A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization

Wang, Wenbo; Nie, Jianhui; Prochnow, Courtney; Truong, Carolyn; Jia, Zheng; Wang, Suting; Chen, Xiaojiang S; Wang, Youchun

doi:10.1186/1742-4690-10-14

Cited by 115HIV Research and TreatmentGlycosylation and Glycoproteins ResearchCarbohydrate Chemistry and Synthesis

A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization

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Wang, Wenbo, Nie, Jianhui, Prochnow, Courtney, Truong, Carolyn, Jia, Zheng, Wang, Suting, Chen, Xiaojiang S, Wang, Youchun·2013·Retrovirology

DOI 10.1186/1742-4690-10-14PMC PMC3648360

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Abstract

BACKGROUND: Glycans on the human immunodeficiency virus (HIV) envelope glycoprotein (Env) play an important role in viral infection and evasion of neutralization by antibodies. In this study, all 25 potential N-linked glycosylation sites (PNGS) on the HIV-1 CRF07_BC Env, FE, were mutated individually to study the effect of their removal on viral infectivity, virion production, and antibody-mediated neutralization. RESULTS: Removal of specific N-glycosylation sites has a significant effect on viral infectivity and antibody-mediated neutralization phenotype. Six of these glycosylation mutants located on the V1/V2 and C1/C2 domains lost infectivity. PNGS mutations located on V4/C4/V5 (except N392 on V4), were shown to increase viral infectivity. Furthermore, FE is much more dependent on specific glycans than clade B Env YU-2. On neutralization effect, PNGS mutations at N197 (C2), N301 (V3), N442 (C4) and N625 (gp41) rendered the virus more susceptible to neutralization by the monoclonal antibodies (MAbs) that recognize the CD4 binding site or gp41. Generally, mutations on V4/V5 loops, C2/C3/C4 regions and gp41 reduced the neutralization sensitivity to PG16. However, mutation of N289 (C2) made the virus more sensitive to both PG9 and PG16. Furthermore, we showed that mutations at N142 (V1), N355 (C3) and N463 (V5) conferred resistance to neutralization by anti-gp41 MAbs. We used the available structural information of HIV Env and homology modeling to provide a structural basis for the observed biological effects of these mutations. CONCLUSIONS: This report provides the first systematic experimental account of the biological role of the entire PNGS on an HIV-1 Env, which should provide valuable insights for understanding the function of Env in HIV infection cycle and for developing future anti-HIV strategies.

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HIV-1 Env contains ~25 glycosylation sites and forms a glycan shield protecting the virus from neutralizing antibodies; HTLV-1 Env contains only five sites for N-glycan attachment.
“Unlike HIV-1 Env, which contains ~25 glycosylation sites [101], and forms a “glycan shield” protecting the virus from neutralizing antibodies [102], HTLV-1 Env contains only five sites for N-glycan attachment [103].”
From HIV-1 and HTLV-1 Transmission Modes: Mechanisms and Importance for Virus Spread (2022) · cites this paper as [101]
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Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N. V., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2020) · doi:10.1101/2020.12.28.424451
“The introduction of a glycan is a well-known immunogenic escape strategy described in influenza (29), HIV-1 and other viruses (30-32), although to our knowledge this finding presents the first patient-derived escape mutant utilizing this mechanism for SARS-CoV-2.”
