Crystallographic and cryo EM analysis of virion-receptor interactions.
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.
Rossmann
M G
MG
Department of Biological Sciences, Purdue University, West Lafayette, Indiana.
Olson
N H
NH
Kolatkar
P R
PR
Oliveira
M A
MA
Cheng
R H
RH
Greve
J M
JM
McClelland
A
A
Baker
T S
TS
D015815:Cell Adhesion Molecules / Q000648:ultrastructure*; D015925:Cryopreservation; D018360:Crystallography, X-Ray; D006801:Humans; D018799:Intercellular Adhesion Molecule-1; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008958:Models, Molecular; D008961:Models, Structural; D011991:Receptors, Virus / Q000648:ultrastructure*; D012229:Rhinovirus / Q000648:ultrastructure*; D013329:Structure-Activity Relationship; D014771:Virion / Q000648:ultrastructure*
D015815:Cell Adhesion Molecules; D046911:Macromolecular Substances; D011991:Receptors, Virus; D018799:Intercellular Adhesion Molecule-1