Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope

Barnes, Christopher O.; Gristick, Harry B.; Freund, Natalia T.; Escolano, Amelia; Lyubimov, Artem Y.; Hartweger, Harald; West, Anthony P.; Cohen, Aina E.; Nussenzweig, Michel C.; Bjorkman, Pamela J.

doi:10.1038/s41467-018-03632-y

Title: Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope

Journal Article · Wed Mar 28 00:00:00 EDT 2018 · Nature Communications

DOI:https://doi.org/10.1038/s41467-018-03632-y· OSTI ID:1624084

Barnes, Christopher O. ^[1]; Gristick, Harry B. ^[2]; Freund, Natalia T. ^[3]; Escolano, Amelia ^[4]; Lyubimov, Artem Y. ^[5]; Hartweger, Harald ^[6]; West, Anthony P. ^[2]; Cohen, Aina E. ^[5]; Nussenzweig, Michel C. ^[7]; Bjorkman, Pamela J. ^[2]

California Institute of Technology (CalTech), Pasadena, CA (United States). Division of Biology and Biological Engineering
California Institute of Technology (CalTech), Pasadena, CA (United States). Division of Biology and Biological Engineering
Rockefeller Univ., New York, NY (United States). Laboratory of Molecular Immunology; Tel Aviv Univ., Ramat Aviv (Israel). Sackler Faculty of Medicine, Dept. of Clinical Immunology and Microbiology
Rockefeller Univ., New York, NY (United States). Laboratory of Molecular Immunology
SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Rockefeller Univ., New York, NY (United States). Laboratory of Molecular Immunology
Rockefeller Univ., New York, NY (United States). Laboratory of Molecular Immunology; Rockefeller Univ., New York, NY (United States). Howard Hughes Medical Institute

Broadly neutralizing antibodies (bNAbs) isolated from HIV-1-infected individuals inform HIV-1 vaccine design efforts. Developing bNAbs with increased efficacy requires understanding how antibodies interact with the native oligomannose and complex-type N-glycan shield that hides most protein epitopes on HIV-1 envelope (Env). Here we present crystal structures, including a 3.8-Å X-ray free electron laser dataset, of natively glycosylated Env trimers complexed with BG18, the most potent V3/N332_gp120 glycan-targeting bNAb reported to date. Our structures show conserved contacts mediated by common D gene-encoded residues with the N332_gp120 glycan and the gp120 GDIR peptide motif, but a distinct Env-binding orientation relative to PGT121/10-1074 bNAbs. BG18’s binding orientation provides additional contacts with N392_gp120 and N386_gp120 glycans near the V3-loop base and engages protein components of the V1-loop. The BG18-natively-glycosylated Env structures facilitate understanding of bNAb–glycan interactions critical for using V3/N332_gp120 bNAbs therapeutically and targeting their epitope for immunogen design.

View Accepted Manuscript (DOE)

Cite

Export

Save

Research Organization:: SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL) and Linac Coherent Light Source (LCLS)

Sponsoring Organization:: Burroughs Wellcome Fund; National Institute of Allergy and Infectious Diseases (NIAID); National Institutes of Health (NIH); Bill and Melinda Gates Foundation; Gordon and Betty Moore Foundation; USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institute of General Medical Sciences (NIGMS)

Grant/Contract Number:: AC02-76SF00515; HIVRAD P01 AI100148; OPP1124068

OSTI ID:: 1624084

Journal Information:: Nature Communications, Vol. 9, Issue 1; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

References (83)

Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env Do Kwon, Young; Pancera, Marie; Acharya, Priyamvada Nature Structural & Molecular Biology, Vol. 22, Issue 7 https://doi.org/10.1038/nsmb.3051	journal	June 2015
Goniometer-based femtosecond crystallography with X-ray free electron lasers Cohen, Aina E.; Soltis, S. Michael; González, Ana Proceedings of the National Academy of Sciences, Vol. 111, Issue 48, p. 17122-17127 https://doi.org/10.1073/pnas.1418733111	journal	October 2014
Affinity Maturation of a Potent Family of HIV Antibodies Is Primarily Focused on Accommodating or Avoiding Glycans Garces, Fernando; Lee, Jeong Hyun; de Val, Natalia Immunity, Vol. 43, Issue 6 https://doi.org/10.1016/j.immuni.2015.11.007	journal	December 2015
Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site Gristick, Harry B.; von Boehmer, Lotta; West Jr, Anthony P. Nature Structural & Molecular Biology, Vol. 23, Issue 10 https://doi.org/10.1038/nsmb.3291	journal	September 2016
Comprehensive Mapping of HIV-1 Escape from a Broadly Neutralizing Antibody Dingens, Adam S.; Haddox, Hugh K.; Overbaugh, Julie Cell Host & Microbe, Vol. 21, Issue 6 https://doi.org/10.1016/j.chom.2017.05.003	journal	June 2017
Overview of the CCP 4 suite and current developments Winn, Martyn D.; Ballard, Charles C.; Cowtan, Kevin D. Acta Crystallographica Section D Biological Crystallography, Vol. 67, Issue 4 https://doi.org/10.1107/S0907444910045749	journal	March 2011
Broad and potent HIV-1 neutralization by a human antibody that binds the gp41–gp120 interface Huang, Jinghe; Kang, Byong H.; Pancera, Marie Nature, Vol. 515, Issue 7525 https://doi.org/10.1038/nature13601	journal	September 2014
PHENIX: a comprehensive Python-based system for macromolecular structure solution. Adams, Paul D.; Afonine, Pavel V.; Bunkóczi, Gábor Apollo - University of Cambridge Repository https://doi.org/10.17863/cam.45787	text	January 2010
Viraemia suppressed in HIV-1-infected humans by broadly neutralizing antibody 3BNC117 Caskey, Marina; Klein, Florian; Lorenzi, Julio C. C. Nature, Vol. 522, Issue 7557 https://doi.org/10.1038/nature14411	journal	April 2015
Increasing the Potency and Breadth of an HIV Antibody by Using Structure-Based Rational Design Diskin, R.; Scheid, J. F.; Marcovecchio, P. M. Science, Vol. 334, Issue 6060 https://doi.org/10.1126/science.1213782	journal	October 2011
IOTA : integration optimization, triage and analysis tool for the processing of XFEL diffraction images Lyubimov, Artem Y.; Uervirojnangkoorn, Monarin; Zeldin, Oliver B. Journal of Applied Crystallography, Vol. 49, Issue 3 https://doi.org/10.1107/S1600576716006683	journal	May 2016
X-ray and EM structures of a natively glycosylated HIV-1 envelope trimer Gristick, Harry B.; Wang, Haoqing; Bjorkman, Pamela J. Acta Crystallographica Section D Structural Biology, Vol. 73, Issue 10 https://doi.org/10.1107/s2059798317013353	journal	September 2017
HIV-1 suppression and durable control by combining single broadly neutralizing antibodies and antiretroviral drugs in humanized mice Horwitz, J. A.; Halper-Stromberg, A.; Mouquet, H. Proceedings of the National Academy of Sciences, Vol. 110, Issue 41 https://doi.org/10.1073/pnas.1315295110	journal	September 2013
Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody Kwong, Peter D.; Wyatt, Richard; Robinson, James Nature, Vol. 393, Issue 6686 https://doi.org/10.1038/31405	journal	June 1998
Coexistence of potent HIV-1 broadly neutralizing antibodies and antibody-sensitive viruses in a viremic controller Freund, Natalia T.; Wang, Haoqing; Scharf, Louise Science Translational Medicine, Vol. 9, Issue 373 https://doi.org/10.1126/scitranslmed.aal2144	journal	January 2017