Global aspects of viral glycosylation
Bagdonaite, I., & Wandall, H. H. (2018) · Glycobiology · doi:10.1093/glycob/cwy021 · Cited by 234 · see citing works
Current status on the development of pseudoviruses for enveloped viruses
Li, Q., Liu, Q., Huang, W., Li, X., & Wang, Y. (2017) · Reviews in Medical Virology · doi:10.1002/rmv.1963 · Cited by 167 · see citing works
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The Importance of Glycans of Viral and Host Proteins in Enveloped Virus Infection
Li, Y., Liu, D., Wang, Y., Su, W., Liu, G., & Dong, W. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.638573 · Cited by 134 · see citing works
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The HIV glycan shield as a target for broadly neutralizing antibodies
Doores, K. J. (2015) · FEBS Journal · doi:10.1111/febs.13530 · Cited by 131 · see citing works
Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies
Pritchard, L. K., Spencer, D. I. R., Royle, L., Bonomelli, C., Seabright, G. E., Behrens, A., Kulp, D. W., Menis, S., Krumm, S. A., Dunlop, D. C., et al. (2015) · Nature Communications · doi:10.1038/ncomms8479 · Cited by 125 · see citing works
Modular synthesis of N-glycans and arrays for the hetero-ligand binding analysis of HIV antibodies
Shivatare, S. S., Chang, S., Tsai, T.-I., Tseng, S. Y., Shivatare, V. S., Lin, Y., Cheng, Y., Ren, C., Lee, C.-C. D., Pawar, S., et al. (2016) · Nature Chemistry · doi:10.1038/nchem.2463 · Cited by 122 · see citing works
Mapping mutational effects along the evolutionary landscape of HIV envelope
Haddox, H. K., Dingens, A. S., Hilton, S. K., Overbaugh, J. M., & Bloom, J. D. (2018) · eLife · doi:10.7554/elife.34420 · Cited by 120 · see citing works
Experimental Estimation of the Effects of All Amino-Acid Mutations to HIV’s Envelope Protein on Viral Replication in Cell Culture
Haddox, H. K., Dingens, A. S., & Bloom, J. D. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1006114 · Cited by 88 · see citing works
Antibody-dependent-cellular-cytotoxicity-inducing antibodies significantly affect the post-exposure treatment of Ebola virus infection
Liu, Q., Fan, C., Li, Q., Zhou, S., Huang, W., Wang, L., Sun, C., Wang, M., Wu, X., Ma, J., et al. (2017) · Scientific Reports · doi:10.1038/srep45552 · Cited by 87 · see citing works
Self-citation
Visualization of the HIV-1 Env glycan shield across scales
Berndsen, Z. T., Chakraborty, S., Wang, X., Cottrell, C. A., Torres, J. L., Diedrich, J. K., López, C. A., Yates, J. R., van Gils, M. J., Paulson, J. C., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000260117 · Cited by 86 · see citing works
Incomplete Neutralization and Deviation from Sigmoidal Neutralization Curves for HIV Broadly Neutralizing Monoclonal Antibodies
McCoy, L. E., Falkowska, E., Doores, K. J., Le, K. M., Sok, D., van Gils, M. J., Euler, Z., Burger, J. A., Seaman, M. S., Sanders, R. W., et al. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005110 · Cited by 86 · see citing works
Application of pseudovirus system in the development of vaccine, antiviral-drugs, and neutralizing antibodies
Xiang, Q., Li, L., Wu, J., Tian, M., & Fu, Y. (2022) · Microbiological Research · doi:10.1016/j.micres.2022.126993 · Cited by 74 · see citing works
Polyclonal antibody responses to HIV Env immunogens resolved using cryoEM
Antanasijevic, A., Sewall, L. M., Cottrell, C. A., Carnathan, D. G., Jimenez, L. E., Ngo, J. T., Silverman, J. B., Gröschel, B., Georgeson, E., Bhiman, J. N., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25087-4 · Cited by 71 · see citing works
HIV-1 and HTLV-1 Transmission Modes: Mechanisms and Importance for Virus Spread
Kalinichenko, S., Komkov, D., & Mazurov, D. (2022) · Viruses · doi:10.3390/v14010152 · Cited by 68 · see citing works
“Unlike HIV-1 Env, which contains ~25 glycosylation sites [101], and forms a “glycan shield” protecting the virus from neutralizing antibodies [102], HTLV-1 Env contains only five sites for N-glycan attachment [103].”
