Crystallisation and preliminary X-ray diffraction analysis of the carbohydrate-recognizing domain (VP8*) of bovine rotavirus strain NCDV
Author(s)
Yu, Xing
Guillon, Annabel
Szyczew, Alex J
Kiefel, Milton J
Coulson, Barbara S
von Itzstein, Mark
Blanchard, Helen
Year published
2008
Metadata
Show full item recordAbstract
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 ...
View more >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 Šand the crystallographic structure of NCDV VP8*64-224 determined by molecular replacement.
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View more >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 Šand the crystallographic structure of NCDV VP8*64-224 determined by molecular replacement.
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Journal Title
Acta Crystallographica Section F - Structural Biology and Crystallization Communications
Volume
F64
Subject
Chemical sciences
Biological sciences