| Literature DB >> 18540062 |
Xing Yu1, Annabel Guillon, Alex J Szyczew, Milton J Kiefel, Barbara S Coulson, Mark von Itzstein, Helen Blanchard.
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.Entities:
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Year: 2008 PMID: 18540062 PMCID: PMC2496849 DOI: 10.1107/S1744309108011949
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091