Structural Rearrangements Maintain the Glycan Shield of an HIV-1 Envelope Trimer After the Loss of a Glycan
暂无分享,去创建一个
Simon A. A. Travers | Robert J Woods | Oliver C Grant | Oliver C. Grant | S. Travers | R. Woods | J. Dorfman | N. Wood | Roux-Cil Ferreira | Thandeka Moyo | Jeffrey R Dorfman | Simon A Travers | Natasha T Wood | Roux-Cil Ferreira | Thandeka Moyo
[1] Cinque S. Soto,et al. Quantification of the Impact of the HIV-1-Glycan Shield on Antibody Elicitation. , 2017, Cell reports.
[2] Xuesong Yu,et al. Factors Associated with the Development of Cross-Reactive Neutralizing Antibodies during Human Immunodeficiency Virus Type 1 Infection , 2008, Journal of Virology.
[3] M. Gonda,et al. Characterization of envelope and core structural gene products of HTLV-III with sera from AIDS patients. , 1985, Science.
[4] K. Tomer,et al. Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells. , 2000, Biochemistry.
[5] B. Korber,et al. Prevalence of broadly neutralizing antibody responses during chronic HIV-1 infection , 2014, AIDS.
[6] Peter D. Kwong,et al. The antigenic structure of the HIV gp120 envelope glycoprotein , 1998, Nature.
[7] Daniel R Roe,et al. PTRAJ and CPPTRAJ: Software for Processing and Analysis of Molecular Dynamics Trajectory Data. , 2013, Journal of chemical theory and computation.
[8] Hui Zhang,et al. Glycoform Analysis of Recombinant and Human Immunodeficiency Virus Envelope Protein gp120 via Higher Energy Collisional Dissociation and Spectral-Aligning Strategy , 2014, Analytical chemistry.
[9] L. Deterding,et al. Characterization of glycopeptides from HIV-ISF2 gp120 by liquid chromatography mass spectrometry , 2004, Journal of the American Society for Mass Spectrometry.
[10] Hans Wolf,et al. Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS , 1986, Cell.
[11] Michael W. Mahoney,et al. A five-site model for liquid water and the reproduction of the density anomaly by rigid, nonpolarizable potential functions , 2000 .
[12] Young Do Kwon,et al. Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9 , 2011, Nature.
[13] T. Blundell,et al. Comparative protein modelling by satisfaction of spatial restraints. , 1993, Journal of molecular biology.
[14] B. Haynes,et al. HIV‐1 neutralizing antibodies: understanding nature's pathways , 2013, Immunological reviews.
[15] Karl Nicholas Kirschner,et al. GLYCAM06: A generalizable biomolecular force field. Carbohydrates , 2008, J. Comput. Chem..
[16] J. Stadlmann,et al. Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140 , 2012, Biological chemistry.
[17] S. Zolla-Pazner,et al. Structure/Function Studies Involving the V3 Region of the HIV-1 Envelope Delineate Multiple Factors That Affect Neutralization Sensitivity , 2015, Journal of Virology.
[18] Young Do Kwon,et al. Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G , 2016, Cell.
[19] Leo S. D. Caves,et al. Bio3d: An R Package , 2022 .
[20] G. Nakamura,et al. Neutralization of the AIDS retrovirus by antibodies to a recombinant envelope glycoprotein. , 1986, Science.
[21] A. Grafmüller,et al. Solution Properties of Hemicellulose Polysaccharides with Four Common Carbohydrate Force Fields. , 2015, Journal of chemical theory and computation.
[22] Ben M. Webb,et al. Comparative Protein Structure Modeling Using MODELLER , 2016, Current protocols in bioinformatics.
[23] Feng Gao,et al. Polyclonal B Cell Responses to Conserved Neutralization Epitopes in a Subset of HIV-1-Infected Individuals , 2011, Journal of Virology.
[24] Tongqing Zhou,et al. Structure and immune recognition of trimeric prefusion HIV-1 Env , 2014, Nature.