Background
Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus
Bagdonaite, I., Nordén, R., Joshi, H. J., King, S. L., Vakhrushev, S. Y., Olofsson, S., & Wandall, H. H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.721746 · Cited by 68 · see citing works
Structure and Recognition of a Novel HIV-1 gp120-gp41 Interface Antibody that Caused MPER Exposure through Viral Escape
Wibmer, C. K., Gorman, J., Ozorowski, G., Bhiman, J. N., Sheward, D. J., Elliott, D. H., Rouelle, J. A., Smira, A. R., Joyce, M. G., Ndabambi, N., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006074 · Cited by 64 · see citing works
A Strategy for O-Glycoproteomics of Enveloped Viruses—the O-Glycoproteome of Herpes Simplex Virus Type 1
Bagdonaite, I., Nordén, R., Joshi, H. J., Dabelsteen, S., Nyström, K., Vakhrushev, S. Y., Olofsson, S., & Wandall, H. H. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004784 · Cited by 56 · see citing works
The external domains of the HIV-1 envelope are a mutational cold spot
Geller, R., Domingo‐Calap, P., Cuevas, J. M., Rossolillo, P., Negroni, M., & Sanjuán, R. (2015) · Nature Communications · doi:10.1038/ncomms9571 · Cited by 55 · see citing works
Networks of HIV-1 Envelope Glycans Maintain Antibody Epitopes in the Face of Glycan Additions and Deletions
Seabright, G. E., Cottrell, C. A., van Gils, M. J., D’Addabbo, A., Harvey, D. J., Behrens, A., Allen, J. D., Watanabe, Y., Scaringi, N., Polveroni, T. M., et al. (2020) · Structure · doi:10.1016/j.str.2020.04.022 · Cited by 52 · see citing works
Lentil lectin derived from Lens culinaris exhibit broad antiviral activities against SARS-CoV-2 variants
Wang, W., Li, Q., Wu, J., Hu, Y., Wu, G., Yu, C., Xu, K., Liu, X., Wang, Q., Huang, W., et al. (2021) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.1957720 · Cited by 49 · see citing works
Self-citation
The N276 Glycosylation Site Is Required for HIV-1 Neutralization by the CD4 Binding Site Specific HJ16 Monoclonal Antibody
Balla-Jhagjhoorsingh, S. S., Corti, D., Heyndríckx, L., Willems, E., Vereecken, K., Davis, D. A., & Vanham, G. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068863 · Cited by 46 · see citing works
Strategies to induce broadly protective antibody responses to viral glycoproteins
Krammer, F. (2017) · Expert Review of Vaccines · doi:10.1080/14760584.2017.1299576 · Cited by 41 · see citing works
Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
Veillette, M., Coutu, M., Richard, J., Batraville, L.-A., Désormeaux, A., Roger, M., & Finzi, A. (2014) · Journal of Visualized Experiments · doi:10.3791/51995 · Cited by 40 · see citing works
Differential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection
Raška, M., Czerneková, L., Moldoveanu, Z., Zachová, K., Elliott, M. C., Novák, Z., Hall, S. D., Höelscher, M., Maboko, L., Brown, R., et al. (2014) · AIDS Research and Therapy · doi:10.1186/1742-6405-11-23 · Cited by 35 · see citing works
Delineating CD4 dependency of HIV-1: Adaptation to infect low level CD4 expressing target cells widens cellular tropism but severely impacts on envelope functionality
Beauparlant, D., Rusert, P., Magnus, C., Kadelka, C., Weber, J., Uhr, T., Zagordi, O., Oberle, C. S., Duenas-Decamp, M. J., Clapham, P. R., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006255 · Cited by 35 · see citing works
Deletion of the Highly Conserved N-Glycan at Asn260 of HIV-1 gp120 Affects Folding and Lysosomal Degradation of gp120, and Results in Loss of Viral Infectivity
Mathys, L., François, K. O., Quandte, M., Braakman, I., & Balzarini, J. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101181 · Cited by 31 · see citing works
Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity
Rathore, U., Saha, P., Kesavardhana, S., Kumar, A. A., Datta, R., Sankar, D. S., Das, R., Mascola, J. R., & Varadarajan, R. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.788919 · Cited by 31 · see citing works
