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Science, ISSN 0036-8075, 11/2011, 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 | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 2014, Volume 515, Issue 7525, pp. 138 - 142
The isolation of human monoclonal antibodies is providing important insights into the specificities that underlie broad neutralization of HIV-1 (reviewed in... 
B-CELLS | SPECIFICITIES | MULTIDISCIPLINARY SCIENCES | SERA | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENV TRIMERS | VULNERABILITY | GP120 | HUMAN MONOCLONAL-ANTIBODIES | CLEAVAGE | DEPENDENT EPITOPE | Immunoglobulin Fab Fragments - ultrastructure | Antibody Specificity | Epitope Mapping | HIV Envelope Protein gp41 - immunology | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Leukocytes, Mononuclear | HIV Envelope Protein gp41 - chemistry | Virus Internalization - drug effects | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | Receptors, CCR5 - metabolism | HIV Antibodies - immunology | Conserved Sequence | Inhibitory Concentration 50 | HIV Envelope Protein gp120 - chemistry | HIV Antibodies - pharmacology | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Cell Line | Immunoglobulin Fab Fragments - genetics | HIV-1 - drug effects | Antibodies, Monoclonal - pharmacology | Models, Molecular | Antibodies, Neutralizing - pharmacology | Antibody Affinity | Antibodies, Neutralizing - genetics | HIV Antibodies - chemistry | AIDS Vaccines - chemistry | Antibodies, Monoclonal - genetics | HIV-1 - immunology | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Cell Membrane - virology | Epitopes - chemistry | HIV Antibodies - genetics | Immunoglobulin Fab Fragments - immunology | CD4 Antigens - metabolism | Viral antibodies | Care and treatment | Antibodies | Physiological aspects | Genetic aspects | Research | HIV infection | Antigenic determinants | Amino acids | Mutation | Vaccines | Human immunodeficiency virus--HIV | Binding sites | Index Medicus
Journal Article
Science, ISSN 0036-8075, 9/2011, 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 | Index Medicus | ANTIBODIES | IMMUNITY | BASIC BIOLOGICAL SCIENCES | GENETICS | IMMUNOGLOBULINS | CRYSTAL STRUCTURE | CRYSTALLOGRAPHY | CHAINS | 60 APPLIED LIFE SCIENCES | FUNCTIONALS
Journal Article
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 | Index Medicus
Journal Article
Science, ISSN 0036-8075, 9/2011, Volume 333, Issue 6049, pp. 1633 - 1637
Passive transfer of broadly neutralizing HIV antibodies can prevent infection, which suggests that vaccines that elicit such antibodies would be protective.... 
Germ cells | HIV | B lymphocytes | Neutralizing antibodies | REPORTS | Antibodies | Bone marrow | Plasma cells | Viruses | Trimers | Inhibitory concentration 50 | INDIVIDUALS | MEMORY B-CELLS | NEUTRALIZING ANTIBODIES | EPITOPE | TYPE-1 GP120 | MULTIDISCIPLINARY SCIENCES | GP41 | ENVELOPE GLYCOPROTEIN | RECEPTOR | HUMAN-IMMUNODEFICIENCY-VIRUS | HUMAN MONOCLONAL-ANTIBODIES | Consensus Sequence | Antibody Specificity | Humans | Antibodies, Neutralizing - metabolism | Immunoglobulin Heavy Chains - chemistry | Molecular Sequence Data | Crystallography, X-Ray | HIV Envelope Protein gp120 - metabolism | Genes, Immunoglobulin Heavy Chain | HIV Envelope Protein gp120 - immunology | Immunoglobulin Light Chains - chemistry | HIV Infections - immunology | Antibodies, Neutralizing - immunology | Molecular Mimicry | HIV Antibodies - immunology | Cloning, Molecular | HIV Envelope Protein gp120 - chemistry | Binding Sites | HIV Antibodies - metabolism | Amino Acid Sequence | CD4 Antigens - immunology | Antibody Affinity | HIV Antibodies - chemistry | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Protein Conformation | Mutation | Binding Sites, Antibody | CD4 Antigens - metabolism | HIV antibodies | Physiological aspects | Genetic aspects | Research | Nucleotide sequencing | Health aspects | Protein binding | Proteins | Immunoglobulins | Vaccines | Human immunodeficiency virus--HIV | Binding sites | Polyclonal antibodies | Index Medicus
Journal Article
by Liao, Hua-Xin and Lynch, Rebecca and Zhou, Tongqing and Gao, Feng and Munir Alam, S and Boyd, Scott D and Fire, Andrew Z and Roskin, Krishna M and Schramm, Chaim A and Zhang, Zhenhai and Zhu, Jiang and Shapiro, Lawrence and Mullikin, James C and Gnanakaran, S and Hraber, Peter and Wiehe, Kevin and Kelsoe, Garnett and Yang, Guang and Xia, Shi-Mao and Montefiori, David C and Parks, Robert and Lloyd, Krissey E and Scearce, Richard M and Soderberg, Kelly A and Cohen, Myron and Kamanga, Gift and Louder, Mark K and Tran, Lillian M and Chen, Yue and Cai, Fangping and Chen, Sheri and Moquin, Stephanie and Du, Xiulian and Gordon Joyce, M and Srivatsan, Sanjay and Zhang, Baoshan and Zheng, Anqi and Shaw, George M and Hahn, Beatrice H and Kepler, Thomas B and Korber, Bette T. M and Kwong, Peter D and Mascola, John R and Haynes, Barton F 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, Casandra and Mulliki, 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 Progra and NISC Comparative Sequencing Program
Nature, ISSN 0028-0836, 04/2013, Volume 496, Issue 7446, pp. 469 - 476
Current human immunodeficiency virus-1 (HIV-1) vaccines elicit strain-specific neutralizing antibodies. However, cross-reactive neutralizing antibodies arise... 
