Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8
AuthorScott, SA; Holloway, G; Coulson, BS; Szyczew, AJ; Kiefel, MJ; von Itzstein, M; Blanchard, H
Source TitleActa Crystallographica Section F: Structural Biology Communications
PublisherINT UNION CRYSTALLOGRAPHY
AffiliationMicrobiology And Immunology
Document TypeJournal Article
CitationsScott, 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 StatusAccess this item via the Open Access location
Open Access at PMChttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1952324
C1 - Journal Articles Refereed
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.
KeywordsMedical Virology ; Infectious Diseases
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