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Science (American Association for the Advancement of Science), ISSN 1095-9203, 2011, Volume 334, Issue 6059, pp. 1097 - 1103
The HIV envelope (Env) protein gpl20 is protected from antibody recognition by a dense glycan shield. However, several of the recently identified PGT broadly... 
Polysaccharides | HIV | Neutralizing antibodies | RESEARCH ARTICLES | Antibodies | Viruses | Trimers | Epitopes | Grants | Binding sites | Crystal structure | PANEL | TRIMERS | MULTIDISCIPLINARY SCIENCES | IMMUNOGENS | ENVELOPE GLYCOPROTEIN COMPLEX | GP120 | HUMAN-IMMUNODEFICIENCY-VIRUS | MONOCLONAL-ANTIBODIES | TYPE-1 | Antibody Specificity | Mannose - immunology | Disaccharides - metabolism | Humans | Antibodies, Neutralizing - metabolism | Crystallography, X-Ray | Disaccharides - chemistry | Mannosides - chemistry | HIV Envelope Protein gp120 - metabolism | HIV Envelope Protein gp120 - immunology | Mannose - metabolism | Antibodies, Neutralizing - immunology | HIV-1 - physiology | HIV Antibodies - immunology | Immunoglobulin Fab Fragments - metabolism | Oligosaccharides - chemistry | Polysaccharides - chemistry | HIV Envelope Protein gp120 - chemistry | Mannose - chemistry | HIV Antibodies - metabolism | Protein Structure, Tertiary | Cell Line | Models, Molecular | Antibodies, Neutralizing - genetics | Glycosylation | Polysaccharides - immunology | Oligosaccharides - metabolism | HIV Antibodies - chemistry | Polysaccharides - metabolism | HIV-1 - immunology | Hydrogen Bonding | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Oligosaccharides - immunology | Protein Conformation | Mannosides - metabolism | HIV Antibodies - genetics | Immunoglobulin Fab Fragments - immunology | Mutation | Binding Sites, Antibody | Carbohydrate Conformation | Viral antibodies | Physiological aspects | Development and progression | Glycoproteins | HIV (Viruses) | Health aspects | Proteins | Antigens | Immunoglobulins | Human immunodeficiency virus--HIV
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2011, Volume 333, Issue 6049, pp. 1593 - 1602
Antibody VRC01 is a human immunoglobulin that neutralizes about 90% of HIV-1 isolates. To understand how such broadly neutralizing antibodies develop, we used... 
Germ cells | Neutralizing antibodies | B lymphocytes | RESEARCH ARTICLES | Genomics | Alleles | Antibodies | Phylogenetics | Epitopes | HIV 1 | High throughput nucleotide sequencing | DESIGN | DOMAIN | EPITOPE | MULTIDISCIPLINARY SCIENCES | BROAD | DIVERSITY | GLYCOPROTEIN | GP120 | MONOCLONAL-ANTIBODIES | SELECTION | BREADTH | Antibody Specificity | Complementarity Determining Regions - genetics | Humans | Immunoglobulin Heavy Chains - chemistry | Molecular Sequence Data | Crystallography, X-Ray | HIV Antibodies - isolation & purification | HIV Envelope Protein gp120 - metabolism | Genes, Immunoglobulin Heavy Chain | HIV Envelope Protein gp120 - immunology | Immunoglobulin Light Chains - chemistry | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HIV-1 - chemistry | Immunoglobulin J-Chains - genetics | Base Sequence | HIV Envelope Protein gp120 - chemistry | Binding Sites | Immunoglobulin Heavy Chains - immunology | Immunoglobulin Light Chains - immunology | Amino Acid Sequence | Models, Molecular | Antibody Affinity | Antibodies, Neutralizing - genetics | HIV Antibodies - chemistry | Sequence Analysis, DNA | Antibodies, Neutralizing - isolation & purification | HIV-1 - immunology | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | AIDS Vaccines | High-Throughput Nucleotide Sequencing | HIV Antibodies - genetics | Immunoglobulin Fab Fragments - immunology | Mutation | Binding Sites, Antibody | CD4 Antigens - metabolism | Evolution, Molecular | Viral antibodies | X-ray crystallography | Immunoglobulins | Physiological aspects | Genetic aspects | HIV (Viruses) | Health aspects | Methods | ANTIBODIES | IMMUNITY | BASIC BIOLOGICAL SCIENCES | GENETICS | IMMUNOGLOBULINS | CRYSTAL STRUCTURE | CRYSTALLOGRAPHY | CHAINS | 60 APPLIED LIFE SCIENCES | FUNCTIONALS
Journal Article
Nature (London), ISSN 1476-4687, 2019, Volume 570, Issue 7762, pp. 468 - 473
Broadly neutralizing monoclonal antibodies protect against infection with HIV-1 in animal models, suggesting that a vaccine that elicits these antibodies would... 
