Structure and immune recognition of trimeric prefusion HIV-1 Env
暂无分享,去创建一个
Tongqing Zhou | Yongping Yang | Baoshan Zhang | Gwo-Yu Chuang | M. Gordon Joyce | Peter D. Kwong | Jason Gorman | John R. Mascola | James B. Munro | Scott C. Blanchard | Priyamvada Acharya | Marie Pancera | Aliaksandr Druz | Ivelin S. Georgiev | Cinque S. Soto | Jinghe Huang | Gilad Ofek | Guillaume B. E. Stewart-Jones | Jonathan Stuckey | Robert T. Bailer | Mark K. Louder | Nancy Tumba | Myron S. Cohen | Barton F. Haynes | Lynn Morris | Walther Mothes | Mark Connors | B. Haynes | J. Mascola | G. Chuang | M. Connors | I. Georgiev | L. Morris | P. Acharya | Baoshan Zhang | T. Zhou | R. Bailer | M. Louder | P. Kwong | G. Ofek | Yongping Yang | J. Gorman | M. Pancera | A. Druz | M. Joyce | S. Blanchard | W. Mothes | G. Stewart-Jones | J. Stuckey | Jinghe Huang | Nancy L. Tumba | M. Cohen | Baoshan Zhang | Myron S. Cohen | Barton F. Haynes | James B. Munro
[1] Alan J. Hay,et al. Evolution of the receptor binding properties of the influenza A(H3N2) hemagglutinin , 2012, Proceedings of the National Academy of Sciences.
[2] P. Kwong,et al. Structure of Respiratory Syncytial Virus Fusion Glycoprotein in the Postfusion Conformation Reveals Preservation of Neutralizing Epitopes , 2011, Journal of Virology.
[3] Renate Kunert,et al. Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. , 2005, Immunity.
[4] Ron Diskin,et al. Sequence and Structural Convergence of Broad and Potent HIV Antibodies That Mimic CD4 Binding , 2011, Science.
[5] Z. Otwinowski,et al. [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[6] J. Sodroski,et al. Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein , 1991, Journal of virology.
[7] B. Korber,et al. Prevalence of broadly neutralizing antibody responses during chronic HIV-1 infection , 2014, AIDS.
[8] R L Stanfield,et al. Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[9] Z. Otwinowski,et al. Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[10] M. Lawrence,et al. The structural biology of type I viral membrane fusion , 2003, Nature Reviews Molecular Cell Biology.
[11] Karl Nicholas Kirschner,et al. GLYCAM06: A generalizable biomolecular force field. Carbohydrates , 2008, J. Comput. Chem..
[12] J. Sodroski,et al. Stoichiometry of Envelope Glycoprotein Trimers in the Entry of Human Immunodeficiency Virus Type 1 , 2005, Journal of Virology.
[13] M. Luftig,et al. Structural basis for HIV-1 neutralization by a gp41 fusion intermediate–directed antibody , 2006, Nature Structural &Molecular Biology.
[14] W. Weissenhorn,et al. Crystal Structure and Size-Dependent Neutralization Properties of HK20, a Human Monoclonal Antibody Binding to the Highly Conserved Heptad Repeat 1 of gp41 , 2010, PLoS pathogens.
[15] Colin Echeverría Aitken,et al. An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments. , 2008, Biophysical journal.
[16] Tongqing Zhou,et al. Structural definition of a conserved neutralization epitope on HIV-1 gp120 , 2007, Nature.
[17] Lijun Rong,et al. Role of the HIV gp120 Conserved Domain 1 in Processing and Viral Entry* , 2008, Journal of Biological Chemistry.
[18] J. Sodroski,et al. Role of the gp120 inner domain beta-sandwich in the interaction between the human immunodeficiency virus envelope glycoprotein subunits. , 2003, Virology.
[19] Boguslaw Stec,et al. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses , 2009, Nature Structural &Molecular Biology.
[20] P. S. Kim,et al. Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[21] J. Sodroski,et al. Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein , 1993, Journal of virology.
[22] John Steel,et al. Cross-neutralization of influenza A viruses mediated by a single antibody loop , 2012, Nature.
[23] J. Skehel,et al. Structure of influenza haemagglutinin at the pH of membrane fusion , 1994, Nature.
