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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the VP8* carbohydrate-binding protein of the human rotavirus strain Wa

Journal Article


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 P3221 and monoclinic P21) have been obtained and X-ray diffraction data have been collected, enabling determination of the VP8*64-223 structure by molecular replacement. © 2005 International Union of Crystallography All rights reserved.

Publication Date


  • 2005

Citation


  • Kraschnefski, 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 and Crystallization Communications, 61(11), 989-993. doi:10.1107/S1744309105032999

Scopus Eid


  • 2-s2.0-33744462880

Start Page


  • 989

End Page


  • 993

Volume


  • 61

Issue


  • 11

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 P3221 and monoclinic P21) have been obtained and X-ray diffraction data have been collected, enabling determination of the VP8*64-223 structure by molecular replacement. © 2005 International Union of Crystallography All rights reserved.

Publication Date


  • 2005

Citation


  • Kraschnefski, 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 and Crystallization Communications, 61(11), 989-993. doi:10.1107/S1744309105032999

Scopus Eid


  • 2-s2.0-33744462880

Start Page


  • 989

End Page


  • 993

Volume


  • 61

Issue


  • 11