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

• Published in: EMBO molecular medicine Vol. 6; no. 3; pp. 358 - 371
• Main Authors: Fibriansah, Guntur, Tan, Joanne L, Smith, Scott A, de Alwis, Adamberage R, Ng, Thiam‐Seng, Kostyuchenko, Victor A, Ibarra, Kristie D, Wang, Jiaqi, Harris, Eva, de Silva, Aravinda, Crowe, James E, Lok, Shee‐Mei
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.03.2014; EMBO Press; Blackwell Publishing Ltd; Springer Nature
• Subjects: Amino Acid Sequence; Animals; Antibodies, Monoclonal - immunology; Antibodies, Monoclonal - pharmacology; Antibodies, Monoclonal - therapeutic use; Antibodies, Neutralizing - immunology; Antibodies, Viral - immunology; Bone marrow; Cell Line; cryoEM; Dengue - drug therapy; Dengue - veterinary; Dengue fever; dengue virus; Dengue Virus - metabolism; EMBO19; EMBO23; Encephalitis; Epitopes; Epitopes - chemistry; Epitopes - immunology; Fab; human antibody; Humans; Immunoglobulin Fab Fragments - chemistry; Immunoglobulin Fab Fragments - immunology; Immunoglobulins; Infections; Mice; Microscopy; Molecular Dynamics Simulation; Molecular Sequence Data; Monoclonal antibodies; Monomers; neutralization; Protein structure; Protein Structure, Tertiary; Proteins; Quaternary structure; Research Article; Serotypes; Standard deviation; structure; Tropical diseases; Variance analysis; Viral envelope proteins; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - immunology; Virus Internalization - drug effects; West Nile virus; cryoEM; human antibody; neutralization; structure; dengue virus

Dengue virus (DENV), which consists of four serotypes (DENV1‐4), infects over 400 million people annually. Previous studies have indicated most human monoclonal antibodies (HMAbs) from dengue patients are cross‐reactive and poorly neutralizing. Rare neutralizing HMAbs are usually serotype‐specific a...