A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface

• Main Authors: Fibriansah G., Tan J.L., Smith S.A., de Alwis A.R., Ng T.-S., Kostyuchenko V.A., Ibarra K.D., Wang J., Harris E., de Silva A., Crowe J.E., Lok S.-M.
• Other Authors: DUKE-NUS MEDICAL SCHOOL
• Format: Article
• Published: 2020
• Subjects: CD209 antigen; epitope; genomic RNA; human monoclonal antibody; human monoclonal antibody 1F4; immunoglobulin F(ab) fragment; immunoglobulin G; immunoglobulin G1; membrane protein; neutralizing antibody; unclassified drug; virus envelope protein; virus receptor; amino acid sequence; animal experiment; animal model; animal tissue; article; bone marrow cell; cell strain U937; complementarity determining region; conformation; controlled study; cryoelectron microscopy; dengue; Dengue virus; Dengue virus 1; Dengue virus 2; Dengue virus 3; Dengue virus 4; enzyme linked immunosorbent assay; gene dosage; glycosylation; heavy chain; hinge region; human; hydrogen bond; in vitro study; in vivo study; lethal dose; light chain; limit of detection; mature virus; mouse; nonhuman; priority journal; protein assembly; protein conformation; protein quaternary structure; protein secondary structure; receptor binding; sequence alignment; serodiagnosis; serotype; sublethal dose; Vero cell; virus attachment; virus entry; virus load; virus morphology; virus neutralization; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antibodies, Neutralizing; Antibodies, Viral; Cell Line; Dengue; Dengue Virus; Epitopes; Humans; Immunoglobulin Fab Fragments; Mice; Molecular Dynamics Simulation; Molecular Sequence Data; Protein Structure, Tertiary; Viral Envelope Proteins; Virus Internalization
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/174171
• Institution: National University of Singapore

10.1002/emmm.201303404