Viral glycoproteomes: technologies for characterization and outlook for vaccine design
Bagdonaite, I., Vakhrushev, S., Joshi, H., & Wandall, H. (2018) · FEBS Letters · doi:10.1002/1873-3468.13177 · Cited by 29 · see citing works
Characterization of the role of N-glycosylation sites in the respiratory syncytial virus fusion protein in virus replication, syncytium formation and antigenicity
Leemans, A., Boeren, M., der Gucht, W. V., Martinet, W., Caljon, G., Maes, L. J. R. M., Cos, P., & Delputte, P. (2019) · Virus Research · doi:10.1016/j.virusres.2019.04.006 · Cited by 30 · see citing works
Computational Refinement and Validation Protocol for Proteins with Large Variable Regions Applied to Model HIV Env Spike in CD4 and 17b Bound State
Rasheed, M., Bettadapura, R., & Bajaj, C. (2015) · Structure · doi:10.1016/j.str.2015.03.026 · Cited by 30 · see citing works
Antigenic variations of recent street rabies virus
Wang, W., Ma, J., Nie, J., Li, J., Cao, S., Wang, L., Yu, C., Huang, W., Li, Y., Yu, Y., et al. (2019) · Emerging Microbes & Infections · doi:10.1080/22221751.2019.1683436 · Cited by 28 · see citing works
Self-citation
Autologous neutralizing antibodies increase with early antiretroviral therapy and shape HIV rebound after treatment interruption
Esmaeilzadeh, E., Etemad, B., Lavine, C. L., Garneau, L., Li, Y., Regan, J., Wong, C., Sharaf, R. R., Connick, E., Volberding, P. A., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abq4490 · Cited by 28 · see citing works
Loss of a Conserved N-Linked Glycosylation Site in the Simian Immunodeficiency Virus Envelope Glycoprotein V2 Region Enhances Macrophage Tropism by Increasing CD4-Independent Cell-to-Cell Transmission
Yen, P.-J., Herschhorn, A., Haim, H., Salas, I., Gu, C., Sodroski, J., & Gabuzda, D. H. (2014) · Journal of Virology · doi:10.1128/jvi.02785-13 · Cited by 28 · see citing works
Arms Race between Enveloped Viruses and the Host ERAD Machinery
Frabutt, D. A., & Zheng, Y. (2016) · Viruses · doi:10.3390/v8090255 · Cited by 27 · see citing works
Synthetic Carbohydrate Chemistry and Translational Medicine
Shivatare, S. S., & Wong, C. (2020) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.0c01834 · Cited by 28 · see citing works
Changes in Structure and Antigenicity of HIV-1 Env Trimers Resulting from Removal of a Conserved CD4 Binding Site-Proximal Glycan
Liang, Y., Guttman, M., Williams, J. A., Verkerke, H., Alvarado, D., Hu, S.-L., & Lee, K. K. (2016) · Journal of Virology · doi:10.1128/jvi.01116-16 · Cited by 27 · see citing works
Bioinformatic Analysis of HIV-1 Entry and Pathogenesis
Aiamkitsumrit, B., Dampier, W., Antell, G. C., Rivera, N., Martín‐García, J., Pirrone, V., Nonnemacher, M. R., & Wigdahl, B. L. (2014) · Current HIV Research · doi:10.2174/1570162x12666140526121746 · Cited by 27 · see citing works
Pseudoviruses, a safer toolbox for vaccine development against enveloped viruses
Thimmiraju, S. R., Kimata, J. T., & Pollet, J. B. K. (2024) · Expert Review of Vaccines · doi:10.1080/14760584.2023.2299380 · Cited by 24 · see citing works
HIV-1 Envelope Glycan Moieties Modulate HIV-1 Transmission
Shen, R., Raška, M., Bimczok, D., Novák, J., & Smith, P. D. (2014) · Journal of Virology · doi:10.1128/jvi.02164-14 · Cited by 23 · see citing works
Defining HIV-1 Envelope N-Glycan Microdomains through Site-Specific Heterogeneity Profiles
Hargett, A. A., Wei, Q., Knoppová, B., Hall, S. D., Huang, Z., Prakash, A., Green, T. J., Moldoveanu, Z., Raška, M., Novák, J., et al. (2018) · Journal of Virology · doi:10.1128/jvi.01177-18 · Cited by 22 · see citing works
Glycosylation profiling to evaluate glycoprotein immunogens against HIV-1
Behrens, A., Struwe, W. B., & Crispin, M. (2017) · Expert Review of Proteomics · doi:10.1080/14789450.2017.1376658 · Cited by 22 · see citing works
SARS-CoV-2 spike protein receptor-binding domain N-glycans facilitate viral internalization in respiratory epithelial cells