HIV-1 therapy with monoclonal antibody 3BNC117 elicits host immune responses against HIV-1 Schoofs, T.; Klein, F.; Braunschweig, M. Science, Vol. 352, Issue 6288 https://doi.org/10.1126/science.aaf0972	journal	May 2016
Intra-Spike Crosslinking Overcomes Antibody Evasion by HIV-1 Galimidi, Rachel P.; Klein, Joshua S.; Politzer, Maria S. Cell, Vol. 160, Issue 3 https://doi.org/10.1016/j.cell.2015.01.016	journal	January 2015
Web servers and services for electrostatics calculations with APBS and PDB2PQR Unni, Samir; Huang, Yong; Hanson, Robert M. Journal of Computational Chemistry, Vol. 32, Issue 7 https://doi.org/10.1002/jcc.21720	journal	February 2011
Structure and immune recognition of trimeric pre-fusion HIV-1 Env B., Munro, James; Lynn, Morris,; Tongqing, Zhou, The University of North Carolina at Chapel Hill University Libraries https://doi.org/10.17615/bt86-bx50	text	January 2014
Crystal Structure of a Soluble Cleaved HIV-1 Envelope Trimer Julien, J. -P.; Cupo, A.; Sok, D. Science, Vol. 342, Issue 6165 https://doi.org/10.1126/science.1245625	journal	October 2013
In situ click chemistry generation of cyclooxygenase-2 inhibitors Bhardwaj, Atul; Kaur, Jatinder; Wuest, Melinda Nature Communications, Vol. 8, Issue 1 https://doi.org/10.1038/s41467-016-0009-6	journal	February 2017
XDS Kabsch, Wolfgang Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2 https://doi.org/10.1107/S0907444909047337	journal	January 2010
Inference of Macromolecular Assemblies from Crystalline State Krissinel, Evgeny; Henrick, Kim Journal of Molecular Biology, Vol. 372, Issue 3 https://doi.org/10.1016/j.jmb.2007.05.022	journal	September 2007
Antibody 8ANC195 Reveals a Site of Broad Vulnerability on the HIV-1 Envelope Spike Scharf, Louise; Scheid, Johannes F.; Lee, Jeong Hyun Cell Reports, Vol. 7, Issue 3 https://doi.org/10.1016/j.celrep.2014.04.001	journal	May 2014
Broad neutralization coverage of HIV by multiple highly potent antibodies Walker, Laura M.; Huber, Michael; Doores, Katie J. Nature, Vol. 477, Issue 7365 https://doi.org/10.1038/nature10373	journal	September 2011
Few and Far Between: How HIV May Be Evading Antibody Avidity Klein, Joshua S.; Bjorkman, Pamela J. PLoS Pathogens, Vol. 6, Issue 5 https://doi.org/10.1371/journal.ppat.1000908	journal	May 2010
Mass Spectrometric Characterization of the Glycosylation Pattern of HIV-gp120 Expressed in CHO Cells Zhu, Xuegong; Borchers, Christoph; Bienstock, Rachelle J. Biochemistry, Vol. 39, Issue 37 https://doi.org/10.1021/bi000432m	journal	September 2000
Architecture of the synaptotagmin–SNARE machinery for neuronal exocytosis Zhou, Qiangjun; Lai, Ying; Bacaj, Taulant Nature, Vol. 525, Issue 7567 https://doi.org/10.1038/nature14975	journal	August 2015
Accurate macromolecular structures using minimal measurements from X-ray free-electron lasers Hattne, Johan; Echols, Nathaniel; Tran, Rosalie Nature Methods, Vol. 11, Issue 5 https://doi.org/10.1038/nmeth.2887	journal	March 2014
Computational analysis of anti-HIV-1 antibody neutralization panel data to identify potential functional epitope residues West, A. P.; Scharf, L.; Horwitz, J. Proceedings of the National Academy of Sciences, Vol. 110, Issue 26 https://doi.org/10.1073/pnas.1309215110	journal	June 2013
Glycans Function as Anchors for Antibodies and Help Drive HIV Broadly Neutralizing Antibody Development Andrabi, Raiees; Su, Ching-Yao; Liang, Chi-Hui Immunity, Vol. 47, Issue 3 https://doi.org/10.1016/j.immuni.2017.08.006	journal	September 2017
Composition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope Glycoprotein Behrens, Anna-Janina; Vasiljevic, Snezana; Pritchard, Laura K. Cell Reports, Vol. 14, Issue 11 https://doi.org/10.1016/j.celrep.2016.02.058	journal	March 2016
Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01 Zhou, T.; Georgiev, I.; Wu, X. Science, Vol. 329, Issue 5993 https://doi.org/10.1126/science.1192819	journal	July 2010
Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G Stewart-Jones, Guillaume B. E.; Soto, Cinque; Lemmin, Thomas Cell, Vol. 165, Issue 4 https://doi.org/10.1016/j.cell.2016.04.010	journal	May 2016
Broadly Neutralizing Antibody 8ANC195 Recognizes Closed and Open States of HIV-1 Env Scharf, Louise; Wang, Haoqing; Gao, Han Cell, Vol. 162, Issue 6 https://doi.org/10.1016/j.cell.2015.08.035	journal	September 2015
Effect of HIV Antibody VRC01 on Viral Rebound after Treatment Interruption Bar, Katharine J.; Sneller, Michael C.; Harrison, Linda J. New England Journal of Medicine, Vol. 375, Issue 21 https://doi.org/10.1056/NEJMoa1608243	journal	November 2016
Electron Density Sharpening as a General Technique in Crystallographic Studies Liu, Chang; Xiong, Yong Journal of Molecular Biology, Vol. 426, Issue 4 https://doi.org/10.1016/j.jmb.2013.11.014	journal	February 2014
PHENIX: a comprehensive Python-based system for macromolecular structure solution Adams, Paul D.; Afonine, Pavel V.; Bunkóczi, Gábor Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2, p. 213-221 https://doi.org/10.1107/S0907444909052925	journal	January 2010
Sequential Immunization Elicits Broadly Neutralizing Anti-HIV-1 Antibodies in Ig Knockin Mice Escolano, Amelia; Steichen, Jon M.; Dosenovic, Pia Cell, Vol. 166, Issue 6 https://doi.org/10.1016/j.cell.2016.07.030	journal	September 2016
Antibody neutralization and escape by HIV-1 Wei, Xiping; Decker, Julie M.; Wang, Shuyi Nature, Vol. 422, Issue 6929 https://doi.org/10.1038/nature01470	journal	March 2003
Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies Mouquet, H.; Scharf, L.; Euler, Z. Proceedings of the National Academy of Sciences, Vol. 109, Issue 47 https://doi.org/10.1073/pnas.1217207109	journal	October 2012
Antibody-mediated immunotherapy of macaques chronically infected with SHIV suppresses viraemia Shingai, Masashi; Nishimura, Yoshiaki; Klein, Florian Nature, Vol. 503, Issue 7475 https://doi.org/10.1038/nature12746	journal	October 2013
Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys Barouch, Dan H.; Whitney, James B.; Moldt, Brian Nature, Vol. 503, Issue 7475 https://doi.org/10.1038/nature12744	journal	October 2013
A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield Pejchal, R.; Doores, K. J.; Walker, L. M. Science, Vol. 334, Issue 6059 https://doi.org/10.1126/science.1213256	journal	October 2011
Quantification of the Impact of the HIV-1-Glycan Shield on Antibody Elicitation Zhou, Tongqing; Doria-Rose, Nicole A.; Cheng, Cheng Cell Reports, Vol. 19, Issue 4 https://doi.org/10.1016/j.celrep.2017.04.013	journal	April 2017
Structural Evolution of Glycan Recognition by a Family of Potent HIV Antibodies Garces, Fernando; Sok, Devin; Kong, Leopold Cell, Vol. 159, Issue 1 https://doi.org/10.1016/j.cell.2014.09.009	journal	September 2014
Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120 West, Anthony P.; Diskin, Ron; Nussenzweig, Michel C. Proceedings of the National Academy of Sciences, Vol. 109, Issue 30 https://doi.org/10.1073/pnas.1208984109	journal	June 2012
Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120 Kong, Leopold; Lee, Jeong Hyun; Doores, Katie J. Nature Structural & Molecular Biology, Vol. 20, Issue 7 https://doi.org/10.1038/nsmb.2594	journal	May 2013
Antibody 10-1074 suppresses viremia in HIV-1-infected individuals Caskey, Marina; Schoofs, Till; Gruell, Henning Nature Medicine, Vol. 23, Issue 2 https://doi.org/10.1038/nm.4268	journal	January 2017
A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans Sok, Devin; Pauthner, Matthias; Briney, Bryan Immunity, Vol. 45, Issue 1 https://doi.org/10.1016/j.immuni.2016.06.026	journal	July 2016