B-CELL RESPONSES | CONFORMATIONAL EPITOPE | POTENT NEUTRALIZATION | CD4 BINDING-SITE | VACCINE DESIGN | MULTIDISCIPLINARY SCIENCES | ENVELOPE GLYCOPROTEIN | HIV-1-INFECTED INDIVIDUALS | HUMAN MONOCLONAL-ANTIBODIES | SUBTYPE-B | IN-SITU PROTEOLYSIS | HIV Envelope Protein gp120 - genetics | Clone Cells - cytology | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Crystallography, X-Ray | Neutralization Tests | Phylogeny | HIV Envelope Protein gp120 - metabolism | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HIV-1 - chemistry | HIV Envelope Protein gp120 - chemistry | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Protein Structure, Tertiary | Amino Acid Sequence | CD4 Antigens - immunology | Africa | Cells, Cultured | Models, Molecular | Antibodies, Neutralizing - genetics | Cross Reactions - immunology | HIV Antibodies - chemistry | HIV-1 - classification | Antibodies, Monoclonal - genetics | Cell Lineage | HIV-1 - immunology | CD4 Antigens - chemistry | Antibodies, Neutralizing - chemistry | Epitopes - chemistry | HIV Antibodies - genetics | Mutation | Evolution, Molecular | Monoclonal antibodies | AIDS vaccines | Genetic aspects | Research | HIV (Viruses) | Properties | Proteins | Plasma | Infections | Patients | Binding sites | Crystal structure | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 12/2011, Volume 480, Issue 7377, pp. 336 - 343
Variable regions 1 and 2 (V1/V2) of human immunodeficiency virus-1 (HIV-1) gp120 envelope glycoprotein are critical for viral evasion of antibody... 
SYSTEM | POTENT NEUTRALIZATION | DEXTRAN SULFATE | EPITOPE | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENVELOPE GLYCOPROTEIN | RECEPTOR | BINDING | T-CELLS | SOFTWARE | AIDS Vaccines - immunology | Glycopeptides - chemistry | Molecular Sequence Data | Antibody Affinity - immunology | Crystallography, X-Ray | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | Glycopeptides - immunology | Antibody Specificity - immunology | HIV Antibodies - immunology | HIV-1 - chemistry | Protein Structure, Quaternary | Conserved Sequence | Polysaccharides - chemistry | HIV Envelope Protein gp120 - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Binding Sites, Antibody - immunology | Models, Molecular | Glycosylation | Polysaccharides - immunology | HIV Antibodies - chemistry | AIDS Vaccines - chemistry | Amino Acid Motifs | HIV-1 - immunology | Immune Evasion | Hydrogen Bonding | Antigen-Antibody Complex - chemistry | Antibodies, Neutralizing - chemistry | Epitopes - chemistry | Antigen-Antibody Complex - immunology | Viral envelopes | Genetic aspects | Research | HIV (Viruses) | Structure | Binding sites (Biochemistry) | Proteins | Crystals | Vaccines | Index Medicus | ANTIBODIES | AIDS VIRUS | BASIC BIOLOGICAL SCIENCES | AFFINITY | BIOLOGY | GLYCOPROTEINS | VULNERABILITY | ANTIGENS | IMMUNOLOGY | 60 APPLIED LIFE SCIENCES
Journal Article