Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8
Acta Crystallographica Section F
Volume 61, Issue 6, pages 617–620, June 2005
How to Cite
Scott, S. A., Holloway, G., Coulson, B. S., Szyczew, A. J., Kiefel, M. J., Von Itzstein, M. and Blanchard, H. (2005), Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8. Acta Cryst. F, 61: 617–620. doi: 10.1107/S1744309105013849
- sialic acid-binding domain;
- procine rotavirus.
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 Å resolution, enabling the determination of the VP8* structure by molecular replacement.