Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the VP8* carbohydrate-binding protein of the human rotavirus strain Wa
| Autor: | Helen Blanchard, Mark J. Kraschnefski, Stacy A. Scott, Gavan Holloway, Barbara S. Coulson, Mark von Itzstein |
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| Rok vydání: | 2005 |
| Předmět: |
Rotavirus
viruses Biophysics Carbohydrates RNA-binding protein Plasma protein binding Biology Viral Nonstructural Proteins medicine.disease_cause Biochemistry Virus X-Ray Diffraction Structural Biology Genetics medicine Escherichia coli Molecular replacement Cloning Molecular DNA Primers Cloning Strain (chemistry) Cell Membrane RNA-Binding Proteins Condensed Matter Physics Molecular biology N-Acetylneuraminic Acid Crystallization Communications RNA Viral Electrophoresis Polyacrylamide Gel Crystallization Protein Binding |
| Zdroj: | Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 11) |
| ISSN: | 1744-3091 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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