Focused Evolution of HIV-1 Neutralizing Antibodies Revealed by Structures and Deep Sequencing Wu, X.; Zhou, T.; Zhu, J. Science, Vol. 333, Issue 6049 https://doi.org/10.1126/science.1207532	journal	August 2011
Glycosylation Benchmark Profile for HIV-1 Envelope Glycoprotein Production Based on Eleven Env Trimers Go, Eden P.; Ding, Haitao; Zhang, Shijian Journal of Virology, Vol. 91, Issue 9 https://doi.org/10.1128/jvi.02428-16	journal	February 2017
Structural basis for germline gene usage of a potent class of antibodies targeting the CD4 binding site of HIV-1 gp120 West, Ap; Diskin, R.; Nussenzweig, Mc Retrovirology, Vol. 9, Issue S2 https://doi.org/10.1186/1742-4690-9-s2-o33	journal	September 2012
HIV Vaccine Design to Target Germline Precursors of Glycan-Dependent Broadly Neutralizing Antibodies Steichen, Jon M.; Kulp, Daniel W.; Tokatlian, Talar Immunity, Vol. 45, Issue 3 https://doi.org/10.1016/j.immuni.2016.08.016	journal	September 2016
HIV therapy by a combination of broadly neutralizing antibodies in humanized mice Klein, Florian; Halper-Stromberg, Ariel; Horwitz, Joshua A. Nature, Vol. 492, Issue 7427 https://doi.org/10.1038/nature11604	journal	October 2012
Stable 293 T and CHO cell lines expressing cleaved, stable HIV-1 envelope glycoprotein trimers for structural and vaccine studies Chung, Nancy PY; Matthews, Katie; Kim, Helen J. Retrovirology, Vol. 11, Issue 1 https://doi.org/10.1186/1742-4690-11-33	journal	January 2014
Structure and immune recognition of trimeric pre-fusion HIV-1 Env Pancera, Marie; Zhou, Tongqing; Druz, Aliaksandr Nature, Vol. 514, Issue 7523 https://doi.org/10.1038/nature13808	journal	October 2014
Linking Crystallographic Model and Data Quality Karplus, P. A.; Diederichs, K. Science, Vol. 336, Issue 6084 https://doi.org/10.1126/science.1218231	journal	May 2012
Attosecond pulse retrieval from noisy streaking traces with conditional variational generative network Zhu, Zheyuan; White, Jonathon; Chang, Zenghu Scientific Reports, Vol. 10, Issue 1 https://doi.org/10.1038/s41598-020-62291-6	journal	April 2020
Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer Lee, J. H.; Ozorowski, G.; Ward, A. B. Science, Vol. 351, Issue 6277 https://doi.org/10.1126/science.aad2450	journal	March 2016
Virologic effects of broadly neutralizing antibody VRC01 administration during chronic HIV-1 infection Lynch, Rebecca M.; Boritz, Eli; Coates, Emily E. Science Translational Medicine, Vol. 7, Issue 319 https://doi.org/10.1126/scitranslmed.aad5752	journal	December 2015
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination Brünger, A. T.; Adams, P. D.; Clore, G. M. Acta Crystallographica Section D Biological Crystallography, Vol. 54, Issue 5 https://doi.org/10.1107/S0907444998003254	journal	September 1998
Conformational exchange in the potassium channel blocker ShK Iwakawa, Naoto; Baxter, Nicola J.; Wai, Dorothy C. C. Scientific Reports, Vol. 9, Issue 1 https://doi.org/10.1038/s41598-019-55806-3	journal	December 2019
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody Kong, R.; Xu, K.; Zhou, T. Science, Vol. 352, Issue 6287 https://doi.org/10.1126/science.aae0474	journal	May 2016
The HIV-1 envelope glycoprotein structure: nailing down a moving target Ward, Andrew B.; Wilson, Ian A. Immunological Reviews, Vol. 275, Issue 1 https://doi.org/10.1111/imr.12507	journal	January 2017
Model Building and Refinement of a Natively Glycosylated HIV-1 Env Protein by High-Resolution Cryoelectron Microscopy Lee, Jeong Hyun; de Val, Natalia; Lyumkis, Dmitry Structure, Vol. 23, Issue 10 https://doi.org/10.1016/j.str.2015.07.020	journal	October 2015
PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome Sharma, Deepti; De Falco, Louis; Padavattan, Sivaraman Nature Communications, Vol. 10, Issue 1 https://doi.org/10.1038/s41467-019-13641-0	journal	December 2019
Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation Tillu, Vikas A.; Rae, James; Gao, Ya Nature Communications, Vol. 12, Issue 1 https://doi.org/10.1038/s41467-021-21035-4	journal	February 2021
Features and development of Coot Emsley, P.; Lohkamp, B.; Scott, W. G. Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 4 https://doi.org/10.1107/S0907444910007493	journal	March 2010
A Native-Like SOSIP.664 Trimer Based on an HIV-1 Subtype B env Gene Pugach, Pavel; Ozorowski, Gabriel; Cupo, Albert Journal of Virology, Vol. 89, Issue 6 https://doi.org/10.1128/JVI.03473-14	journal	January 2015
Antibody engineering for increased potency, breadth and half-life Sievers, Stuart A.; Scharf, Louise; West, Anthony P. Current Opinion in HIV and AIDS, Vol. 10, Issue 3 https://doi.org/10.1097/COH.0000000000000148	journal	January 2015
Two Classes of Broadly Neutralizing Antibodies within a Single Lineage Directed to the High-Mannose Patch of HIV Envelope Doores, Katie J.; Kong, Leopold; Krumm, Stefanie A. Journal of Virology, Vol. 89, Issue 2 https://doi.org/10.1128/jvi.02905-14	journal	November 2014
Structural Insights on the Role of Antibodies in HIV-1 Vaccine and Therapy West, Anthony P.; Scharf, Louise; Scheid, Johannes F. Cell, Vol. 156, Issue 4 https://doi.org/10.1016/j.cell.2014.01.052	journal	February 2014
Overview of the CCP4 suite and current developments. Winn, Martyn D.; Ballard, Charles C.; Cowtan, Kevin D. Apollo - University of Cambridge Repository https://doi.org/10.17863/cam.52322	text	January 2011
Somatic Mutations of the Immunoglobulin Framework Are Generally Required for Broad and Potent HIV-1 Neutralization Klein, Florian; Diskin, Ron; Scheid, Johannes F. Cell, Vol. 153, Issue 1 https://doi.org/10.1016/j.cell.2013.03.018	journal	March 2013
Glycans Function as Anchors for Antibodies and Help Drive HIV Broadly Neutralizing Antibody Development Andrabi, Raiees; Su, Ching-Yao; Liang, Chi-Hui Immunity, Vol. 47, Issue 5 https://doi.org/10.1016/j.immuni.2017.10.012	journal	November 2017
Multidonor Analysis Reveals Structural Elements, Genetic Determinants, and Maturation Pathway for HIV-1 Neutralization by VRC01-Class Antibodies Zhou, Tongqing; Zhu, Jiang; Wu, Xueling Immunity, Vol. 39, Issue 2 https://doi.org/10.1016/j.immuni.2013.04.012	journal	August 2013
Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals Uervirojnangkoorn, Monarin; Zeldin, Oliver B.; Lyubimov, Artem Y. eLife, Vol. 4 https://doi.org/10.7554/eLife.05421	journal	March 2015
Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion Benton, Donald J.; Wrobel, Antoni G.; Xu, Pengqi Nature, Vol. 588, Issue 7837 https://doi.org/10.1038/s41586-020-2772-0	journal	September 2020
Role of Complex Carbohydrates in Human Immunodeficiency Virus Type 1 Infection and Resistance to Antibody Neutralization Binley, James M.; Ban, Yih-En Andrew; Crooks, Emma T. Journal of Virology, Vol. 84, Issue 11 https://doi.org/10.1128/jvi.00105-10	journal	March 2010
Phaser crystallographic software McCoy, Airlie J.; Grosse-Kunstleve, Ralf W.; Adams, Paul D. Journal of Applied Crystallography, Vol. 40, Issue 4 https://doi.org/10.1107/S0021889807021206	journal	July 2007
Programmable RNA targeting by bacterial Argonaute nucleases with unconventional guide binding and cleavage specificity Lisitskaya, Lidiya; Shin, Yeonoh; Agapov, Aleksei Nature Communications, Vol. 13, Issue 1 https://doi.org/10.1038/s41467-022-32079-5	journal	August 2022
A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but Not Non-Neutralizing Antibodies Sanders, Rogier W.; Derking, Ronald; Cupo, Albert PLoS Pathogens, Vol. 9, Issue 9, Article No. e1003618 https://doi.org/10.1371/journal.ppat.1003618	journal	September 2013

