Immunization expands HIV-1 V3-glycan specific B-cells in mice and macaques

[1]  Erik Lindahl,et al.  New tools for automated high-resolution cryo-EM structure determination in RELION-3 , 2018, eLife.

[2]  F. Alt,et al.  Glycan Masking Focuses Immune Responses to the HIV‐1 CD4‐Binding Site and Enhances Elicitation of VRC01‐Class Precursor Antibodies , 2018, Immunity.

[3]  J. Mascola,et al.  HIV-1 Vaccines Based on Antibody Identification, B Cell Ontogeny, and Epitope Structure. , 2018, Immunity.

[4]  L. Stamatatos,et al.  Anti–HIV-1 B cell responses are dependent on B cell precursor frequency and antigen-binding affinity , 2018, Proceedings of the National Academy of Sciences.

[5]  Thomas Höfer,et al.  Clonal selection drives protective memory B cell responses in controlled human malaria infection , 2018, Science Immunology.

[6]  B. Pulendran,et al.  Epitopes for neutralizing antibodies induced by HIV-1 envelope glycoprotein BG505 SOSIP trimers in rabbits and macaques , 2018, PLoS pathogens.

[7]  Daniel W. Kulp,et al.  Precursor Frequency and Affinity Determine B Cell Competitive Fitness in Germinal Centers, Tested with Germline‐Targeting HIV Vaccine Immunogens , 2018, Immunity.

[8]  Thomas C Terwilliger,et al.  Automated map sharpening by maximization of detail and connectivity , 2018, bioRxiv.

[9]  D. Burton,et al.  Glycans Function as Anchors for Antibodies and Help Drive HIV Broadly Neutralizing Antibody Development. , 2017, Immunity.

[10]  M. Nussenzweig,et al.  Asymmetric recognition of HIV-1 Envelope trimer by V1V2 loop-targeting antibodies , 2017, eLife.

[11]  D. Agard,et al.  MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy , 2017, Nature Methods.

[12]  David J. Fleet,et al.  cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination , 2017, Nature Methods.

[13]  B. Walker,et al.  Coexistence of potent HIV-1 broadly neutralizing antibodies and antibody-sensitive viruses in a viremic controller , 2017, Science Translational Medicine.

[14]  S. Munir Alam,et al.  Antibody‐virus co‐evolution in HIV infection: paths for HIV vaccine development , 2017, Immunological reviews.

[15]  M. Nussenzweig,et al.  Progress toward active or passive HIV-1 vaccination , 2017, The Journal of experimental medicine.

[16]  D. Burton,et al.  Identification and specificity of broadly neutralizing antibodies against HIV , 2017, Immunological reviews.

[17]  G. B. Karlsson Hedestam,et al.  Production of individualized V gene databases reveals high levels of immunoglobulin genetic diversity , 2016, Nature Communications.

[18]  M. Nussenzweig,et al.  Sequencing and cloning of antigen-specific antibodies from mouse memory B cells , 2016, Nature Protocols.

[19]  J. Mascola,et al.  Multiple Antibody Lineages in One Donor Target the Glycan-V3 Supersite of the HIV-1 Envelope Glycoprotein and Display a Preference for Quaternary Binding , 2016, Journal of Virology.

[20]  M. Nussenzweig,et al.  Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site , 2016, Nature Structural &Molecular Biology.

[21]  Daniel W. Kulp,et al.  Sequential Immunization Elicits Broadly Neutralizing Anti-HIV-1 Antibodies in Ig Knockin Mice , 2016, Cell.

[22]  Dong Soo Yun,et al.  HIV Vaccine Design to Target Germline Precursors of Glycan-Dependent Broadly Neutralizing Antibodies , 2016, Immunity.

[23]  Bryan Briney,et al.  Holes in the Glycan Shield of the Native HIV Envelope Are a Target of Trimer-Elicited Neutralizing Antibodies. , 2016, Cell reports.

[24]  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.

[25]  Dennis R Burton,et al.  Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design. , 2016, Annual review of immunology.

[26]  Michael Meyer-Hermann,et al.  Visualizing antibody affinity maturation in germinal centers , 2016, Science.

[27]  L. Stamatatos,et al.  Structural basis for germline antibody recognition of HIV-1 immunogens , 2016, eLife.

