Differential processing of HIV envelope glycans on the virus and soluble recombinant trimer
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John R Yates | James C Paulson | Zachary Berndsen | Dennis R Burton | William R Schief | Liwei Cao | J. Diedrich | J. Yates | R. Wyatt | D. Burton | W. Schief | A. Ward | K. Rantalainen | Z. Berndsen | J. Paulson | D. Sok | S. Menis | M. Pauthner | Jolene K Diedrich | R. Andrabi | Matthias Pauthner | Lin He | Sung-Kyu Robin Park | Devin Sok | Claire M Delahunty | Sergey Menis | Raiees Andrabi | Javier Guenaga | Andrew B Ward | J. Guenaga | R. Bastidas | Liwei Cao | Kimmo Rantalainen | Raiza Bastidas | Richard T Wyatt | S. Park | C. Delahunty | Lin He
[1] John P. Moore,et al. Molecular Architecture of the Cleavage-Dependent Mannose Patch on a Soluble HIV-1 Envelope Glycoprotein Trimer , 2016, Journal of Virology.
[2] M. Crispin,et al. Cell- and Protein-Directed Glycosylation of Native Cleaved HIV-1 Envelope , 2015, Journal of Virology.
[3] E. Go,et al. cGMP production and analysis of BG505 SOSIP.664, an extensively glycosylated, trimeric HIV‐1 envelope glycoprotein vaccine candidate , 2017, Biotechnology and bioengineering.
[4] P. McKay,et al. Discrete partitioning of HIV-1 Env forms revealed by viral capture , 2015, Retrovirology.
[5] Torsten Schwede,et al. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling , 2006, Bioinform..
[6] Wayne C Koff,et al. Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers. , 2014, Immunity.
[7] Peter D. Kwong,et al. The Mannose-Dependent Epitope for Neutralizing Antibody 2G12 on Human Immunodeficiency Virus Type 1 Glycoprotein gp120 , 2002, Journal of Virology.
[8] J. Binley,et al. Nature of Nonfunctional Envelope Proteins on the Surface of Human Immunodeficiency Virus Type 1 , 2006, Journal of Virology.
[9] M. Kirschner,et al. The production of cleaved, trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein vaccine antigens and infectious pseudoviruses using linear polyethylenimine as a transfection reagent. , 2006, Protein expression and purification.
[10] John P. Moore,et al. A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but Not Non-Neutralizing Antibodies , 2013, PLoS pathogens.
[11] Dennis R Burton,et al. Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design. , 2016, Annual review of immunology.
[12] Sung Kyu Park,et al. A quantitative analysis software tool for mass spectrometry–based proteomics , 2008, Nature Methods.
[13] J. Mascola,et al. Human Immunodeficiency Virus Type 1 Neutralization Measured by Flow Cytometric Quantitation of Single-Round Infection of Primary Human T Cells , 2002, Journal of Virology.
[14] D. Baker,et al. Refinement of protein structures into low-resolution density maps using rosetta. , 2009, Journal of molecular biology.
[15] Ping Zhu,et al. Antibody Domain Exchange Is an Immunological Solution to Carbohydrate Cluster Recognition , 2003, Science.
[16] Dennis R. Burton,et al. Variable Loop Glycan Dependency of the Broad and Potent HIV-1-Neutralizing Antibodies PG9 and PG16 , 2010, Journal of Virology.
[17] Sreeurpa Ray,et al. The Cell: A Molecular Approach , 1996 .
[18] Young Do Kwon,et al. Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G , 2016, Cell.
[19] Tongqing Zhou,et al. Structural definition of a conserved neutralization epitope on HIV-1 gp120 , 2007, Nature.
[20] H. Katinger,et al. Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[21] D. Burton,et al. Identification of Common Features in Prototype Broadly Neutralizing Antibodies to HIV Envelope V2 Apex to Facilitate Vaccine Design. , 2015, Immunity.
[22] J. Yates,et al. DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. , 2002, Journal of proteome research.
[23] Weston B Struwe,et al. Composition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope Glycoprotein , 2016, Cell reports.
[24] Randy J. Read,et al. Acta Crystallographica Section D Biological , 2003 .
[25] Gary Walsh,et al. Biopharmaceutical benchmarks 2010 , 2010, Nature Biotechnology.
[26] D. Burton,et al. Identification and specificity of broadly neutralizing antibodies against HIV , 2017, Immunological reviews.
[27] J. Binley,et al. A Recombinant Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Complex Stabilized by an Intermolecular Disulfide Bond between the gp120 and gp41 Subunits Is an Antigenic Mimic of the Trimeric Virion-Associated Structure , 2000, Journal of Virology.
[28] E. Go,et al. Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility. , 2008, Journal of proteome research.
[29] Ian A Wilson,et al. Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers. , 2015, Cell reports.
[30] E. Go,et al. Glycosylation Benchmark Profile for HIV-1 Envelope Glycoprotein Production Based on Eleven Env Trimers , 2017, Journal of Virology.
[31] D. Burton,et al. Glycans Function as Anchors for Antibodies and Help Drive HIV Broadly Neutralizing Antibody Development. , 2017, Immunity.
[32] Andrew B. Ward,et al. EMHP: an accurate automated hole masking algorithm for single-particle cryo-EM image processing , 2017, bioRxiv.
