title: Recent structural solutions for antibody neutralization of viruses.
abstract: Structural studies of virus-antibody interactions can offer insights into mechanisms of virus neutralization and immune escape. Crystallography and cryoelectron microscopy can reveal the structural relationship between receptor-binding sites and neutralization epitopes, as well as whether molecular rearrangements occur upon antibody binding.
authors.affiliation: Dept of Molecular and Medical Pharmacology, UCLA School of Medicine 90095-1770, USA. pstewart@mail.nuc.ucla.edu
authors.forename: P L
authors.initials: PL
authors.lastname: Stewart
authors.forename: G R
authors.initials: GR
authors.lastname: Nemerow
mesh_terms: D000818:Animals; D000936:Antigen-Antibody Complex / Q000648:ultrastructure*; D005537:Aphthovirus / Q000276:immunology*; D000939:Epitopes / Q000648:ultrastructure; D006389:Hemagglutinins, Viral / Q000276:immunology; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000276:immunology; D018799:Intercellular Adhesion Molecule-1 / Q000276:immunology; D008854:Microscopy, Electron; D009975:Orthomyxoviridae / Q000276:immunology*; D012229:Rhinovirus / Q000276:immunology*
chemical_list: D000936:Antigen-Antibody Complex; D000939:Epitopes; D006389:Hemagglutinins, Viral; D007140:Immunoglobulin Fab Fragments; D018799:Intercellular Adhesion Molecule-1