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Nature (London), ISSN 1476-4687, 2014, Volume 515, Issue 7525, pp. 138 - 142
....664. Mutagenesis and a reconstruction by negative-stain electron microscopy of the Fab in complex with trimer revealed that it bound to a conserved epitope, which stretched across gp120 and gp41... 
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
The Journal of immunology (1950), ISSN 1550-6606, 2016, Volume 196, Issue 4, pp. 1435 - 1441
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2010, Volume 107, Issue 44, pp. 18950 - 18955
...) infection at a postattachment stage in the viral life-cycle. Here, we determined the structure of WNV complexed with Fab fragments of CR4354 using cryoelectron microscopy... 
Molecules | West Nile virus | Virions | Rafts | Antibodies | Viruses | Glycoproteins | Epitopes | Monomers | Binding sites | Antibody | Flavivirus | Cryoelectron microscopy | DOMAIN-III | antibody | PARTICLE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ENVELOPE GLYCOPROTEIN | SOFTWARE | ORGANIZATION | cryoelectron microscopy | DENGUE-VIRUS | INFECTION | BINDING | flavivirus | Endosomes - immunology | Antibodies, Viral - pharmacology | Humans | Molecular Sequence Data | Viral Structural Proteins - immunology | Virus Internalization - drug effects | Epitopes - immunology | Antibodies, Neutralizing - immunology | Binding Sites | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Endosomes - virology | Amino Acid Sequence | West Nile virus - ultrastructure | West Nile Fever - immunology | West Nile virus - immunology | Antibodies, Monoclonal - pharmacology | Antibodies, Neutralizing - pharmacology | Viral Structural Proteins - chemistry | Immunoglobulin Fab Fragments - pharmacology | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | West Nile virus - chemistry | Antibodies, Viral - chemistry | Antibodies, Viral - immunology | Epitopes - chemistry | Immunoglobulin Fab Fragments - immunology | Proteins | Monoclonal antibodies | Physiological aspects | Crosslinking | Research | Chemical properties | Infection | Pathogens | Microscopy | protein E | Fab | Shells | double prime E protein | Immune response (humoral) | MONOMERS | DISTURBANCES | LIFE CYCLE | BASIC BIOLOGICAL SCIENCES | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | CROSS-LINKING | GLYCOPROTEINS | MICROSCOPY | PROTEINS | PATHOGENS | Biological Sciences
Journal Article
Infection and Immunity, ISSN 0019-9567, 03/2009, Volume 77, Issue 3, pp. 1083 - 1090
Journal Article
Mucosal immunology, ISSN 1933-0219, 2009, Volume 2, Issue 5, pp. 412 - 426
.... We have constructed a mucosal Fab IgA library from HEPS and have characterized a series of HIV-1 IgAs specific for gp41 that, in vitro, are transcytosis-blocking and infection-neutralizing... 
VACCINE CANDIDATE | CRYSTAL-STRUCTURE | SECRETORY IGA | GALACTOSYL CERAMIDE | SEX WORKERS | IMMUNOLOGY | HUMAN-IMMUNODEFICIENCY-VIRUS | TYPE-1 ANTIBODY 2F5 | STEP PURIFICATION | MEMBRANE-PROXIMAL REGION | F-AB FRAGMENT | HIV Infections - prevention & control | HIV Envelope Protein gp41 - immunology | Humans | Vagina - immunology | Molecular Sequence Data | Immunoglobulin A, Secretory - isolation & purification | Peptide Library | HIV Antibodies - isolation & purification | Virus Internalization | CD4-Positive T-Lymphocytes - immunology | Sequence Homology | HIV Infections - immunology | Immunoglobulin A, Secretory - genetics | HIV-1 - physiology | HIV Antibodies - immunology | Peptide Fragments - immunology | Conserved Sequence | Adult | Female | Gene Rearrangement, B-Lymphocyte | CD4-Positive T-Lymphocytes - virology | Antibodies, Monoclonal - immunology | Amino Acid Sequence | Immunoglobulin Fab Fragments - genetics | Immunoglobulin A, Secretory - immunology | Antibodies, Monoclonal - isolation & purification | Environmental Exposure | HIV Seronegativity - immunology | Antibodies, Monoclonal - genetics | Immunity, Innate - immunology | HIV-1 - immunology | Sequence Alignment | Mucous Membrane - immunology | Cervix Uteri - immunology | HIV Antibodies - genetics | Immunoglobulin Fab Fragments - immunology | Sexual Partners | Index Medicus | HIV Infections | HIV-1 | Peptide Fragments | HIV Antibodies | Mucous Membrane | Life Sciences | CD4-Positive T-Lymphocytes | Immunoglobulin Fab Fragments | Immunoglobulin A, Secretory | HIV Seronegativity | HIV Envelope Protein gp41 | Vagina | Antibodies, Monoclonal | Immunity, Innate | Cervix Uteri | Microbiology and Parasitology
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2011, Volume 334, Issue 6059, pp. 1097 - 1103
.... Crystal structures of antigen-binding fragments (Fabs) PGT 127 and 128 with Man 9 at 1.65 and 1.29 angstrom resolution, respectively, and glycan binding data delineate a specific high mannose-binding site... 
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
Journal of autoimmunity, ISSN 0896-8411, 2017, Volume 77, pp. 104 - 115
Journal Article
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2009, Volume 324, Issue 5933, pp. 1444 - 1447
.... We report the crystal structure at 3.4 angstrom resolution of VP7 bound with the Fab fragment of a neutralizing monoclonal antibody... 
Infectious diseases | Rotavirus | Neutralizing antibodies | Virions | Vaccination | Disulfides | Antibodies | Reports | Trimers | Epitopes | Virology | 3-DIMENSIONAL STRUCTURE | ANTIBODIES | HEMAGGLUTININ | MULTIDISCIPLINARY SCIENCES | SEQUENCE | CALCIUM | VACCINE | RHESUS ROTAVIRUS | BINDING | EPITOPES | Protein Subunits | Antibodies, Viral - metabolism | Antigens, Viral - metabolism | Calcium - metabolism | Protein Multimerization | Rotavirus - immunology | Molecular Sequence Data | Antigens, Viral - genetics | Crystallography, X-Ray | Neutralization Tests | Rotavirus - chemistry | Epitopes - immunology | Immunoglobulin Fab Fragments - metabolism | Capsid Proteins - chemistry | Capsid Proteins - immunology | Binding Sites | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Serotyping | Protein Structure, Tertiary | Amino Acid Sequence | Capsid Proteins - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Antigens, Viral - chemistry | Protein Folding | Antigens, Viral - immunology | Immunoglobulin Fab Fragments - chemistry | Antibodies, Viral - chemistry | Antibodies, Viral - immunology | Antibodies, Monoclonal - metabolism | Immunoglobulin Fab Fragments - immunology | Mutation | Binding Sites, Antibody | Capsid Proteins - genetics | Proteins | Viral proteins | Rotaviruses | Physiological aspects | Research | Chemical properties | Structure | Protein binding | Viruses | Immunology | Crystal structure
Journal Article