[33] Gary Walsh,et al. Biopharmaceutical benchmarks , 2000, Nature Biotechnology.
[34] E. Lindahl,et al. Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2 , 2016, bioRxiv.
[35] Tongqing Zhou,et al. Structure and immune recognition of trimeric prefusion HIV-1 Env , 2014, Nature.
[36] John P. Moore,et al. Stabilization of the Soluble, Cleaved, Trimeric Form of the Envelope Glycoprotein Complex of Human Immunodeficiency Virus Type 1 , 2002, Journal of Virology.
[37] John R Yates,et al. Extracting Accurate Precursor Information for Tandem Mass Spectra by RawConverter. , 2015, Analytical chemistry.
[38] David Hua,et al. Comparative Analysis of the Glycosylation Profiles of Membrane-Anchored HIV-1 Envelope Glycoprotein Trimers and Soluble gp140 , 2015, Journal of Virology.
[39] John P. Moore,et al. CD4-induced activation in a soluble HIV-1 Env trimer. , 2014, Structure.
[40] R. Desrosiers,et al. Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding , 2016, Scientific Reports.
[41] D. Burton,et al. A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans. , 2016, Immunity.
[42] D. Burton,et al. A Broadly Neutralizing Antibody Targets the Dynamic HIV Envelope Trimer Apex via a Long, Rigidified, and Anionic β-Hairpin Structure , 2017, Immunity.
[43] Nathaniel Echols,et al. EMRinger: Side-chain-directed model and map validation for 3D Electron Cryomicroscopy , 2015, Nature Methods.
[44] Y. Durocher,et al. Therapeutic glycoprotein production in mammalian cells. , 2017, Journal of biotechnology.
[45] D. Burton,et al. Synthetic glycopeptides reveal the glycan specificity of HIV-neutralizing antibodies , 2013, Nature chemical biology.
[46] A. Ward,et al. Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer , 2016, Science.
[47] James C Paulson,et al. Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. , 2014, Immunity.
[48] John P. Moore,et al. Open and Closed Structures Reveal Allostery and Pliability in the HIV-1 Envelope Spike , 2017, Nature.
[49] A. Helenius,et al. Intracellular functions of N-linked glycans. , 2001, Science.
[50] Dennis R Burton,et al. Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens , 2010, Proceedings of the National Academy of Sciences.
[51] Kai Zhang,et al. Gctf: Real-time CTF determination and correction , 2015, bioRxiv.
[52] D. Burton,et al. The Glycan Shield of HIV Is Predominantly Oligomannose Independently of Production System or Viral Clade , 2011, PloS one.
[53] R. Wyatt,et al. Well-Ordered Trimeric HIV-1 Subtype B and C Soluble Spike Mimetics Generated by Negative Selection Display Native-like Properties , 2015, PLoS pathogens.
[54] P. Emsley,et al. Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.
[55] Baoshan Zhang,et al. Structural basis for diverse N-glycan recognition by HIV-1–neutralizing V1–V2–directed antibody PG16 , 2013, Nature Structural &Molecular Biology.
[56] J. Binley,et al. HIV-1 Virus-Like Particles Bearing Pure Env Trimers Expose Neutralizing Epitopes but Occlude Nonneutralizing Epitopes , 2012, Journal of Virology.
[57] J. Mascola,et al. Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies , 2000, Nature Medicine.
[58] J. Binley,et al. Enzyme Digests Eliminate Nonfunctional Env from HIV-1 Particle Surfaces, Leaving Native Env Trimers Intact and Viral Infectivity Unaffected , 2011, Journal of Virology.
[59] John R Yates,et al. Global site-specific N-glycosylation analysis of HIV envelope glycoprotein , 2017, Nature Communications.
[60] J. Yates,et al. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database , 1994, Journal of the American Society for Mass Spectrometry.
[61] Erdmann Rapp,et al. Quantitative mapping of glycoprotein micro-heterogeneity and macro-heterogeneity: an evaluation of mass spectrometry signal strengths using synthetic peptides and glycopeptides. , 2013, Journal of mass spectrometry : JMS.
[62] John P. Moore,et al. A Native-Like SOSIP.664 Trimer Based on an HIV-1 Subtype B env Gene , 2015, Journal of Virology.
[63] J. Diedrich,et al. Global site-specific analysis of glycoprotein N-glycan processing , 2018, Nature Protocols.
[64] M. Crispin,et al. Glycosylation profiling to evaluate glycoprotein immunogens against HIV-1 , 2017, Expert review of proteomics.
[65] Vincent B. Chen,et al. Correspondence e-mail: , 2000 .
[66] D. Agard,et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy , 2017, Nature Methods.
[67] Conrad C. Huang,et al. UCSF Chimera—A visualization system for exploratory research and analysis , 2004, J. Comput. Chem..
[68] A. Ward,et al. Model Building and Refinement of a Natively Glycosylated HIV-1 Env Protein by High-Resolution Cryoelectron Microscopy. , 2015, Structure.
[69] Dennis R. Burton,et al. A Limited Number of Antibody Specificities Mediate Broad and Potent Serum Neutralization in Selected HIV-1 Infected Individuals , 2010, PLoS pathogens.