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Journal articles on the topic 'Env ectodomain gp140'

Author: Grafiati

Published: 6 September 2023

Last updated: 31 July 2025

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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 (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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2

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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3

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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4

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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5

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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6

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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10

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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11

Edwards, Terri G., Stéphanie Wyss, Jacqueline D. Reeves, et al. "Truncation of the Cytoplasmic Domain Induces Exposure of Conserved Regions in the Ectodomain of Human Immunodeficiency Virus Type 1 Envelope Protein." Journal of Virology 76, no. 6 (2002): 2683–91. http://dx.doi.org/10.1128/jvi.76.6.2683-2691.2002.

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ABSTRACT We have described a CD4-independent variant of HXBc2, termed 8x, that binds directly to CXCR4 and mediates CD4-independent virus infection. Determinants for CD4 independence map to residues in the V3 and V4-C4 domains together with a single nucleotide deletion in the transmembrane domain which introduces a frameshift (FS) at position 706. This FS results in a truncated cytoplasmic domain of 27 amino acids. We demonstrate here that while introduction of the 8x FS mutation into heterologous R5, X4, or R5X4 Env proteins did not impart CD4 independence, it did affect the conformation of t

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12

McInerney, Tracey L., Walid El Ahmar, Bruce E. Kemp, and Pantelis Poumbourios. "Mutation-Directed Chemical Cross-Linking of Human Immunodeficiency Virus Type 1 gp41 Oligomers." Journal of Virology 72, no. 2 (1998): 1523–33. http://dx.doi.org/10.1128/jvi.72.2.1523-1533.1998.

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ABSTRACT The human immunodeficiency virus type 1 transmembrane protein gp41 oligomer anchors the attachment protein, gp120, to the viral envelope and mediates viral envelope-cell membrane fusion following gp120-CD4 receptor-chemokine coreceptor binding. We have used mutation-directed chemical cross-linking with bis(sulfosuccinimidyl)suberate (BS3) to investigate the architecture of the gp41 oligomer. Treatment of gp41 with BS3 generates a ladder of four bands on sodium dodecyl sulfate-polyacrylamide gels, corresponding to monomers, dimers, trimers, and tetramers. By systematically replacing gp

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13

Labrosse, Béatrice, Carole Treboute, and Marc Alizon. "Sensitivity to a Nonpeptidic Compound (RPR103611) Blocking Human Immunodeficiency Virus Type 1 Env-Mediated Fusion Depends on Sequence and Accessibility of the gp41 Loop Region." Journal of Virology 74, no. 5 (2000): 2142–50. http://dx.doi.org/10.1128/jvi.74.5.2142-2150.2000.

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ABSTRACT The triterpene RPR103611 is an efficient inhibitor of membrane fusion mediated by the envelope proteins (Env, gp120-gp41) of CXCR4-dependent (X4) human immunodeficiency virus type 1 (HIV-1) strains, such as HIV-1LAI (LAI). Other X4 strains, such as HIV-1NDK (NDK), and CCR5-dependent (R5) HIV-1 strains, such as HIV-1ADA (ADA), were totally resistant to RPR103611. Analysis of chimeric LAI-NDK Env proteins identified a fragment of the NDK gp41 ectodomain determining drug resistance. A single difference at position 91, leucine in LAI and histidine in NDK, apparently accounted for their se

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McKenna, Philip M., Pyone Pyone Aye, Bernhard Dietzschold, et al. "Immunogenicity Study of Glycoprotein-Deficient Rabies Virus Expressing Simian/Human Immunodeficiency Virus SHIV89.6P Envelope in a Rhesus Macaque." Journal of Virology 78, no. 24 (2004): 13455–59. http://dx.doi.org/10.1128/jvi.78.24.13455-13459.2004.

