NMR experiments reveal the molecular basis of receptor recognition by a calicivirus.
The analysis of virus-receptor interactions at atomic resolution is of fundamental importance to understand infection processes, and to establish novel anti-viral therapies. As an example, rabbit hemorrhagic disease virus (RHDV), a member of the Caliciviridae family and considered as an "emerging" virus, attaches to histo-blood group antigens (HBGA) on the surface of adult rabbit epithelial cells of the upper respiratory and digestive tracts. It appears that this attachment is a key step in the process of infection with RHDV. Here, we report NMR experiments that reveal the atomic details of the recognition of HBGAs and fragments thereof by RHDV virus-like particles (VLP). The experiments yield binding epitopes of several HBGAs and show that L-fucose is a minimal structural requirement for specific molecular recognition by the VLPs. As the methodology is general, these studies may pave the way for the development of novel anti-viral entry inhibitors.
Rademacher
Christoph
C
University of Luebeck, Institute of Chemistry, Ratzeburger Allee 160, 23538 Luebeck, Germany.
Krishna
N Rama
NR
Palcic
Monica
M
Parra
Francisco
F
Peters
Thomas
T
D000818:Animals; D001667:Binding, Competitive; D001789:Blood Group Antigens / Q000737:chemistry*; D002236:Carbohydrate Conformation; D004847:Epithelial Cells / Q000378:metabolism; D005643:Fucose / Q000737:chemistry; D017929:Hemorrhagic Disease Virus, Rabbit / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods* / Q000592:standards; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D011817:Rabbits; D011991:Receptors, Virus / Q000737:chemistry*
D001789:Blood Group Antigens; D010446:Peptide Fragments; D011991:Receptors, Virus; D005643:Fucose