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

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 A and the crystallographic structure of NCDV VP8*(64-224) was determined by molecular replacement.

SUBMITTER: Yu X 

PROVIDER: S-EPMC2496849 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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

Yu Xing X   Guillon Annabel A   Szyczew Alex J AJ   Kiefel Milton J MJ   Coulson Barbara S BS   von Itzstein Mark M   Blanchard Helen H  

Acta crystallographica. Section F, Structural biology and crystallization communications 20080523 Pt 6

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 NC  ...[more]

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