[25] J. Chermann,et al. Identification and antigenicity of the major envelope glycoprotein of lymphadenopathy-associated virus. , 1985, Virology.
[26] Cinque S. Soto,et al. Microsecond Dynamics and Network Analysis of the HIV-1 SOSIP Env Trimer Reveal Collective Behavior and Conserved Microdomains of the Glycan Shield. , 2017, Structure.
[27] John P. Moore,et al. Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer , 2013, Science.
[28] Feng Gao,et al. Cooperation of B Cell Lineages in Induction of HIV-1-Broadly Neutralizing Antibodies , 2014, Cell.
[29] 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.
[30] Douglas A. Lauffenburger,et al. Exploiting glycan topography for computational design of Env glycoprotein antigenicity , 2018, PLoS Comput. Biol..
[31] A. Trkola,et al. Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization. , 1994, AIDS research and human retroviruses.
[32] L. Morris,et al. The C3-V4 Region Is a Major Target of Autologous Neutralizing Antibodies in Human Immunodeficiency Virus Type 1 Subtype C Infection , 2007, Journal of Virology.
[33] Andrej Sali,et al. Comparative Protein Structure Modeling Using MODELLER , 2014, Current protocols in bioinformatics.
[34] Barbra A. Richardson,et al. Removal of a Single N-Linked Glycan in Human Immunodeficiency Virus Type 1 gp120 Results in an Enhanced Ability To Induce Neutralizing Antibody Responses , 2007, Journal of Virology.
[35] J. Overbaugh,et al. Human Immunodeficiency Virus Type 1 V1-V2 Envelope Loop Sequences Expand and Add Glycosylation Sites over the Course of Infection, and These Modifications Affect Antibody Neutralization Sensitivity , 2006, Journal of Virology.
[36] Shiu-Lok Hu,et al. Conserved Role of an N-Linked Glycan on the Surface Antigen of Human Immunodeficiency Virus Type 1 Modulating Virus Sensitivity to Broadly Neutralizing Antibodies against the Receptor and Coreceptor Binding Sites , 2015, Journal of Virology.
[37] Raymond A Dwek,et al. Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding. , 2003, Glycobiology.
[38] Pham Phung,et al. Broad and Potent Neutralizing Antibodies from an African Donor Reveal a New HIV-1 Vaccine Target , 2009, Science.
[39] Ben M. Webb,et al. Comparative Protein Structure Modeling Using MODELLER , 2007, Current protocols in protein science.
[40] Pham Phung,et al. Broad neutralization coverage of HIV by multiple highly potent antibodies , 2011, Nature.
[41] Mario Roederer,et al. Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1 , 2010, Science.
[42] D. Richman,et al. Rapid evolution of the neutralizing antibody response to HIV type 1 infection , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[43] Conrad C. Huang,et al. UCSF Chimera—A visualization system for exploratory research and analysis , 2004, J. Comput. Chem..
[44] E. Go,et al. Comparison of HPLC/ESI-FTICR MS versus MALDI-TOF/TOF MS for glycopeptide analysis of a highly glycosylated HIV envelope glycoprotein , 2008, Journal of the American Society for Mass Spectrometry.
[45] Simon A. A. Travers,et al. Chinks in the armor of the HIV-1 Envelope glycan shield: Implications for immune escape from anti-glycan broadly neutralizing antibodies. , 2017, Virology.
[46] L. Stamatatos,et al. N-Linked Glycosylation of the V3 Loop and the Immunologically Silent Face of gp120 Protects Human Immunodeficiency Virus Type 1 SF162 from Neutralization by Anti-gp120 and Anti-gp41 Antibodies , 2004, Journal of Virology.
[47] A. Sali,et al. Statistical potential for assessment and prediction of protein structures , 2006, Protein science : a publication of the Protein Society.
