The cellular receptor to human rhinovirus 2 binds around the 5-fold axis and not in the canyon: a structural view.
Human rhinovirus serotype 2 (HRV2) belongs to the minor group of HRVs that bind to members of the LDL-receptor family including the very low density lipoprotein (VLDL)-receptor (VLDL-R). We have determined the structures of the complex between HRV2 and soluble fragments of the VLDL-R to 15 A resolution by cryo-electron microscopy. The receptor fragments, which include the first three ligand-binding repeats of the VLDL-R (V1-3), bind to the small star-shaped dome on the icosahedral 5-fold axis. This is in sharp contrast to the major group of HRVs where the receptor site for ICAM-1 is located at the base of a depression around each 5-fold axis. Homology models of the three domains of V1-3 were used to explore the virus-receptor interaction. The footprint of VLDL-R on the viral surface covers the BC- and HI-loops on VP1.
Hewat
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EA
Institut de Biologie Structurale Jean-Pierre Ebel, 41 rue Jules Horowitz, 38027 Grenoble, France.
Neumann
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E
Conway
J F
JF
Moser
R
R
Ronacher
B
B
Marlovits
T C
TC
Blaas
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D
D000595:Amino Acid Sequence; D001665:Binding Sites; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D006367:HeLa Cells; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000737:chemistry; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011973:Receptors, LDL / Q000737:chemistry; D011991:Receptors, Virus / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D012229:Rhinovirus / Q000737:chemistry* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D008024:Ligands; D011973:Receptors, LDL; D011991:Receptors, Virus; D011994:Recombinant Proteins; C036053:VLDL receptor; D018799:Intercellular Adhesion Molecule-1