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Structural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus.

Nat Commun. 2015; 
Hu L, Ramani S, Czako R, Sankaran B, Yu Y, Smith DF, Cummings RD, Estes MK, Venkataram Prasad BV,.
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Biochemicals Plates were washed three times with assay buffer and bound GST-VP8* was detected by horseradish peroxidase-conjugated anti-GST (0.1 μg ml−1, GenScript, Cat. No. A00130-40). Get A Quote

摘要

Strain-dependent variation of glycan recognition during initial cell attachment of viruses is a critical determinant of host specificity, tissue-tropism and zoonosis. Rotaviruses (RVs), which cause life-threatening gastroenteritis in infants and children, display significant genotype-dependent variations in glycan recognition resulting from sequence alterations in the VP8* domain of the spike protein VP4. The structural basis of this genotype-dependent glycan specificity, particularly in human RVs, remains poorly understood. Here, from crystallographic studies, we show how genotypic variations configure a novel binding site in the VP8* of a neonate-specific bovine-human reassortant to uniquely recognize either ... More

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