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

Abstract

Infectivity of rotavirus is dramatically enhanced by proteolytic cleavage of its outer layer VP4 spike protein into two function domains, VP8* and VP5*. The carbohydrate-recognising domain VP8* is proposed to bind sialic acid-containing host cell-surface glycans, followed by a series of subsequent virus-cell interactions. Live attenuated human and bovine rotavirus vaccine candidates to prevent gastroenteritis have been derived from bovine rotavirus strain NCDV. The NCDV VP8*64-224 was over-expressed, purified to homogeneity and crystallized in the presence of a 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 determined by molecular replacement.