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ABSTRACT Rabies virus (RV) has recently been developed as a novel vaccine candidate for human immunodeficiency virus type 1 (HIV-1). The RV glycoprotein (G) can be functionally replaced by HIV-1 envelope glycoprotein (Env) if the gp160 cytoplasmic domain (CD) of HIV-1 Env is replaced by that of RV G. Here, we describe a pilot study of the in vivo replication and immunogenicity of an RV with a deletion of G (ΔG) expressing a simian/human immunodeficiency virus SHIV89.6P Env ectodomain and transmembrane domain fused to the RV G CD (ΔG-89.6P-RVG) in a rhesus macaque. An animal vaccinated with ΔG-

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15

Finnegan, Catherine M., Werner Berg, George K. Lewis, and Anthony L. DeVico. "Antigenic Properties of the Human Immunodeficiency Virus Transmembrane Glycoprotein during Cell-Cell Fusion." Journal of Virology 76, no. 23 (2002): 12123–34. http://dx.doi.org/10.1128/jvi.76.23.12123-12134.2002.

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ABSTRACT Human immunodeficiency virus (HIV) entry is triggered by interactions between a pair of heptad repeats in the gp41 ectodomain, which convert a prehairpin gp41 trimer into a fusogenic three-hairpin bundle. Here we examined the disposition and antigenic nature of these structures during the HIV-mediated fusion of HeLa cells expressing either HIVHXB2 envelope (Env cells) or CXCR4 and CD4 (target cells). Cell-cell fusion, indicated by cytoplasmic dye transfer, was allowed to progress for various lengths of time and then arrested. Fusion intermediates were then examined for reactivity with

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16

York, Joanne, Kathryn E. Follis, Meg Trahey, Phillipe N. Nyambi, Susan Zolla-Pazner, and Jack H. Nunberg. "Antibody Binding and Neutralization of Primary and T-Cell Line-Adapted Isolates of Human Immunodeficiency Virus Type 1." Journal of Virology 75, no. 6 (2001): 2741–52. http://dx.doi.org/10.1128/jvi.75.6.2741-2752.2001.

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ABSTRACT The relative resistance of human immunodeficiency virus type 1 (HIV-1) primary isolates (PIs) to neutralization by a wide range of antibodies remains a theoretical and practical barrier to the development of an effective HIV vaccine. One model to account for the differential neutralization sensitivity between Pls and laboratory (or T-cell line-adapted [TCLA]) strains of HIV suggests that the envelope protein (Env) complex is made more accessible to antibody binding as a consequence of adaptation to growth in established cell lines. Here, we revisit this question using genetically rela

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17

Labrosse, Béatrice, Laurence Morand-Joubert, Armelle Goubard, et al. "Role of the Envelope Genetic Context in the Development of Enfuvirtide Resistance in Human Immunodeficiency Virus Type 1-Infected Patients." Journal of Virology 80, no. 17 (2006): 8807–19. http://dx.doi.org/10.1128/jvi.02706-05.

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ABSTRACT Acquired human immunodeficiency virus type 1(HIV-1) resistance to the fusion inhibitor enfuvirtide (ENF) is primarily associated with mutations within the highly conserved first heptad repeat (HR1) region of gp41. Viral env sequences, however, are remarkably variable, and the envelope genetic background could have an important impact on optimal expression of HR1 mutations. We have examined the genetic evolution of env sequences, ENF susceptibility, and Env replicative capacity in patients failing ENF treatment. Sequential plasma-derived virus populations, obtained from six patients in

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18

BAHBOUHI, Bouchaib, Nabil Georges SEIDAH та Elmostafa BAHRAOUI. "Replication of HIV-1 viruses in the presence of the Portland α1-antitrypsin variant (α1-PDX) inhibitor". Biochemical Journal 360, № 1 (2001): 127–34. http://dx.doi.org/10.1042/bj3600127.

