title: Virus-ligand interactions: identification and characterization of ligand binding by NMR spectroscopy.
abstract: We demonstrate the detection and characterization of ligand binding to viruses via NMR. To illustrate the methodology, the interaction of an antiviral compound with human rhinovirus serotype 2 (HRV2) was investigated. Specific interaction of a capsid-binding inhibitor and native HRV2 was monitored utilizing saturation transfer difference (STD) NMR. STD NMR experiments at atomic resolution allowed those regions of the ligand that are involved in the interaction with the virus to be determined. The approach allows for (i) the fast and robust assessment of binding, (ii) the determination of the ligand binding epitope at atomic resolution without the necessity to crystallize virus-ligand complexes, and (iii) the reuse of the virus in subsequent assays. This methodology enables one to easily identify binding of drugs, peptides, and receptor or antibody fragments to the viral capsid.
authors.affiliation: Institute for Chemistry, University of Luebeck, Ratzeburger Allee 160, 23568 Luebeck, Germany.
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Benie
authors.forename: Rosita
authors.initials: R
authors.lastname: Moser
authors.forename: Englbert
authors.initials: E
authors.lastname: Bäuml
authors.forename: Dieter
authors.initials: D
authors.lastname: Blaas
authors.forename: Thomas
authors.initials: T
authors.lastname: Peters
mesh_terms: D000998:Antiviral Agents / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D001665:Binding Sites; D006801:Humans; D007555:Isoxazoles / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D007700:Kinetics; D008024:Ligands; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D012229:Rhinovirus / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000998:Antiviral Agents; D007555:Isoxazoles; D008024:Ligands; C049869:Win 52084