TARGET | RECOGNITION | AFFINITY | BROADLY NEUTRALIZING ANTIBODIES | MULTIDISCIPLINARY SCIENCES | VACCINE | ENVELOPE GLYCOPROTEIN | VALIDATION | VULNERABILITY | IDENTIFICATION | SUPERSITE | Immunodominant Epitopes - immunology | Clone Cells - cytology | Cell Proliferation | Vaccination | AIDS Vaccines - immunology | Macaca mulatta - immunology | Antibodies, Neutralizing - ultrastructure | Male | Antibodies, Neutralizing - immunology | Antibody Specificity - immunology | HIV Antibodies - immunology | HIV-1 - chemistry | Clone Cells - immunology | Cloning, Molecular | Female | Immunodominant Epitopes - ultrastructure | Amino Acid Sequence | Rabbits | B-Lymphocytes - cytology | Somatic Hypermutation, Immunoglobulin | Immunodominant Epitopes - chemistry | Lymphocyte Activation | Models, Molecular | Antibody Affinity | Antibodies, Neutralizing - genetics | Polysaccharides - immunology | HIV Antibodies - chemistry | Cryoelectron Microscopy | HIV Antibodies - ultrastructure | HIV-1 - immunology | Animals | B-Lymphocytes - immunology | Cross-Priming - immunology | Antibodies, Neutralizing - chemistry | Mice | HIV Antibodies - genetics | Antigen-Antibody Complex - immunology | AIDS vaccines | AIDS (Disease) | Monoclonal antibodies | Physiological aspects | B cells | Research | AIDS research | Immunological research | Animal models | Viruses | Vaccines | Virus-like particles | Design | Polysaccharides | Precursors | Human immunodeficiency virus--HIV | Antigens | Immunization | Immunoglobulins | Automation | Cloning | Envelope protein | Priming | Electron microscopy | Glycan | Microscopy | Lymphocytes B | Neutralizing | Mutation | Binding sites
Journal Article
Nature (London), ISSN 1476-4687, 2018, Volume 561, Issue 7724, pp. 479 - 484
Individuals infected with HIV-1 require lifelong antiretroviral therapy, because interruption of treatment leads to rapid rebound viraemia. Here we report on a... 
SHIV INFECTION | PRIMARY HIV-INFECTION | RESERVOIR | DURABLE CONTROL | BROADLY NEUTRALIZING ANTIBODIES | MULTIDISCIPLINARY SCIENCES | PASSIVE TRANSFER | IN-VIVO | TREATMENT INTERRUPTION | T-CELLS | HUMANIZED MICE | Antibodies, Neutralizing - administration & dosage | Humans | Middle Aged | Antibodies, Monoclonal - adverse effects | Drug Resistance, Viral | Antibodies, Monoclonal - therapeutic use | Male | Phylogeny | Anti-HIV Agents - administration & dosage | Young Adult | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - adverse effects | HIV Antibodies - immunology | HIV-1 - isolation & purification | Antibodies, Neutralizing - therapeutic use | Adult | Anti-HIV Agents - therapeutic use | Antibodies, Neutralizing - adverse effects | Female | HIV Antibodies - therapeutic use | Historically Controlled Study | Antibodies, Monoclonal - immunology | Carrier State - immunology | HIV Infections - virology | Viremia - drug therapy | HIV Antibodies - administration & dosage | Carrier State - virology | HIV-1 - immunology | Viremia - virology | Antibodies, Monoclonal - administration & dosage | Viremia - prevention & control | Adolescent | Carrier State - drug therapy | HIV Infections - drug therapy | Viremia - immunology | Aged | HIV Envelope Protein gp160 - immunology | Infusions, Intravenous | Binding Sites, Antibody | Virus Activation - immunology | Virus Latency - immunology | Anti-HIV Agents - immunology | Drug Combinations | Physiological aspects | HIV patients | Care and treatment | Drug therapy, Combination | HIV antibodies | Antiretroviral drugs | Therapy | Antiviral agents | Interruption | Immunoglobulins | Viremia | Clinical trials | Viruses | Infections | Genomes | Antiretroviral therapy | Antiretroviral agents | Lymphocytes | Human immunodeficiency virus--HIV | Monoclonal antibodies | Drug therapy | Bioinformatics | Binding sites
Journal Article
Immunity (Cambridge, Mass.), ISSN 1074-7613, 2017, Volume 46, Issue 4, pp. 690 - 702
Broadly neutralizing antibodies (bnAbs) to HIV delineate vaccine targets and are prophylactic and therapeutic agents. Some of the most potent bnAbs target a... 