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The Portland α1-antitrypsin variant (α1-PDX) inhibits gp160 cleavage into gp120 and gp41 by different prohormone convertases (PCs) including furin, PC5 and PC7. Jurkat cells stably transfected with this inhibitor (J-PDX cells) and, as controls, Jurkat cells transfected with the empty vector (J-pcDNA3) were tested for their susceptibility to HIV-1 infection. We found that HIV-1 replication was significantly impaired in J-PDX cells. However, the analysis of the infectivity of HIV-1 viruses produced in J-PDX cells on different days during the infection indicated that they recovered infectivity st

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Bär, Séverine, and Marc Alizon. "Role of the Ectodomain of the gp41 Transmembrane Envelope Protein of Human Immunodeficiency Virus Type 1 in Late Steps of the Membrane Fusion Process." Journal of Virology 78, no. 2 (2004): 811–20. http://dx.doi.org/10.1128/jvi.78.2.811-820.2004.

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ABSTRACT The membrane fusion process mediated by the gp41 transmembrane envelope glycoprotein of the human immunodeficiency virus type 1 (HIV-1) was addressed by a flow cytometry assay detecting exchanges of fluorescent membrane probes (DiI and DiO) between cells expressing the HIV-1 envelope proteins (Env) and target cells. Double-fluorescent cells were detected when target cells expressed the type of chemokine receptor, CXCR4 or CCR5, matching the type of gp120 surface envelope protein, X4 or R5, respectively. Background levels of double-fluorescent cells were observed when the gp120-recepto

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Desmezieres, Emmanuel, Nidhi Gupta, Russell Vassell, et al. "Human Immunodeficiency Virus (HIV) gp41 Escape Mutants: Cross-Resistance to Peptide Inhibitors of HIV Fusion and Altered Receptor Activation of gp120." Journal of Virology 79, no. 8 (2005): 4774–81. http://dx.doi.org/10.1128/jvi.79.8.4774-4781.2005.

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ABSTRACT Human immunodeficiency virus (HIV) infects cells by fusing with cellular membranes. Fusion occurs when the envelope glycoprotein (Env) undergoes conformational changes while binding to cellular receptors. Fusogenic changes involve assembly of two heptad repeats in the ectodomain of the gp41 transmembrane subunit to form a six-helix bundle (6HB), consisting of a trimeric N heptad repeat (N-HR) coiled-coil core with three antiparallel C heptad repeats (C-HRs) that pack in the coiled-coil grooves. Peptides corresponding to the N-and C-HRs (N and C peptides, respectively) interfere with f

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Chen, Steve S. L., Sheau-Fen Lee, and Chin-Tien Wang. "Cellular Membrane-Binding Ability of the C-Terminal Cytoplasmic Domain of Human Immunodeficiency Virus Type 1 Envelope Transmembrane Protein gp41." Journal of Virology 75, no. 20 (2001): 9925–38. http://dx.doi.org/10.1128/jvi.75.20.9925-9938.2001.

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ABSTRACT The amphipathic α-helices located in the cytoplasmic tail of the envelope (Env) transmembrane glycoprotein gp41 of human immunodeficiency virus type 1 have been implicated in membrane association and cytopathicity. Deletion of the last 12 amino acids in the C terminus of this domain severely impairs infectivity. However, the nature of the involvement of the cytoplasmic tail in Env-membrane interactions in cells and the molecular basis for the defect in infectivity of this mutant virus are still poorly understood. In this study we examined the interaction of the cytoplasmic tail with m

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Foley, Heather D., Miguel Otero, Jan M. Orenstein, Roger J. Pomerantz, and Matthias J. Schnell. "Rhabdovirus-Based Vectors with Human Immunodeficiency Virus Type 1 (HIV-1) Envelopes Display HIV-1-Like Tropism and Target Human Dendritic Cells." Journal of Virology 76, no. 1 (2002): 19–31. http://dx.doi.org/10.1128/jvi.76.1.19-31.2002.

