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.
Cite
CITATION STYLE
Rossmann, M. G., Olson, N. H., Kolatkar, P. R., Oliveira, M. A., Cheng, R. H., Greve, J. M., … Baker, T. S. (1994). Crystallographic and cryo EM analysis of virion-receptor interactions. Archives of Virology. Supplementum, 9, 531–541. https://doi.org/10.1007/978-3-7091-9326-6_51
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.