Zheng, L., Ma, Y., Chen, M., Wu, G., Yan, C., & Zhang, X. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.09.053 · Cited by 21 · see citing works
Several N-Glycans on the HIV Envelope Glycoprotein gp120 Preferentially Locate Near Disulphide Bridges and Are Required for Efficient Infectivity and Virus Transmission
Mathys, L., & Balzarini, J. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130621 · Cited by 21 · see citing works
HIV-1 pseudoviruses constructed in China regulatory laboratory
Nie, J., Huang, W., Liu, Q., & Wang, Y. (2019) · Emerging Microbes & Infections · doi:10.1080/22221751.2019.1702479 · Cited by 20 · see citing works
Self-citation
The Glycan Hole Area of HIV-1 Envelope Trimers Contributes Prominently to the Induction of Autologous Neutralization
Schorcht, A., Cottrell, C. A., Pugach, P., Ringe, R. P., Han, A. X., Allen, J. D., van den Kerkhof, T. L. G. M., Seabright, G. E., Schermer, E. E., Ketas, T. J., et al. (2021) · Journal of Virology · doi:10.1128/jvi.01552-21 · Cited by 20 · see citing works
Conformational Engineering of HIV-1 Env Based on Mutational Tolerance in the CD4 and PG16 Bound States
Heredia, J. D., Park, J., Choi, H. S. J., Gill, K. S., & Procko, E. (2019) · Journal of Virology · doi:10.1128/jvi.00219-19 · Cited by 19 · see citing works
Glycosylation of ALV-J Envelope Protein at Sites 17 and 193 Is Pivotal in the Virus Infection
Xu, M., Qian, K., Shao, H., Yao, Y., Nair, V., Ye, J., & Qin, A. (2021) · Journal of Virology · doi:10.1128/jvi.01549-21 · Cited by 18 · see citing works
Mannose-specific plant and microbial lectins as antiviral agents: A review
Gupta, A., Yadav, K., Yadav, A., Ahmad, R., Srivastava, A., Kumar, D., Khan, M. A., & Dwivedi, U. N. (2024) · Glycoconjugate Journal · doi:10.1007/s10719-023-10142-7 · Cited by 18 · see citing works
Structural Rearrangements Maintain the Glycan Shield of an HIV-1 Envelope Trimer After the Loss of a Glycan
Ferreira, R.-C., Grant, O. C., Moyo-Gwete, T., Dorfman, J. R., Woods, R. J., Travers, S. A. A., & Wood, N. T. (2018) · Scientific Reports · doi:10.1038/s41598-018-33390-2 · Cited by 17 · see citing works
Molecular Characterization of Small Ruminant Lentiviruses in Polish Mixed Flocks Supports Evidence of Cross Species Transmission, Dual Infection, a Recombination Event, and Reveals the Existence of New Subtypes within Group A
Olech, M., & Kuźmak, J. M. (2021) · Viruses · doi:10.3390/v13122529 · Cited by 17 · see citing works
N463 Glycosylation Site on V5 Loop of a Mutant gp120 Regulates the Sensitivity of HIV-1 to Neutralizing Monoclonal Antibodies VRC01/03
Wang, W., Zirkle, B., Nie, J., Ma, J., Gao, K., Chen, X. S., Huang, W., Kong, W., & Wang, Y. (2015) · JAIDS Journal of Acquired Immune Deficiency Syndromes · doi:10.1097/qai.0000000000000595 · Cited by 16 · see citing works
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HIV-1 Entry and Prospects for Protecting against Infection
Bruxelle, J.-F., Trattnig, N., Mureithi, M., Landais, E., & Pantophlet, R. A. (2021) · Microorganisms · doi:10.3390/microorganisms9020228 · Cited by 16 · see citing works
Induction of complex immune responses and strong protection against retrovirus challenge by adenovirus-based immunization depends on the order of vaccine delivery
Kaulfuß, M., Wensing, I., Windmann, S., Hrycak, C. P., & Bayer, W. (2017) · Retrovirology · doi:10.1186/s12977-017-0336-7 · Cited by 14 · see citing works
Antibody Responses Elicited by Immunization with BG505 Trimer Immune Complexes
Gach, J. S., Mara, K. J. V., LaBranche, C. C., van Gils, M. J., McCoy, L. E., Klasse, P. J., Montefiori, D. C., Sanders, R. W., Moore, J. P., & Forthal, D. N. (2019) · Journal of Virology · doi:10.1128/jvi.01188-19 · Cited by 14 · see citing works
Human Immunodeficiency Virus Type 1 Cellular Entry and Exit in the T Lymphocytic and Monocytic Compartments
