Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Stacy A ScottHelen Blanchard

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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Citations

Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Mark J KraschnefskiHelen Blanchard
Feb 6, 2007·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Yang-De ZhangYi-Feng Pan
Jun 10, 2008·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Xing YuHelen Blanchard
Jul 15, 2016·Archives of Virology·Arpaporn YodmeeklinNiwat Maneekarn
Jan 6, 2015·Nature Communications·Raphael BöhmThomas Haselhorst
Feb 3, 2021·Biotechnology and Bioengineering·Moo Sun HongRichard D Braatz

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