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ABSTRACT We describe replication-competent, vaccine strain-based rabies viruses (RVs) that lack their own single glycoprotein and express, instead, a chimeric RV-human immunodeficiency virus type 1 (HIV-1) envelope protein composed of the ectodomain and transmembrane domains of HIV-1 gp160 and the cytoplasmic domain of RV G. The envelope proteins from both X4 (NL4-3)- and R5X4 (89.6)-tropic HIV-1 strains were utilized. These recombinant viruses very closely mimicked an HIV-1- like tropism, as indicated by blocking experiments. Infection was inhibited by SDF-1 on cells expressing CD4 and CXCR4

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Johnson, Welkin E., Hannah Sanford, Linda Schwall, et al. "Assorted Mutations in the Envelope Gene of Simian Immunodeficiency Virus Lead to Loss of Neutralization Resistance against Antibodies Representing a Broad Spectrum of Specificities." Journal of Virology 77, no. 18 (2003): 9993–10003. http://dx.doi.org/10.1128/jvi.77.18.9993-10003.2003.

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ABSTRACT Simian immunodeficiency virus (SIV) of macaques isolate SIVmac239 is highly resistant to neutralization by polyclonal antisera or monoclonal antibodies, a property that it shares with most primary isolates of human immunodeficiency virus type 1 (HIV-1). This resistance is important for the ability of the virus to persist at high levels in vivo. To explore the physical features of the viral envelope complex that contribute to the neutralization-resistant phenotype, we examined a panel of SIVmac239 derivatives for sensitivity to neutralization by a large collection of monoclonal antibod

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Weissenhorn, W., S. A. Wharton, L. J. Calder, et al. "The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide." EMBO Journal 15, no. 7 (1996): 1507–14. http://dx.doi.org/10.1002/j.1460-2075.1996.tb00494.x.

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Liu, Yuhang, Junhua Pan, Yongfei Cai, Nikolaus Grigorieff, Stephen C. Harrison, and Bing Chen. "Conformational States of a Soluble, Uncleaved HIV-1 Envelope Trimer." Journal of Virology 91, no. 10 (2017). http://dx.doi.org/10.1128/jvi.00175-17.

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ABSTRACT The HIV-1 envelope spike [Env; trimeric (gp160)3 cleaved to (gp120/gp41)3] induces membrane fusion, leading to viral entry. It is also the viral component targeted by neutralizing antibodies. Vaccine development requires production, in quantities suitable for clinical studies, of a recombinant form that resembles functional Env. HIV-1 gp140 trimers—the uncleaved ectodomains of (gp160)3—from a few selected viral isolates adopt a compact conformation with many antigenic properties of native Env spikes. One is currently being evaluated in a clinical trial. We report here low-resolution (

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Sullivan, Jonathan T., Chidananda Sulli, Alberto Nilo, et al. "High-Throughput Protein Engineering Improves the Antigenicity and Stability of Soluble HIV-1 Envelope Glycoprotein SOSIP Trimers." Journal of Virology 91, no. 22 (2017). http://dx.doi.org/10.1128/jvi.00862-17.

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ABSTRACT Soluble envelope glycoprotein (Env) trimers (SOSIP.664 gp140) are attractive HIV-1 vaccine candidates, with structures that mimic the native membrane-bound Env spike (gp160). Since engineering trimers can be limited by the difficulty of rationally predicting beneficial mutations, here we used a more comprehensive mutagenesis approach with the goal of identifying trimer variants with improved antigenic and stability properties. We created 341 cysteine pairs at predicted points of stabilization throughout gp140, 149 proline residue substitutions at every residue of the gp41 ectodomain,

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Das, Raksha, Rohini Datta, and Raghavan Varadarajan. "Probing the Structure of the HIV-1 Envelope Trimer Using Aspartate Scanning Mutagenesis." Journal of Virology 94, no. 21 (2020). http://dx.doi.org/10.1128/jvi.01426-20.