broadly neutralizing antibody | HIV | PGT145 | trimer apex | envelope glycoprotein | cryo-electron microscopy | REFINEMENT | SYSTEM | PROTEIN | RECOGNITION | VALIDATION | IMMUNOLOGY | REVEAL | QUATERNARY | BINDING | FEATURES | REGION | Surface Plasmon Resonance | Epitopes - metabolism | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | Protein Multimerization | Antibodies, Neutralizing - metabolism | Crystallography, X-Ray | env Gene Products, Human Immunodeficiency Virus - metabolism | Anions - chemistry | Epitopes - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HEK293 Cells | Polysaccharides - chemistry | Protein Domains | env Gene Products, Human Immunodeficiency Virus - chemistry | HIV Antibodies - metabolism | Amino Acid Sequence | HIV-1 - metabolism | Protein Structure, Secondary | Models, Molecular | Polysaccharides - immunology | Protein Binding - immunology | HIV Antibodies - chemistry | Polysaccharides - metabolism | Cryoelectron Microscopy | Sequence Homology, Amino Acid | HIV-1 - immunology | Antibodies, Neutralizing - chemistry | Epitopes - chemistry | Atomic force microscopy | Residues | Immunoglobulins | Quaternary | Envelope protein | Antibodies | Pharmacology | Vaccines | Electron microscopy | Chemical compounds | Transmission electron microscopy | Human immunodeficiency virus--HIV | Neutralizing | Canopies | Atomic structure | Dismantling | Symmetry | Immune system
Journal Article
Nature (London), ISSN 0028-0836, 08/2014, Volume 514, Issue 7524, pp. 642 - 645
To protect against human immunodeficiency virus (HIV-1) infection, broadly neutralizing antibodies (bnAbs) must be active at the portals of viral entry in the... 
HALF-LIFE | CHALLENGE | IMMUNITY | TRANSPORT | NEUTRALIZING ANTIBODIES | HUMAN IGG1 | DENDRITIC CELLS | MULTIDISCIPLINARY SCIENCES | IN-VIVO | MONOCLONAL-ANTIBODIES | HIV-1 VACCINE | HIV Antibodies - blood | Antibodies, Neutralizing - analysis | HIV Infections - prevention & control | Immunity, Mucosal - immunology | Antibody-Dependent Cell Cytotoxicity - immunology | Half-Life | Administration, Rectal | Antibody Affinity - immunology | Male | HIV - immunology | Macaca mulatta | Antibodies, Viral - blood | Receptors, IgG - metabolism | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HIV Envelope Protein gp160 - chemistry | Antibodies, Viral - analysis | HIV - chemistry | Intestinal Mucosa - immunology | Female | Transcytosis | Simian Immunodeficiency Virus - immunology | HIV Antibodies - analysis | Mutagenesis, Site-Directed | Histocompatibility Antigens Class I - immunology | Antibody Affinity - genetics | Antibodies, Neutralizing - genetics | Binding Sites - genetics | Receptors, IgG - immunology | Rectum - immunology | Simian Acquired Immunodeficiency Syndrome - prevention & control | Animals | Receptors, Fc - immunology | Simian Acquired Immunodeficiency Syndrome - immunology | Immunization, Passive | Antibodies, Viral - immunology | HIV Envelope Protein gp160 - immunology | Mice | HIV Antibodies - genetics | Antibodies, Neutralizing - blood | Antibodies, Viral - genetics | CD4 Antigens - metabolism | Viral antibodies | Infection | Prevention | Fc receptors | Protein research | Antibodies | Primates | Research | Simian immunodeficiency virus | Health aspects | T cell receptors | Physiology | Mutation | Human immunodeficiency virus--HIV | Viral infections | Index Medicus
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2018, Volume 362, Issue 6414, pp. 598 - 602
Broadly neutralizing antibodies against highly variable pathogens have stimulated the design of vaccines and therapeutics. We report the use of diverse camelid... 
REFINEMENT | NEUTRALIZING ANTIBODIES | RECOGNITION | IMAGES | A VIRUSES | MULTIDISCIPLINARY SCIENCES | SELECTION | ELECTRON-MICROSCOPE | EFFICIENT | VACCINES | INSIGHTS | Immunodominant Epitopes - immunology | Orthomyxoviridae Infections - prevention & control | Antibodies, Neutralizing - ultrastructure | Crystallography, X-Ray | Neutralization Tests | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Peptide Library | Antibodies, Neutralizing - immunology | Camelids, New World - immunology | Madin Darby Canine Kidney Cells | Female | Influenza A virus - immunology | Influenza B virus - immunology | Immunodominant Epitopes - genetics | Single-Domain Antibodies | Immunodominant Epitopes - chemistry | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Animals | Antibodies, Viral - ultrastructure | Influenza Vaccines - immunology | Recombinant Proteins - immunology | Antibodies, Neutralizing - chemistry | Antibodies, Viral - chemistry | Dogs | Antibodies, Viral - immunology | Mice | Mice, Inbred BALB C | Antigen-antibody reactions | Care and treatment | Influenza | Research | Camelidae | Antigenic determinants | Influenza research | Pathogens | Antigens | Immunoglobulins | Gene transfer | Cross-reactivity | Vaccination | Antibodies | Viruses | Infections | Vaccines | Epitopes | Electron microscopy | Neutralizing | Hemagglutinins | Influenza A | Strains (organisms) | Crystal structure
Journal Article