Title Crystallographic and cryo EM analysis of virion-receptor interactions.
Author Rossmann, M G; Olson, N H; Kolatkar, P R; Oliveira, M A; Cheng, R H; Greve, J M; McClelland, A; Baker, T S
Journal Arch Virol Suppl Publication Year/Month 1994
PMID 7913361 PMCID PMC4140090
Affiliation 1.Department of Biological Sciences, Purdue University, West Lafayette, Indiana.

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.

  • Copyright © 2023
    National Institute of Pathogen Biology, CAMS & PUMC, Bejing, China
    All rights reserved.