Cited By (19)

Cooperation between somatic mutation and germline-encoded residues enables antibody recognition of HIV-1 envelope glycans Wu, Nelson R.; Nicely, Nathan I.; Lee, Esther M. PLOS Pathogens, Vol. 15, Issue 12 https://doi.org/10.1371/journal.ppat.1008165	journal	December 2019
Structural Definition of a Unique Neutralization Epitope on the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein Zhang, Senyan; Zhou, Panpan; Wang, Pengfei Cell Reports, Vol. 24, Issue 2 https://doi.org/10.1016/j.celrep.2018.06.041	journal	July 2018
Nylon mesh-based sample holder for fixed-target serial femtosecond crystallography Lee, Donghyeon; Baek, Sangwon; Park, Jaehyun Scientific Reports, Vol. 9, Issue 1 https://doi.org/10.1038/s41598-019-43485-z	journal	May 2019
Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide Kumar, Sonu; Sarkar, Anita; Pugach, Pavel Nature Communications, Vol. 10, Issue 1 https://doi.org/10.1038/s41467-019-08738-5	journal	February 2019
Introduction of the YTE mutation into the non-immunogenic HIV bnAb PGT121 induces anti-drug antibodies in macaques Rosenberg, Yvonne J.; Lewis, George K.; Montefiori, David C. PLOS ONE, Vol. 14, Issue 2 https://doi.org/10.1371/journal.pone.0212649	journal	February 2019
The crystal structure of dGTPase reveals the molecular basis of dGTP selectivity Barnes, Christopher O.; Wu, Ying; Song, Jinhu Proceedings of the National Academy of Sciences, Vol. 116, Issue 19 https://doi.org/10.1073/pnas.1814999116	journal	April 2019
Exploiting B Cell Receptor Analyses to Inform on HIV-1 Vaccination Strategies Kreer, Christoph; Gruell, Henning; Mora, Thierry Vaccines, Vol. 8, Issue 1 https://doi.org/10.3390/vaccines8010013	journal	January 2020
Protein and Glycan Mimicry in HIV Vaccine Design Seabright, Gemma E.; Doores, Katie J.; Burton, Dennis R. Journal of Molecular Biology, Vol. 431, Issue 12 https://doi.org/10.1016/j.jmb.2019.04.016	journal	May 2019
Kappa chain maturation helps drive rapid development of an infant HIV-1 broadly neutralizing antibody lineage Simonich, Cassandra A.; Doepker, Laura; Ralph, Duncan Nature Communications, Vol. 10, Issue 1 https://doi.org/10.1038/s41467-019-09481-7	journal	May 2019
HIV envelope trimer-elicited autologous neutralizing antibodies bind a region overlapping the N332 glycan supersite Nogal, Bartek; McCoy, Laura E.; van Gils, Marit J. Science Advances, Vol. 6, Issue 23 https://doi.org/10.1126/sciadv.aba0512	journal	June 2020
Recent progress in broadly neutralizing antibodies to HIV Sok, Devin; Burton, Dennis R. Nature Immunology, Vol. 19, Issue 11 https://doi.org/10.1038/s41590-018-0235-7	journal	October 2018
One‐step CRISPR /Cas9 method for the rapid generation of human antibody heavy chain knock‐in mice Lin, Ying‐Cing; Pecetta, Simone; Steichen, Jon M. The EMBO Journal, Vol. 37, Issue 18 https://doi.org/10.15252/embj.201899243	journal	August 2018
