Skip to main content
placeholder image

Crystallization and preliminary X-ray diffraction analysis of the carbohydrate-recognizing domain (VP8*) of bovine rotavirus strain NCDV

Journal Article


Abstract


  • The infectivity of rotavirus is dramatically enhanced by proteolytic cleavage of its outer layer VP4 spike protein into two functional domains, VP8* and VP5*. The carbohydrate-recognizing domain VP8* is proposed to bind sialic acid-containing host cell-surface glycans and this is followed by a series of subsequent virus-cell interactions. Live attenuated human and bovine rotavirus vaccine candidates for the prevention of gastroenteritis have been derived from bovine rotavirus strain NCDV. The NCDV VP8*64-224 was overexpressed, purified to homogeneity and crystallized in the presence of an N-acetylneuraminic acid derivative. X-ray diffraction data were collected to a resolution of 2.0 Å and the crystallographic structure of NCDV VP8*64-224 was determined by molecular replacement. © 2008 International Union of Crystallography All rights reserved.

Publication Date


  • 2008

Citation


  • Yu, X., Guillon, A., Szyczew, A. J., Kiefel, M. J., Coulson, B. S., Von Itzstein, M., & Blanchard, H. (2008). Crystallization and preliminary X-ray diffraction analysis of the carbohydrate-recognizing domain (VP8*) of bovine rotavirus strain NCDV. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(6), 509-511. doi:10.1107/S1744309108011949

Scopus Eid


  • 2-s2.0-46249089851

Start Page


  • 509

End Page


  • 511

Volume


  • 64

Issue


  • 6

Abstract


  • The infectivity of rotavirus is dramatically enhanced by proteolytic cleavage of its outer layer VP4 spike protein into two functional domains, VP8* and VP5*. The carbohydrate-recognizing domain VP8* is proposed to bind sialic acid-containing host cell-surface glycans and this is followed by a series of subsequent virus-cell interactions. Live attenuated human and bovine rotavirus vaccine candidates for the prevention of gastroenteritis have been derived from bovine rotavirus strain NCDV. The NCDV VP8*64-224 was overexpressed, purified to homogeneity and crystallized in the presence of an N-acetylneuraminic acid derivative. X-ray diffraction data were collected to a resolution of 2.0 Å and the crystallographic structure of NCDV VP8*64-224 was determined by molecular replacement. © 2008 International Union of Crystallography All rights reserved.

Publication Date


  • 2008

Citation


  • Yu, X., Guillon, A., Szyczew, A. J., Kiefel, M. J., Coulson, B. S., Von Itzstein, M., & Blanchard, H. (2008). Crystallization and preliminary X-ray diffraction analysis of the carbohydrate-recognizing domain (VP8*) of bovine rotavirus strain NCDV. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(6), 509-511. doi:10.1107/S1744309108011949

Scopus Eid


  • 2-s2.0-46249089851

Start Page


  • 509

End Page


  • 511

Volume


  • 64

Issue


  • 6