Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8.
Rotavirus recognition and attachment to host cells involves interaction with the spike protein VP4 that projects outwards from the surface of the virus particle. An integral component of these spikes is the VP8* domain, which is implicated in the direct recognition and binding of sialic acid-containing cell-surface carbohydrates and facilitates subsequent invasion by the virus. The expression, purification, crystallization and preliminary X-ray diffraction analysis of VP8* from porcine CRW-8 rotavirus is reported. Diffraction data have been collected to 2.3 A resolution, enabling the determination of the VP8* structure by molecular replacement.
Scott
Stacy A
SA
Institute for Glycomics, Griffith University, PMB 50, Gold Coast Mail Centre, Queensland 9726, Australia.
Holloway
Gavan
G
Coulson
Barbara S
BS
Szyczew
Alex J
AJ
Kiefel
Milton J
MJ
von Itzstein
Mark
M
Blanchard
Helen
H
D000818:Animals; D001665:Binding Sites; D003460:Crystallization / Q000379:methods; D019158:N-Acetylneuraminic Acid; D016133:Polymerase Chain Reaction; D016601:RNA-Binding Proteins / Q000737:chemistry*; D012401:Rotavirus / Q000737:chemistry*; D013552:Swine; D017361:Viral Nonstructural Proteins / Q000737:chemistry*; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction
D016601:RNA-Binding Proteins; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins; C079234:NS35 protein, rotavirus; D019158:N-Acetylneuraminic Acid