[24] Q. Sattentau,et al. Dissociation of gp120 from HIV-1 virions induced by soluble CD4. , 1990, Science.
[25] S. Harrison,et al. Atomic structure of the ectodomain from HIV-1 gp41 , 1997, Nature.
[26] Hans Frauenfelder. Tertiary Structure of Proteins , 2010 .
[27] P. Kwong,et al. Structure of a Major Antigenic Site on the Respiratory Syncytial Virus Fusion Glycoprotein in Complex with Neutralizing Antibody 101F , 2010, Journal of Virology.
[28] K. Guthrie,et al. HIV-1 membrane fusion mechanism: structural studies of the interactions between biologically-active peptides from gp41. , 1996, Biochemistry.
[29] Gwo-Yu Chuang,et al. Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-120 interface , 2014, Nature.
[30] W. Weissenhorn,et al. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. , 1998, Molecular cell.
[31] 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.
[32] Ying Sun,et al. A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding. , 1998, Science.
[33] J. Sodroski,et al. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding , 1993, Journal of virology.
[34] 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.
[35] Bette Korber,et al. Structure of a V3-Containing HIV-1 gp120 Core , 2005, Science.
[36] Z. Xiang,et al. Extending the accuracy limits of prediction for side-chain conformations. , 2001, Journal of molecular biology.
[37] Barbra A. Richardson,et al. Neutralization Escape Variants of Human Immunodeficiency Virus Type 1 Are Transmitted from Mother to Infant , 2006, Journal of Virology.
[38] Martin A. Nowak,et al. Antibody neutralization and escape by HIV-1 , 2003, Nature.
[39] Young Do Kwon,et al. Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9 , 2011, Nature.
[40] P. D. Kwong,et al. Use of cryoprotectants in combination with immiscible oils for flash cooling macromolecular crystals , 1999 .
[41] H. B. Mann,et al. On a Test of Whether one of Two Random Variables is Stochastically Larger than the Other , 1947 .
[42] Haiyan Chen,et al. Crystal structure of a non-neutralizing antibody to the HIV-1 gp41 membrane-proximal external region , 2010, Nature Structural &Molecular Biology.
[43] Randy J Read,et al. Recent developments in the PHENIX software for automated crystallographic structure determination. , 2004, Journal of synchrotron radiation.
[44] J. Sodroski,et al. Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions. , 2010, Molecular cell.
[45] Pamela J. Bjorkman,et al. Few and Far Between: How HIV May Be Evading Antibody Avidity , 2010, PLoS pathogens.
[46] D. Bolognesi,et al. A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion , 1995, Journal of virology.
[47] J. Sodroski,et al. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. , 1998, Science.
[48] A. Gronenborn,et al. Three‐dimensional solution structure of the 44 kDa ectodomain of SIV gp41 , 1998, The EMBO journal.
[49] J. Whittle,et al. Self-assembling influenza nanoparticle vaccines elicit broadly neutralizing H1N1 antibodies , 2013, Nature.
[50] Reed J. Harris,et al. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. , 1990, The Journal of biological chemistry.
[51] U. Baxa,et al. Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody , 2013, Science.
[52] John P. Moore,et al. Differential binding of neutralizing and non-neutralizing antibodies to native-like soluble HIV-1 Env trimers, uncleaved Env proteins, and monomeric subunits , 2014, Retrovirology.
[53] Pham Phung,et al. Broad and Potent Neutralizing Antibodies from an African Donor Reveal a New HIV-1 Vaccine Target , 2009, Science.
[54] F. Richards,et al. Identification of structural motifs from protein coordinate data: Secondary structure and first‐level supersecondary structure * , 1988, Proteins.
[55] Joseph Sodroski,et al. Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer , 2012, Nature Structural &Molecular Biology.
[56] J. Sodroski,et al. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody , 1998, Nature.
[57] Ian A Wilson,et al. Structural basis of enhanced binding of extended and helically constrained peptide epitopes of the broadly neutralizing HIV-1 antibody 4E10. , 2007, Journal of molecular biology.
[58] P. Brown,et al. Tyrosine sulfation in the second variable loop (V2) of HIV-1 gp120 stabilizes V2–V3 interaction and modulates neutralization sensitivity , 2014, Proceedings of the National Academy of Sciences.
