Estimating the probability of polyreactive antibodies 4E10 and 2F5 disabling a gp41 trimer after T cell-HIV adhesion

• Published in: PLoS computational biology Vol. 10; no. 1; p. e1003431
• Main Authors: Hu, Bin, Liao, Hua-Xin, Alam, S Munir, Goldstein, Byron
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 01.01.2014; Public Library of Science (PLoS)
• Subjects: Antibodies; Antibodies, Monoclonal - chemistry; Antibodies, Neutralizing - chemistry; Biology; Broadly Neutralizing Antibodies; Cell Adhesion; Cell research; Confidence intervals; Epitopes - chemistry; Experiments; Gene expression; Health aspects; HIV (Viruses); HIV Antibodies - chemistry; HIV Envelope Protein gp41 - chemistry; HIV Infections - immunology; HIV Infections - virology; Host-parasite relationships; Humans; Immunoglobulin Fragments - chemistry; Immunoglobulin G - chemistry; Inhibitory Concentration 50; Lymphocytes; Mathematical models; Medicine; Methods; Parameter estimation; Probability; Protein Conformation; Software; T cells; T-Lymphocytes - virology; Viral antibodies; Virus Internalization; United States; Antibodies, Neutralizing; HIV Infections; T-Lymphocytes; HIV Antibodies; Humans; Immunoglobulin G; HIV Envelope Protein gp41; Probability; Antibodies, Monoclonal; Epitopes; Cell Adhesion; Virus Internalization; Immunoglobulin Fragments; Inhibitory Concentration 50; Protein Conformation

A few broadly neutralizing antibodies, isolated from HIV-1 infected individuals, recognize epitopes in the membrane proximal external region (MPER) of gp41 that are transiently exposed during viral entry. The best characterized, 4E10 and 2F5, are polyreactive, binding to the viral membrane and their...