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ABSTRACT HIV-1 envelope (Env) glycoprotein gp160 exists as a trimer of heterodimers on the viral surface. In most structures of the soluble ectodomain of trimeric HIV-1 envelope glycoprotein, the regions from 512 to 517 of the fusion peptide and from 547 to 568 of the N-heptad repeat are disordered. We used aspartate scanning mutagenesis of subtype B strain JRFL Env as an alternate method to probe residue burial in the context of cleaved, cell surface-expressed Env, as buried residues should be intolerant to substitution with Asp. The data are inconsistent with a fully disordered 547 to 568 st

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Pacheco, Beatriz, Nirmin Alsahafi, Olfa Debbeche, et al. "Residues in the gp41 Ectodomain Regulate HIV-1 Envelope Glycoprotein Conformational Transitions Induced by gp120-Directed Inhibitors." Journal of Virology 91, no. 5 (2016). http://dx.doi.org/10.1128/jvi.02219-16.

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ABSTRACT Interactions between the gp120 and gp41 subunits of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer maintain the metastable unliganded form of the viral spike. Binding of gp120 to the receptor, CD4, changes the Env conformation to promote gp120 interaction with the second receptor, CCR5 or CXCR4. CD4 binding also induces the transformation of Env into the prehairpin intermediate, in which the gp41 heptad repeat 1 (HR1) coiled coil is assembled at the trimer axis. In nature, HIV-1 Envs must balance the requirements to maintain the noncovalent associat

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Thakur, Bhishem, Revansiddha H. Katte, Wang Xu, et al. "Conformational trajectory of the HIV-1 fusion peptide during CD4-induced envelope opening." Nature Communications 16, no. 1 (2025). https://doi.org/10.1038/s41467-025-59721-2.

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Abstract The hydrophobic fusion peptide (FP), a critical component of the HIV-1 entry machinery, is located at the N terminus of the envelope (Env) gp41 subunit. The receptor-binding gp120 subunit of Env forms a heterodimer with gp41. The gp120/gp41 heterodimer assembles into a homotrimer, in which FP is accessible for antibody binding. Env conformational changes or “opening” that follow receptor binding result in FP relocating to a newly formed interprotomer pocket at the gp41-gp120 interface where it is sterically inaccessible to antibodies. The mechanistic steps connecting the entry-related

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Guenaga, Javier, Mehrdad Alirezaei, Yu Feng, et al. "mRNA lipid nanoparticles expressing cell-surface cleavage independent HIV Env trimers elicit autologous tier-2 neutralizing antibodies." Frontiers in Immunology 15 (July 25, 2024). http://dx.doi.org/10.3389/fimmu.2024.1426232.

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The HIV-1 envelope glycoprotein (Env) is the sole neutralizing determinant on the surface of the virus. The Env gp120 and gp41 subunits mediate receptor binding and membrane fusion and are generated from the gp160 precursor by cellular furins. This cleavage event is required for viral entry. One approach to generate HIV-1 neutralizing antibodies following immunization is to express membrane-bound Env anchored on the cell-surface by genetic means using the natural HIV gp41 transmembrane (TM) spanning domain. To simplify the process of Env trimer membrane expression we sought to remove the need

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Ringe, Rajesh P., Philippe Colin, Jonathan L. Torres, et al. "SOS and IP Modifications Predominantly Affect the Yield but Not Other Properties of SOSIP.664 HIV-1 Env Glycoprotein Trimers." Journal of Virology 94, no. 1 (2019). http://dx.doi.org/10.1128/jvi.01521-19.

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ABSTRACT Soluble recombinant native-like (NL) envelope glycoprotein (Env) trimers of various human immunodeficiency virus type 1 (HIV-1) genotypes are being developed as vaccine candidates aimed at the induction of broadly neutralizing antibodies (bNAbs). The prototypic design, designated BG505 SOSIP.664, incorporates an intersubunit disulfide bond (SOS) to covalently link the gp120 and gp41 ectodomain (gp41ECTO) subunits and a point substitution, I559P (IP), to further stabilize the gp41ECTO components. Without the SOS and IP changes, proteolytically cleaved trimers tend to disintegrate into

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