[59] J. Sodroski,et al. Oligomer-specific conformations of the human immunodeficiency virus (HIV-1) gp41 envelope glycoprotein ectodomain recognized by human monoclonal antibodies. , 2009, AIDS research and human retroviruses.
[60] Gira Bhabha,et al. A common solution to group 2 influenza virus neutralization , 2013, Proceedings of the National Academy of Sciences.
[61] J. Sodroski,et al. Lack of correlation between soluble CD4-induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion events , 1992, Journal of virology.
[62] 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.
[63] Michael S. Kay,et al. Protein Design of an HIV-1 Entry Inhibitor , 2001, Science.
[64] J. Binley,et al. Nature of Nonfunctional Envelope Proteins on the Surface of Human Immunodeficiency Virus Type 1 , 2006, Journal of Virology.
[65] D. Y. Thomas,et al. Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[66] David C. Richardson,et al. MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes , 2004, Nucleic Acids Res..
[67] S. Zolla-Pazner,et al. Effects of oligomerization on the epitopes of the human immunodeficiency virus type 1 envelope glycoproteins. , 2000, Virology.
[68] S. Zolla-Pazner,et al. Distinct conformational states of HIV-1 gp41 are recognized by neutralizing and non-neutralizing antibodies , 2010, Nature Structural &Molecular Biology.
[69] 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.
[70] A. Trkola,et al. MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1 , 2011, The Journal of experimental medicine.
[71] Tongqing Zhou,et al. Delineating Antibody Recognition in Polyclonal Sera from Patterns of HIV-1 Isolate Neutralization , 2013, Science.
[72] Cinque S. Soto,et al. Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus , 2013, Science.
[73] I. Wilson,et al. Structural studies of human HIV-1 V3 antibodies. , 2006, Human antibodies.
[74] Baoshan Zhang,et al. Broad and potent neutralization of HIV-1 by a gp41-specific human antibody , 2012, Nature.
[75] A. Keating,et al. Structural specificity in coiled-coil interactions. , 2008, Current opinion in structural biology.
[76] P. Kwong,et al. Structural basis of respiratory syncytial virus neutralization by motavizumab , 2010, Nature Structural &Molecular Biology.
[77] I. Wilson,et al. Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing fabs. , 1999, Structure.
[78] James B. Munro,et al. Mitigating unwanted photophysical processes for improved single-molecule fluorescence imaging. , 2009, Biophysical journal.
[79] Nobuhiko Saitô,et al. Tertiary Structure of Proteins. I. : Representation and Computation of the Conformations , 1972 .
[80] John P. Moore,et al. CD4-induced activation in a soluble HIV-1 Env trimer. , 2014, Structure.
[81] J. Mascola,et al. HIV type 1 Env precursor cleavage state affects recognition by both neutralizing and nonneutralizing gp41 antibodies. , 2011, AIDS research and human retroviruses.
[82] A. Bartesaghi,et al. Molecular Architectures of Trimeric SIV and HIV-1 Envelope Glycoproteins on Intact Viruses: Strain-Dependent Variation in Quaternary Structure , 2010, PLoS pathogens.
[83] Peter D. Kwong,et al. The antigenic structure of the HIV gp120 envelope glycoprotein , 1998, Nature.
[84] J. Skehel,et al. N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[85] Felix Campelo,et al. Crystal Structure of HIV-1 gp41 Including Both Fusion Peptide and Membrane Proximal External Regions , 2010, PLoS pathogens.
[86] Igor A. Sidorov,et al. Concordant Modulation of Neutralization Resistance and High Infectivity of the Primary Human Immunodeficiency Virus Type 1 MN Strain and Definition of a Potential gp41 Binding Site in gp120 , 2003, Journal of Virology.
[87] Rina Levy,et al. A cis proline turn linking two β-hairpin strands in the solution structure of an antibody-bound HIV-1IIIB V3 peptide , 1999, Nature Structural Biology.
[88] Tongqing Zhou,et al. Structural Basis of Immune Evasion at the Site of CD4 Attachment on HIV-1 gp120 , 2009, Science.
[89] D. Burton,et al. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor , 2008, Nature.
[90] John P. Moore,et al. Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation , 2013, Proceedings of the National Academy of Sciences.
[91] G. Sapiro,et al. Molecular architecture of native HIV-1 gp120 trimers , 2008, Nature.
[92] P. Silver,et al. Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases. , 2007, ACS chemical biology.
