Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the VP8*carbohydrate-binding protein of the human rotavirus strain Wa
AuthorKraschnefski, MJ; Scott, SA; Holloway, G; Coulson, BS; von Itzstein, M; Blanchard, H
Source TitleACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
PublisherINT UNION CRYSTALLOGRAPHY
AffiliationMicrobiology And Immunology
Document TypeJournal Article
CitationsKraschnefski, M. J., Scott, S. A., Holloway, G., Coulson, B. S., von Itzstein, M. & Blanchard, H. (2005). Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the VP8*carbohydrate-binding protein of the human rotavirus strain Wa. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 61 (Pt 11), pp.989-993. https://doi.org/10.1107/S1744309105032999.
Access StatusAccess this item via the Open Access location
Open Access at PMChttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1978132
C1 - Journal Articles Refereed
Rotaviruses exhibit host-specificity and the first crystallographic information on a rotavirus strain that infects humans is reported here. Recognition and attachment to host cells, leading to invasion and infection, is critically linked to the function of the outer capsid spike protein of the rotavirus particle. In some strains the VP8* component of the spike protein is implicated in recognition and binding of sialic-acid-containing cell-surface carbohydrates, thereby enabling infection by the virus. The cloning, expression, purification, crystallization and initial X-ray diffraction analysis of the VP8* core from human Wa rotavirus is reported. Two crystal forms (trigonal P3(2)21 and monoclinic P2(1)) have been obtained and X-ray diffraction data have been collected, enabling determination of the VP8*(64-223) structure by molecular replacement.
KeywordsMedical Virology ; Infectious Diseases
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