Aiamkitsumrit, B., Sullivan, N. T., Nonnemacher, M. R., Pirrone, V., & Wigdahl, B. L. (2015) · Advances in virus research · doi:10.1016/bs.aivir.2015.04.001 · Cited by 14 · see citing works
Time-course, negative-stain electron microscopy–based analysis for investigating protein–protein interactions at the single-molecule level
Nogal, B., Bowman, C. A., & Ward, A. B. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.808352 · Cited by 13 · see citing works
Comparative proteomic analysis of hemolymph proteins from Autographa californica multiple nucleopolyhedrovirus (AcMNPV)-sensitive or -resistant silkworm strains during infections
Xu, J. C., Zhang, P., Kusakabe, T., Mon, H., Li, Z., Zhu, L., Iiyama, K., Banno, Y., Morokuma, D., & Lee, J. M. (2015) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2015.07.003 · Cited by 13 · see citing works
Functional and Structural Characterization of Human V3-Specific Monoclonal Antibody 2424 with Neutralizing Activity against HIV-1 JRFL
Kumar, R., Pan, R., Upadhyay, C., Mayr, L. M., Cohen, S., Wang, X.-H., Balasubramanian, P., Nadas, A. J., Seaman, M. S., Zolla‐Pazner, S., et al. (2015) · Journal of Virology · doi:10.1128/jvi.01280-15 · Cited by 12 · see citing works
Increased HIV-1 sensitivity to neutralizing antibodies by mutations in the Env V3-coding region for resistance to CXCR4 antagonists
Hikichi, Y., Yokoyama, M., Takemura, T., Fujino, M., Kumakura, S., Maeda, Y., Yamamoto, N., Sato, H., Matano, T., & Murakami, T. (2016) · Journal of General Virology · doi:10.1099/jgv.0.000536 · Cited by 11 · see citing works
Glycan Positioning Impacts HIV-1 Env Glycan-Shield Density, Function, and Recognition by Antibodies
Wei, Q., Hargett, A. A., Knoppová, B., Duverger, A. E., Rawi, R., Shen, C., Farney, S. K., Hall, S. D., Brown, R., Keele, B. F., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101711 · Cited by 11 · see citing works
A Comprehensive Analysis of Human Endogenous Retroviruses HERV-K (HML.2) from Teratocarcinoma Cell Lines and Detection of Viral Cargo in Microvesicles
Va, M., & Morozov, A. V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212398 · Cited by 11 · see citing works
The role of N -glycans of HIV-1 gp41 in virus infectivity and susceptibility to the suppressive effects of carbohydrate-binding agents
Mathys, L., & Balzarini, J. M. (2014) · Retrovirology · doi:10.1186/preaccept-5732415801310430 · Cited by 11 · see citing works
HIV-1 Entry Mechanisms: Protein-Host Receptor Interactions and Membrane Fusion Dynamics
Elalouf, A., Elalouf, H., & Maoz, H. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl37412 · Cited by 11 · see citing works
Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains
Liang, S. A., Ratnayake, P. U., Keinath, C., Jia, L., Wolfe, R., Ranaweera, A., & Weliky, D. P. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b00753 · Cited by 10 · see citing works
Guiding the humoral response against HIV-1 toward a MPER adjacent region by immunization with a VLP-formulated antibody-selected envelope variant
Beltrán-Pavez, C., Ferreira, C. B., Merino-Mansilla, A., Fabra-García, A., Casadellà, M., Noguera-Julián, M., Paredes, R., Olvera, À., Haro, I., Brander, C., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208345 · Cited by 9 · see citing works
Preferential Targeting of Conserved Gag Regions after Vaccination with a Heterologous DNA Prime-Modified Vaccinia Virus Ankara Boost HIV-1 Vaccine Regimen
Bauer, A. P., Podola, L., Mann, P., Missanga, M., Haule, A., Sudi, L., Nilsson, C., Kaluwa, B., Lueer, C., Mwakatima, M., et al. (2017) · Journal of Virology · doi:10.1128/jvi.00730-17 · Cited by 9 · see citing works
Comprehensive maps of escape mutations from antibodies 10-1074 and 3BNC117 for Envs from two divergent HIV strains
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Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation
Wang, S., Li, W., Wen, J., Wang, L., Tiwari, S. K., Bray, W., Wu, L., Li, N., Hui, H., Clark, A. E., et al. (2025) · mBio · doi:10.1128/mbio.02930-25 · Cited by 8 · see citing works
