ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the VP8* carbohydrate-binding protein of the human rotavirus strain Wa.
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 6 papers.
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Who cites it
6 citing papers in PubMed.
- Bivalent rotavirus VP4∗ stimulates protective antibodies against common genotypes of human rotaviruses.iScience · 2022Article
- Crystallization of a nonreplicating rotavirus vaccine candidate.Biotechnology and bioengineering · 2021Article
- Relative roles of GM1 ganglioside, N-acylneuraminic acids, and α2β1 integrin in mediating rotavirus infection.Journal of virology · 2014Article
- Construction and characterization of human rotavirus recombinant VP8* subunit parenteral vaccine candidates.Vaccine · 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
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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