[28]  Anchi Cheng,et al.  Automated data collection in single particle electron microscopy. , 2016, Microscopy.

[29]  Karl D. Brune,et al.  Plug-and-Display: decoration of Virus-Like Particles via isopeptide bonds for modular immunization , 2016, Scientific Reports.

[30]  Keith S Wilson,et al.  Privateer: software for the conformational validation of carbohydrate structures , 2015, Nature Structural &Molecular Biology.

[31]  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.

[32]  A. Ward,et al.  Model Building and Refinement of a Natively Glycosylated HIV-1 Env Protein by High-Resolution Cryoelectron Microscopy. , 2015, Structure.

[33]  A. McDowall,et al.  Broadly Neutralizing Antibody 8ANC195 Recognizes Closed and Open States of HIV-1 Env , 2015, Cell.

[34]  Kai Zhang,et al.  Gctf: Real-time CTF determination and correction , 2015, bioRxiv.

[35]  John P. Moore,et al.  Structural Evolution of Glycan Recognition by a Family of Potent HIV Antibodies , 2014, Cell.

[36]  Florian Klein,et al.  Structural Insights on the Role of Antibodies in HIV-1 Vaccine and Therapy , 2014, Cell.

[37]  Hemant D. Tagare,et al.  The Local Resolution of Cryo-EM Density Maps , 2013, Nature Methods.

[38]  Daphne Koller,et al.  The Effects of Somatic Hypermutation on Neutralization and Binding in the PGT121 Family of Broadly Neutralizing HIV Antibodies , 2013, PLoS pathogens.

[39]  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.

[40]  Yan Liu,et al.  Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120 , 2013, Nature Structural &Molecular Biology.

[41]  Tongqing Zhou,et al.  Somatic Mutations of the Immunoglobulin Framework Are Generally Required for Broad and Potent HIV-1 Neutralization , 2013, Cell.

[42]  Michael S. Seaman,et al.  Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies , 2012, Proceedings of the National Academy of Sciences.

[43]  Shaoxia Chen,et al.  Prevention of overfitting in cryo-EM structure determination , 2012, Nature Methods.

[44]  B. Zakeri,et al.  Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin , 2012, Proceedings of the National Academy of Sciences.

[45]  M. Nussenzweig,et al.  Dopamine in germinal centers , 2017, Nature Immunology.

[46]  Pham Phung,et al.  Broad neutralization coverage of HIV by multiple highly potent antibodies , 2011, Nature.

[47]  Ron Diskin,et al.  Sequence and Structural Convergence of Broad and Potent HIV Antibodies That Mimic CD4 Binding , 2011, Science.

[48]  M. Nussenzweig,et al.  A dynamic T cell–limited checkpoint regulates affinity-dependent B cell entry into the germinal center , 2011, The Journal of experimental medicine.

[49]  Ron Diskin,et al.  Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity , 2010, Nature Structural &Molecular Biology.

[50]  P. Emsley,et al.  Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.

[51]  A. Tissot,et al.  Versatile Virus-Like Particle Carrier for Epitope Based Vaccines , 2010, PloS one.

[52]  Randy J. Read,et al.  Acta Crystallographica Section D Biological , 2003 .

[53]  Vincent B. Chen,et al.  Correspondence e-mail: , 2000 .

[54]  David C Montefiori,et al.  Measuring HIV neutralization in a luciferase reporter gene assay. , 2009, Methods in molecular biology.

[55]  Conrad C. Huang,et al.  Visualizing density maps with UCSF Chimera. , 2007, Journal of structural biology.

[56]  M. Nussenzweig,et al.  Role of BCR affinity in T cell–dependent antibody responses in vivo , 2002, Nature Immunology.

[57]  M. Shlomchik,et al.  Antigen drives very low affinity B cells to become plasmacytes and enter germinal centers. , 1998, Journal of immunology.

[58]  P. Bjorkman,et al.  High-affinity binding of the neonatal Fc receptor to its IgG ligand requires receptor immobilization. , 1997, Biochemistry.

[59]  G. Rimmelzwaan,et al.  Refocusing neutralizing antibody response by targeted dampening of an immunological epitope , 2001 .