Cryoelectron microscopy revealed that the intercellular adhesion molecule 1 (ICAM-1) binds into the 12-Angstrom deep canyon on the surface of human rhinovirus 16, confirming the canyon hypothesis.
Cryoelectron microscopy reveals that the human rhinovirus receptor binds in a deep canyon on the viral surface, protecting the attachment site from host antibodies.
Cryoelectron microscopy has been used to determine the structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule 1 shows that the intercellular adhesion molecule 1 binds into the 12-A deep "canyon" on the viral surface. This result confirms the prediction that the viral-receptor attachment site lies in a cavity inaccessible to the host's antibodies. The atomic structures of human rhinovirus 14 and CD4, homologous to human rhinovirus 16 and intercellular adhesion molecule 1, showed excellent correspondence with observed density, thus establishing the virus-receptor interactions.
Olson et al. (1993) studied Human rhinovirus (structural biology). Cryoelectron microscopy of HRV-16 complexed with ICAM-1 D1D2 was evaluated on Three-dimensional structure of the virus-receptor complex. Cryoelectron microscopy revealed that the intercellular adhesion molecule 1 (ICAM-1) binds into the 12-Angstrom deep canyon on the surface of human rhinovirus 16, confirming the canyon hypothesis.