The successful crystallization and preliminary X-ray diffraction analysis of the porcine rotavirus CRW-8 VP8 domain enables its 3D structure determination to understand host-specificity and guide rotavirus-specific therapeutics.
Advances structural analysis of rotavirus VP8; leaves open host-specificity mechanisms and therapeutic development.
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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Scott et al. (2005) studied this question.
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