[93] John P. Moore,et al. Crystal Structure of a Soluble Cleaved HIV-1 Envelope Trimer , 2013, Science.
[94] C. Bewley,et al. Structural Basis of HIV-1 Neutralization by Affinity Matured Fabs Directed against the Internal Trimeric Coiled-Coil of gp41 , 2010, PLoS Pathogens.
[95] Feng Gao,et al. Polyclonal B Cell Responses to Conserved Neutralization Epitopes in a Subset of HIV-1-Infected Individuals , 2011, Journal of Virology.
[96] Peter D. Kwong,et al. Structure and Mechanistic Analysis of the Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5 in Complex with Its gp41 Epitope , 2004, Journal of Virology.
[97] Young Do Kwon,et al. Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility , 2009, Proceedings of the National Academy of Sciences.
[98] J. Sodroski,et al. CD4-Induced T-20 Binding to Human Immunodeficiency Virus Type 1 gp120 Blocks Interaction with the CXCR4 Coreceptor , 2004, Journal of Virology.
[99] John P. Moore,et al. Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9 , 2013, Proceedings of the National Academy of Sciences.
[100] Ryan McBride,et al. Broadly Neutralizing Antibody PGT121 Allosterically Modulates CD4 Binding via Recognition of the HIV-1 gp120 V3 Base and Multiple Surrounding Glycans , 2013, PLoS pathogens.
[101] P. Kollman,et al. A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules , 1995 .
[102] Gennaro Ciliberto,et al. A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitope. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[103] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[104] Ping Zhu,et al. Antibody Domain Exchange Is an Immunological Solution to Carbohydrate Cluster Recognition , 2003, Science.
[105] Xiping Wei,et al. Human Immunodeficiency Virus Type 1 env Clones from Acute and Early Subtype B Infections for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies , 2005, Journal of Virology.
[106] Peter D. Kwong,et al. Structures of the CCR5 N Terminus and of a Tyrosine-Sulfated Antibody with HIV-1 gp120 and CD4 , 2007, Science.
[107] Peter D. Kwong,et al. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites , 2002, Nature.
[108] Yifan Cheng,et al. A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies , 2008, Proceedings of the National Academy of Sciences.
[109] Hanqin Peng,et al. Mechanism of HIV-1 Neutralization by Antibodies Targeting a Membrane-Proximal Region of gp41 , 2013, Journal of Virology.
[110] Chaim A. Schramm,et al. Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies , 2014, Nature.
[111] M. Caffrey,et al. Role of the HIV gp120 conserved domain 5 in processing and viral entry. , 2008, Biochemistry.
[112] M. Sajadi,et al. Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding , 2012, Proceedings of the National Academy of Sciences.
[113] Tongqing Zhou,et al. Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01 , 2010, Science.
[114] Han Gao,et al. Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike. , 2014, Cell reports.
[115] A. Ting,et al. Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells. , 2006, Journal of the American Chemical Society.
[116] Peter D. Kwong,et al. Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions , 2014, Science.
[117] James E. Crowe,et al. Structural Basis of Preexisting Immunity to the 2009 H1N1 Pandemic Influenza Virus , 2010, Science.
[118] John P. Moore,et al. Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer , 2013, Science.
[119] Vicki C. Ashley,et al. Initial B-Cell Responses to Transmitted Human Immunodeficiency Virus Type 1: Virion-Binding Immunoglobulin M (IgM) and IgG Antibodies Followed by Plasma Anti-gp41 Antibodies with Ineffective Control of Initial Viremia , 2008, Journal of Virology.
[120] J. Skehel,et al. Refinement of the influenza virus hemagglutinin by simulated annealing. , 1991, Journal of molecular biology.
[121] Cinque S. Soto,et al. Evaluating conformational free energies: The colony energy and its application to the problem of loop prediction , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[122] T. Zhou,et al. Enhancing protein crystallization through precipitant synergy. , 2003, Structure.
[123] Deborah Fass,et al. Core Structure of gp41 from the HIV Envelope Glycoprotein , 1997, Cell.
[124] Chaim A. Schramm,et al. Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus , 2013, Nature.
[125] I. Wilson,et al. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution , 1981, Nature.
[126] Pham Phung,et al. Broad neutralization coverage of HIV by multiple highly potent antibodies , 2011, Nature.