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by Doria-Rose, Nicole A and Schramm, Chaim A and Gorman, Jason and Moore, Penny L and Bhiman, Jinal N and Dekosky, Brandon J and Ernandes, Michael J and Georgiev, Ivelin S and Kim, Helen J and Pancera, Marie and Staupe, Ryan P and Altae-Tran, Han R and Bailer, Robert T and Crooks, Ema T and Cupo, Albert and z, Aliaksan and Garrett, Nigel J and Hoi, Kam H and Kong, Rui and Louder, Mark K and Longo, Nancy S and McKee, Krisha and Nonyane, Molati and O'Dell, Sijy and Roark, Ryan S and Rudicell, Rebecca S and Schmidt, Stephen D and Sheward, Daniel J and Soto, Cinque and Wibmer, Constantinos Kurt and Yang, Yongping and Zhang, Zhenhai and Mullikin, James C and Binley, James M and Sanders, Rogier W and Wilson, Ian A and Moore, John P and Ward, Anew B and Georgiou, George and Williamson, Carolyn and Abdool Karim, Salim S and Morris, Lynn and Kwong, Peter D and Shapiro, Lawrence and Mascola, John R and Becker, Jesse and Benjamin, Betty and Blakesley, Robert and Bouffard, Gerry and Brooks, Shelise and Coleman, Holly and Dekhtyar, Mila and Gregory, Michael and Guan, Xiaobin and Gupta, Jyoti and Han, Joel and Hargrove, April and Ho, Shi-ling and Johnson, Taccara and Legaspi, Richelle and Lovett, Sean and Maduro, Quino and Masiello, Cathy and Maskeri, Baishali and McDowell, Jenny and Montemayor, Casana and Mullikin, James and Park, Morgan and Riebow, Nancy and Schandler, Karen and Schmidt, Brian and Sison, Christina and Stantripop, Mal and Thomas, James and Thomas, Pam and Vemulapalli, Meg and Young, Alice and NISC Comparative Sequencing and NISC Comparative Sequencing Program
Nature, ISSN 0028-0836, 2014, Volume 509, Issue 7498, pp. 55 - 62
Antibodies capable of neutralizing HIV-1 often target variable regions 1 and 2 (V1V2) of the HIV-1 envelope, but the mechanism of their elicitation has been... 
B-CELLS | MAXIMUM-LIKELIHOOD | STRUCTURAL BASIS | HIV-1-NEUTRALIZING ANTIBODIES | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | VACCINE EFFICACY | INFECTION | BROAD | HUMAN MONOCLONAL-ANTIBODIES | ENVELOPE TRIMER | Complementarity Determining Regions - genetics | Epitope Mapping | Epitopes, B-Lymphocyte - chemistry | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Antibody Affinity - immunology | Neutralization Tests | Epitopes, B-Lymphocyte - immunology | HIV Antibodies - isolation & purification | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HIV Envelope Protein gp160 - chemistry | Complementarity Determining Regions - chemistry | HIV-1 - chemistry | Binding Sites - immunology | B-Lymphocytes - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | CD4 Antigens - immunology | B-Lymphocytes - cytology | Models, Molecular | Antibody Affinity - genetics | Antibodies, Neutralizing - genetics | HIV Antibodies - chemistry | AIDS Vaccines - chemistry | Antibodies, Neutralizing - isolation & purification | Cell Lineage | HIV-1 - immunology | B-Lymphocytes - immunology | Antibodies, Neutralizing - chemistry | Complementarity Determining Regions - immunology | HIV Envelope Protein gp160 - immunology | HIV Antibodies - genetics | Somatic Hypermutation, Immunoglobulin - genetics | CD4 Antigens - metabolism | Evolution, Molecular | Viral antibodies | Antigen-antibody reactions | AIDS vaccines | AIDS (Disease) | Antibodies | Physiological aspects | Research | AIDS research | Cell culture | Genes | Human immunodeficiency virus--HIV | Phylogenetics | Amino acids | Infections | Genomes | Mutation
Journal Article
Journal Article
PLoS Pathogens, ISSN 1553-7366, 05/2015, Volume 11, Issue 5, p. e1004932
Journal Article
Immunity, ISSN 1074-7613, 05/2017, Volume 46, Issue 5, pp. 777 - 791.e10
Most HIV-1-specific neutralizing antibodies isolated to date exhibit unusual characteristics that complicate their elicitation. Neutralizing antibodies that... 