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Glycosylation in viral hepatitis
Gruszewska, E., Grytczuk, A., & Chrostek, L. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129997 · Cited by 8 · see citing works
Long-read deep sequencing reveals high rates of multilineage transmission and rapid viral population changes in acute HIV infection
Mullins, J. I., Deng, W., Giorgi, E. E., Magaret, C. A., Rolland, M., Tanmoy Bhattacharya, A., Westfall, D. H., Yssel, A., Bumgarner, R. E., Murrell, B., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-73496-0 · Cited by 7 · see citing works
Glycan Nanostructures of Human Coronaviruses
Guo, W., Lakshminarayanan, H., Rodriguez‐Palacios, A., Salata, R. A., Xu, K., & Draz, M. S. (2021) · International Journal of Nanomedicine · doi:10.2147/ijn.s302516 · Cited by 7 · see citing works
Pseudotyped Viruses for Retroviruses
Solomon, M., & Liang, C. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-981-99-0113-5_4 · Cited by 7 · see citing works
Variability in the Glycosylation Patterns of gp120 Proteins from Different Human Immunodeficiency Virus Type 1 Isolates Expressed in Different Host Cells
Zhao, J., Song, E., Huang, Y., Yu, A., & Mechref, Y. S. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00587 · Cited by 7 · see citing works
Partial HIV C2V3 envelope sequence analysis reveals association of coreceptor tropism, envelope glycosylation and viral genotypic variability among Kenyan patients on HAART
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A shrimp glycosylase protein, PmENGase, interacts with WSSV envelope protein VP41B and is involved in WSSV pathogenesis
Huang, J., Wang, H., Chen, Y., Wang, P.-S., Lin, S.-J., Chang, Y.-S., Liu, K.-F., & Lo, C. (2020) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2020.103667 · Cited by 6 · see citing works
Employing Broadly Neutralizing Antibodies as a Human Immunodeficiency Virus Prophylactic & Therapeutic Application
Ding, C., Patel, D., Ma, Y., Mann, J. F. S., Wu, J., & Gao, Y. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.697683 · Cited by 6 · see citing works
HIV-1 envelope facilitates the development of protease inhibitor resistance through acquiring mutations associated with viral entry and immune escape
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Authors: Wang, W., Nie, J., Prochnow, C., Truong, C., Jia, Z., Wang, S., Chen, X. S., & Wang, Y.
Affiliations: National Institutes for Food and Drug Control (CN)
University of Southern California (US)
Corresponding author: Wang, Youchun
ORCID: Wang, Wenbo
Nie, Jianhui
Jia, Zheng
Wang, Suting
Chen, Xiaojiang S
Wang, Youchun
Venue: Retrovirology
Publisher: Springer Science and Business Media LLC
Published: 2013-02-06
Volume: 10
Issue: 1
Pages: 14-14
ISSN: 1742-4690 (ISSN-L)
DOI: 10.1186/1742-4690-10-14
PMC: PMC3648360
OpenAlex: W2137366946
Cited by: 114
References: 64
Citations by year: 2026: 3 · 2025: 10 · 2024: 6 · 2023: 4 · 2022: 5 · 2021: 16 · 2020: 8 · 2019: 9 · 2018: 8 · 2017: 11 · 2016: 8 · 2015: 13 · 2014: 8 · 2013: 4
FWCI: 5.05
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/2.0 (tdm)
Locations: Retrovirology (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (GM087986)
National Institute of General Medical Sciences (GM087986, R01GM087986)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
Keywords: HIV-1 envelope glycoprotein, N-glycosylation sites, viral infectivity, antibody neutralization, CRF07_BC, V1V2 loop, gp41, CD4 binding site, monoclonal antibodies, PG9, homology modeling, HIV-1 clade B
MeSH terms: Glycosylation, Humans, Neutralization Tests, Virus Replication, HIV Antibodies, HIV-1, env Gene Products, Human Immunodeficiency Virus, Antibodies, Neutralizing

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A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization

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