Opening dynamics of HIV-1 gp120 upon receptor binding is dictated by a key hydrophobic core Da, Lin-Tai; Lin, Mengna Physical Chemistry Chemical Physics, Vol. 21, Issue 47 https://doi.org/10.1039/c9cp04613e	journal	January 2019
Strategies for sample delivery for femtosecond crystallography Martiel, Isabelle; Müller-Werkmeister, Henrike M.; Cohen, Aina E. International Union of Crystallography (IUCr) https://doi.org/10.1107/s2059798318017953/ba5296sup1.pdf	text	January 2019
Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements Henderson, Rory; Lu, Maolin; Zhou, Ye Nature Communications, Vol. 11, Issue 1 https://doi.org/10.1038/s41467-019-14196-w	journal	January 2020
A generalized HIV vaccine design strategy for priming of broadly neutralizing antibody responses Steichen, Jon M.; Lin, Ying-Cing; Havenar-Daughton, Colin Science, Vol. 366, Issue 6470 https://doi.org/10.1126/science.aax4380	journal	October 2019
Quantification of the Resilience and Vulnerability of HIV-1 Native Glycan Shield at Atomistic Detail Chakraborty, Srirupa; Berndsen, Zachary T.; Hengartner, Nicolas W. SSRN Electronic Journal https://doi.org/10.2139/ssrn.3606299	journal	January 2020
Serial Femtosecond X-Ray Diffraction of HIV-1 Gag MA-IP6 Microcrystals at Ambient Temperature I. Ciftci, Halil; G. Sierra, Raymond; Yoon, Chun International Journal of Molecular Sciences, Vol. 20, Issue 7 https://doi.org/10.3390/ijms20071675	journal	April 2019
The Macromolecular Femtosecond Crystallography Instrument at the Linac Coherent Light Source Sierra, Raymond G.; Batyuk, Alexander; Sun, Zhibin Journal of Synchrotron Radiation, Vol. 26, Issue 2 https://doi.org/10.1107/s1600577519001577	journal	February 2019

Similar Records

HIV envelope V3 region mimic embodies key features of a broadly neutralizing antibody lineage epitope

Journal Article · Fri Mar 16 00:00:00 EDT 2018 · Nature Communications · OSTI ID:1624084

Fera, Daniela; Lee, Matthew S.; Wiehe, Kevin; +10 more

HIV Vaccine Design to Target Germline Precursors of Glycan-Dependent Broadly Neutralizing Antibodies

Journal Article · Thu Sep 01 00:00:00 EDT 2016 · Immunity · OSTI ID:1624084

Steichen, Jon M.; Kulp, Daniel W.; Tokatlian, Talar; +26 more

Vaccination with Glycan-Modified HIV NFL Envelope Trimer-Liposomes Elicits Broadly Neutralizing Antibodies to Multiple Sites of Vulnerability

Journal Article · Tue Nov 12 00:00:00 EST 2019 · Immunity · OSTI ID:1624084

Dubrovskaya, Viktoriya; Tran, Karen; Ozorowski, Gabriel; +25 more

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
Science & Technology - Other Topics
Glycoproteins
HIV infections
X-ray crystallography

Title: Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope

Citation Formats

References (83)

Cited By (19)

Similar Records

Related Subjects