[48] William R. Schief,et al. Promiscuous Glycan Site Recognition by Antibodies to the High-Mannose Patch of gp120 Broadens Neutralization of HIV , 2014, Science Translational Medicine.
[49] S. Travers. Conservation, Compensation, and Evolution of N-Linked Glycans in the HIV-1 Group M Subtypes and Circulating Recombinant Forms , 2012, ISRN AIDS.
[50] C. Simmerling,et al. ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB. , 2015, Journal of chemical theory and computation.
[51] Martin A. Nowak,et al. Antibody neutralization and escape by HIV-1 , 2003, Nature.
[52] Renate Kunert,et al. Comprehensive Cross-Clade Neutralization Analysis of a Panel of Anti-Human Immunodeficiency Virus Type 1 Monoclonal Antibodies , 2004, Journal of Virology.
[53] S. Kornfeld,et al. Assembly of asparagine-linked oligosaccharides. , 1985, Annual review of biochemistry.
[54] Richard T. Wyatt,et al. Selection Pressure on HIV-1 Envelope by Broadly Neutralizing Antibodies to the Conserved CD4-Binding Site , 2012, Journal of Virology.
[55] G Himmler,et al. A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1 , 1993, Journal of virology.
[56] E. Go,et al. Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins. , 2013, Journal of proteome research.
[57] M. Crispin,et al. Structural principles controlling HIV envelope glycosylation. , 2017, Current opinion in structural biology.
[58] Bette Korber,et al. Structure of a V3-Containing HIV-1 gp120 Core , 2005, Science.
[59] 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.
[60] B. Berkhout,et al. The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion , 2008, Retrovirology.
[61] Lai-Xi Wang,et al. Conformational Heterogeneity of the HIV Envelope Glycan Shield , 2017, Scientific Reports.
[62] Lynn Morris,et al. Evolution of an HIV glycan–dependent broadly neutralizing antibody epitope through immune escape , 2012, Nature Medicine.
[63] Christoph Grundner,et al. Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition. , 2003, Virology.
[64] E. Go,et al. Characterization of Glycosylation Profiles of HIV-1 Transmitted/Founder Envelopes by Mass Spectrometry , 2011, Journal of Virology.
[65] David Yang,et al. The N-Terminal V3 Loop Glycan Modulates the Interaction of Clade A and B Human Immunodeficiency Virus Type 1 Envelopes with CD4 and Chemokine Receptors , 2000, Journal of Virology.
[66] E. Go,et al. Glycosylation and Disulfide Bond Analysis of Transiently and Stably Expressed Clade C HIV-1 gp140 Trimers in 293T Cells Identifies Disulfide Heterogeneity Present in Both Proteins and Differences in O-Linked Glycosylation , 2014, Journal of proteome research.
[67] E. Go,et al. Glycosylation site-specific analysis of clade C HIV-1 envelope proteins. , 2009, Journal of proteome research.
[68] Steven Wolinsky,et al. Loss of the N-linked glycosylation site at position 386 in the HIV envelope V4 region enhances macrophage tropism and is associated with dementia. , 2007, Virology.
[69] Ian A Wilson,et al. The HIV‐1 envelope glycoprotein structure: nailing down a moving target , 2017, Immunological reviews.
[70] John P. Moore,et al. Crystal Structure of a Soluble Cleaved HIV-1 Envelope Trimer , 2013, Science.
[71] M. Crispin,et al. Glycan Microheterogeneity at the PGT135 Antibody Recognition Site on HIV-1 gp120 Reveals a Molecular Mechanism for Neutralization Resistance , 2015, Journal of Virology.
[72] 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.
[73] T. Copeland,et al. Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene. , 1985, Science.
[74] J. Nie,et al. A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization , 2013, Retrovirology.
[75] Tongqing Zhou,et al. Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01 , 2010, Science.
[76] J. Mascola,et al. HIV-1 Fitness Cost Associated with Escape from the VRC01 Class of CD4 Binding Site Neutralizing Antibodies , 2015, Journal of Virology.