V1V2 | antibody | bnAb | HIV | trimer | neutralization | glycan shield | VLP | B cell ontogeny | CDRH3 | vaccine-design template | NAb | CONFORMATIONAL EPITOPE | RECOGNITION | BROAD | FUSION PEPTIDE | IMMUNOLOGY | MONOCLONAL-ANTIBODIES | IDENTIFICATION | REVEAL | ELECTRON-MICROSCOPE | QUATERNARY | ENVELOPE TRIMERS | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | Protein Multimerization | Antibodies, Neutralizing - metabolism | Vaccines, Virus-Like Particle - metabolism | Phylogeny | HIV Envelope Protein gp120 - metabolism | Vaccines, Virus-Like Particle - chemistry | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | Complementarity Determining Regions - chemistry | Peptide Fragments - immunology | Protein Interaction Domains and Motifs | HIV Envelope Protein gp120 - chemistry | Binding Sites | B-Lymphocytes - metabolism | HIV Antibodies - metabolism | Amino Acid Sequence | Peptide Fragments - metabolism | HIV Infections - virology | Models, Molecular | HIV Antibodies - chemistry | HIV-1 - immunology | Peptide Fragments - chemistry | B-Lymphocytes - immunology | Antibodies, Neutralizing - chemistry | Complementarity Determining Regions - immunology | Protein Binding | Protein Conformation | Vaccines, Virus-Like Particle - immunology | Viral antibodies | Medical research | Crystals | Medicine, Experimental | Antibodies | Research institutes | Structure | HIV (Viruses) | Immunoglobulins | Recombination | Particulates | Viruses | Vaccines | Virus-like particles | Lymphocytes B | Plasmids | Human immunodeficiency virus--HIV | Probes | Binding sites | Crystal structure
Journal Article
PLoS Pathogens, ISSN 1553-7366, 05/2018, Volume 14, Issue 5, p. e1007024
The extensive glycosylation of HIV-1 envelope (Env) glycoprotein leaves few glycan-free holes large enough to admit broadly neutralizing antibodies (bnAb).... 
B-CELL RECEPTORS | BROAD NEUTRALIZATION | CD4 BINDING-SITE | ENVELOPE GLYCOPROTEIN | MICROBIOLOGY | V2 APEX | CONFORMATIONAL EPITOPE | VIROLOGY | VACCINE DESIGN | IMMUNODEFICIENCY-VIRUS TYPE-1 | SYNTHETIC GLYCOPEPTIDES | NONNEUTRALIZING EPITOPES | PARASITOLOGY | HIV Envelope Protein gp41 - immunology | Humans | HIV Envelope Protein gp41 - metabolism | Antibodies, Neutralizing - pharmacology | Glycosylation | Polysaccharides - immunology | HIV Envelope Protein gp120 - metabolism | Polysaccharides - metabolism | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV Antibodies - immunology | Leukocytes, Mononuclear - immunology | HIV Envelope Protein gp120 - blood | HIV Infections - therapy | Protein Conformation | Antibodies, Neutralizing - blood | HIV Envelope Protein gp41 - blood | Viral antibodies | Antibodies | Polysaccharides | HIV (Viruses) | Antigenic determinants | Glycemic index | Research | Neutralization (Chemistry) | Biomedical research | Laboratories | Infections | Vaccines | Glucose | Proteins | Immunology | Exo-a-sialidase | Human immunodeficiency virus--HIV | Peripheral blood mononuclear cells | Research centers | Immunoglobulins | Glycoprotein gp41 | Maturation | Saturation | Glycoprotein | Glycoproteins | Trimers | Epitopes | Glycan | Virology | Sensitivity | Infectious diseases | Neutralizing | Software | Galactose | Endoplasmic reticulum | Glycoprotein gp120 | Neutralization | HIV | Human immunodeficiency virus
Journal Article
Journal Article
Virology, ISSN 0042-6822, 2014, Volume 456, Issue 1, pp. 55 - 69
Abstract Virus-like particles (VLPs) offer a platform to test the hypothesis that, since antibody binding to native envelope glycoprotein (Env) trimers results... 
Infectious Disease | VLPs | HIV | Antibody | gp41 | gp120 | Vaccine | Env | Neutralization | Gp41 | Gp120 | ENVELOPE PROTEINS | VIROLOGY | IMMUNE-RESPONSES | SURFACE GLYCOPROTEIN | BINDING-SITE | TYPE-1 HIV-1 | MONOCLONAL-ANTIBODIES | EPITOPES | Virus diseases | Evaluation | Proteases | Analysis | Immunoglobulin G | HIV (Viruses) | Antigenic determinants | vaccine | antibody | neutralization
Journal Article