Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8
Author
Scott, SA; Holloway, G; Coulson, BS; Szyczew, AJ; Kiefel, MJ; von Itzstein, M; Blanchard, HDate
2005-06-01Source Title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONSPublisher
INT UNION CRYSTALLOGRAPHYAffiliation
Microbiology And ImmunologyMetadata
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Journal ArticleCitations
Scott, S. A., Holloway, G., Coulson, B. S., Szyczew, A. J., Kiefel, M. J., von Itzstein, M. & Blanchard, H. (2005). Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 61 (Pt 6), pp.617-620. https://doi.org/10.1107/S1744309105013849.Access Status
Access this item via the Open Access locationOpen Access at PMC
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1952324Description
C1 - Journal Articles Refereed
Abstract
Rotavirus recognition and attachment to host cells involves interaction with the spike protein VP4 that projects outwards from the surface of the virus particle. An integral component of these spikes is the VP8* domain, which is implicated in the direct recognition and binding of sialic acid-containing cell-surface carbohydrates and facilitates subsequent invasion by the virus. The expression, purification, crystallization and preliminary X-ray diffraction analysis of VP8* from porcine CRW-8 rotavirus is reported. Diffraction data have been collected to 2.3 A resolution, enabling the determination of the VP8* structure by molecular replacement.
Keywords
Medical Virology ; Infectious DiseasesExport Reference in RIS Format
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