학술논문

Crystallographic and cryo EM analysis of virion-receptor interactions
Document Type
article
Source
Subject
Biochemistry and Cell Biology
Biological Sciences
Infection
Cell Adhesion Molecules
Cryopreservation
Crystallography
X-Ray
Humans
Intercellular Adhesion Molecule-1
Macromolecular Substances
Microscopy
Electron
Models
Molecular
Models
Structural
Receptors
Virus
Rhinovirus
Structure-Activity Relationship
Virion
Virology
Language
Abstract
Cryoelectron microscopy has been used to determine the first structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 (HRV16) complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule-1 (ICAM-1) shows that ICAM-1 binds into the 12 A deep "canyon" on the surface of the virus. This is consistent with the prediction that the viral receptor attachment site lies in a cavity inaccessible to the host's antibodies. The atomic structures of HRV14 and CD4, homologous to HRV16 and ICAM-1, showed excellent correspondence with observed density, thus establishing the virus-receptor interactions.