J. Virol. 68:3015–3026, 1994). Here we compared the antibody responses of rabbits to gp120 and gp140 that had been produced and purified in an identical manner. The gp140 antisera exhibited enhanced cross-r
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Sanders, Rogier W., Mika Vesanen, Norbert Schuelke, et al. "Stabilization of the Soluble, Cleaved, Trimeric Form of the Envelope Glycoprotein Complex of Human Immunodeficiency Virus Type 1." Journal of Virology 76, no. 17 (2002): 8875–89. http://dx.doi.org/10.1128/jvi.76.17.8875-8889.2002.

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ABSTRACT The envelope glycoprotein (Env) complex of human immunodeficiency virus type 1 has evolved a structure that is minimally immunogenic while retaining its natural function of receptor-mediated virus-cell fusion. The Env complex is trimeric; its six individual subunits (three gp120 and three gp41 subunits) are associated by relatively weak, noncovalent interactions. The induction of neutralizing antibodies after vaccination with individual Env subunits has proven very difficult, probably because they are inadequate mimics of the native complex. Our hypothesis is that a stable form of the
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Cai, Yongfei, Selen Karaca-Griffin, Jia Chen, et al. "Antigenicity-defined conformations of an extremely neutralization-resistant HIV-1 envelope spike." Proceedings of the National Academy of Sciences 114, no. 17 (2017): 4477–82. http://dx.doi.org/10.1073/pnas.1700634114.

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The extraordinary genetic diversity of the HIV-1 envelope spike [Env; trimeric (gp160)3, cleaved to (gp120/gp41)3] poses challenges for vaccine development. Envs of different clinical isolates exhibit different sensitivities to antibody-mediated neutralization. Envs of difficult-to-neutralize viruses are thought to be more stable and conformationally homogeneous trimers than those of easy-to-neutralize viruses, thereby providing more effective concealment of conserved, functionally critical sites. In this study we have characterized the antigenic properties of an Env derived from one of the mo
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Ringe, Rajesh P., Anila Yasmeen, Gabriel Ozorowski, et al. "Influences on the Design and Purification of Soluble, Recombinant Native-Like HIV-1 Envelope Glycoprotein Trimers." Journal of Virology 89, no. 23 (2015): 12189–210. http://dx.doi.org/10.1128/jvi.01768-15.

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ABSTRACTWe have investigated factors that influence the production of native-like soluble, recombinant trimers based on theenvgenes of two isolates of human immunodeficiency virus type 1 (HIV-1), specifically 92UG037.8 (clade A) and CZA97.012 (clade C). When the recombinant trimers based on theenvgenes of isolates 92UG037.8 and CZA97.012 were made according to the SOSIP.664 design and purified by affinity chromatography using broadly neutralizing antibodies (bNAbs) against quaternary epitopes (PGT145 and PGT151, respectively), the resulting trimers are highly stable and they are fully native-l
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Doranz, Benjamin J., Sarah S. W. Baik, and Robert W. Doms. "Use of a gp120 Binding Assay To Dissect the Requirements and Kinetics of Human Immunodeficiency Virus Fusion Events." Journal of Virology 73, no. 12 (1999): 10346–58. http://dx.doi.org/10.1128/jvi.73.12.10346-10358.1999.

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ABSTRACT Binding of the extracellular subunit of human immunodeficiency type 1 (HIV-1) envelope (Env) glycoprotein (gp120) to CD4 triggers the induction or exposure of a highly conserved coreceptor binding site in gp120 that helps mediate membrane fusion. Characterizing the structural features involved in gp120-coreceptor binding and the conditions under which binding occurs is important for understanding the fusion process, the evolution of pathogenic strains in vivo, the identification of novel anti-HIV compounds, and the development of HIV vaccines that utilize triggered structures of Env.
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Kalia, Vandana, Surojit Sarkar, Phalguni Gupta, and Ronald C. Montelaro. "Antibody Neutralization Escape Mediated by Point Mutations in the Intracytoplasmic Tail of Human Immunodeficiency Virus Type 1 gp41." Journal of Virology 79, no. 4 (2005): 2097–107. http://dx.doi.org/10.1128/jvi.79.4.2097-2107.2005.

