ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005
Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- Crystallization of a nonreplicating rotavirus vaccine candidate.Biotechnology and bioengineering · 2021Article
- A small molecule inhibits virion attachment to heparan sulfate- or sialic acid-containing glycans.Journal of virology · 2014Article
- Relative roles of GM1 ganglioside, N-acylneuraminic acids, and α2β1 integrin in mediating rotavirus infection.Journal of virology · 2014Article
- Structural basis of rotavirus strain preference toward N-acetyl- or N-glycolylneuraminic acid-containing receptors.Journal of virology · 2012Article
- Crystallization and preliminary X-ray diffraction analysis of the carbohydrate-recognizing domain (VP8*) of bovine rotavirus strain NCDV.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- Expression, purification, crystallization and preliminary X-ray diffraction analysis of the VP8* sialic acid-binding domain of porcine rotavirus strain OSU.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
- 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 and crystallization communications · 2005Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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