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ABSTRACT The persistence of human immunodeficiency virus type 1 (HIV-1) infection in the presence of robust host immunity has been associated in part with variation in viral envelope proteins leading to antigenic variation and escape from neutralizing antibodies. Previous studies of natural neutralization escape mutants have predominantly focused on gp120 and gp41 ectodomain sequence variations that alter antibody binding via changes in conformation or glycosylation pattern of the Env, likely due to the immune pressure exerted on the exposed ectodomain component of the glycoprotein. Here, we s
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8

Rao, Mangala, Kristina Peachman, Ousman Jobe, et al. "Induction of linear and conformational V2-specific antibodies using HIV-1 gp145 clade B envelope protein as the immunogen (P4505)." Journal of Immunology 190, no. 1_Supplement (2013): 179.15. http://dx.doi.org/10.4049/jimmunol.190.supp.179.15.

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Abstract TThe potential importance of binding antibodies (Abs) in preventing HIV-1 acquisition was recently demonstrated by the case control analysis of the RV144 phase III HIV-1 vaccine trial, which showed that binding Abs to a gp70 scaffolded V1V2 loop of gp120 correlated inversely with infection. We examined if immunization with a HIV-1 env trimer in the absence of any priming vector could induce functional V2-specific Abs. The clade B HIV-1 gp145 env protein consisting of gp120, gp41 ectodomain, and MPER, trimerized with foldon was expressed in 293F cells and purified. The protein adjuvant
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Steckbeck, Jonathan D., Anne-Sophie Kuhlmann, and Ronald C. Montelaro. "C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic." Journal of General Virology 94, no. 1 (2013): 1–19. http://dx.doi.org/10.1099/vir.0.046508-0.

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The human immunodeficiency virus (HIV) and acquired immunodeficiency syndrome (AIDS) pandemic is amongst the most important current worldwide public health threats. While much research has been focused on AIDS vaccines that target the surface viral envelope (Env) protein, including gp120 and the gp41 ectodomain, the C-terminal tail (CTT) of gp41 has received relatively little attention. Despite early studies highlighting the immunogenicity of a particular CTT sequence, the CTT has been classically portrayed as a type I membrane protein limited to functioning in Env trafficking and virion incor
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Kwong, Peter. "HIV-1 Env structure and vaccine design." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C117. http://dx.doi.org/10.1107/s2053273314098829.

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Roughly one third of the HIV-1 genome is devoted to the HIV-1 envelope (Env) glycoprotein spike, which comprises three gp120 and three gp41 subunits. Structural characterization of the HIV-1 Env by electron microscopy, NMR, and X-ray crystallography reveals considerable conformational alterations, not only between trimeric ground state, CD4 receptor-bound conformation, and postfusion conformation of the spike, but also between monomeric and trimeric configurations of the subunits as well as between free- and antibody–bound states. One important structure, however, that of the prefusion HIV-1 s
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Dissertations / Theses on the topic "Env ectodomain gp140"

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Malladi, Sameer Kumar. "HIV-1 and SARS-CoV-2 immunogen design." Thesis, 2020. https://etd.iisc.ac.in/handle/2005/5595.

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Human Immunodeficiency Virus (HIV-1) is the aetiologic agent of AIDS. Presently there are ~38 million HIV-1 infected individuals worldwide and ~1 million deaths in 2019. Since its discovery, the quest for vaccine candidate for HIV-1 is alive, yet no effective vaccine exists till date. HIV-1 viral displayed Envelope (Env) protein is the primary viral target of the humoral immune system and is thus an obvious vaccine candidate. The historic RV144 HIV-1 clinical trial resulted in a modest efficacy of the gp120 clade B/E vaccine candidate and renewed hope in finding a HIV-1 vaccine. However, monom
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