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

Liya Hu, Sasirekha Ramani, Rita Czako, Banumathi Sankaran, Ying Yu, David F. Smith, Richard D. Cummings, Mary K. Estes and B. V. Venkataram Prasad ()
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Liya Hu: Baylor College of Medicine, One Baylor Plaza
Sasirekha Ramani: Baylor College of Medicine
Rita Czako: Baylor College of Medicine
Banumathi Sankaran: Berkeley Center for Structural Biology, Lawrence Berkeley National Laboratory
Ying Yu: Emory University School of Medicine
David F. Smith: Emory University School of Medicine
Richard D. Cummings: Emory University School of Medicine
Mary K. Estes: Baylor College of Medicine
B. V. Venkataram Prasad: Baylor College of Medicine, One Baylor Plaza

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: Abstract 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 type I or type II precursor glycans, and to restrict type II glycan binding in the bovine counterpart. Such a distinct glycan-binding site that allows differential recognition of the precursor glycans, which are developmentally regulated in the neonate gut and abundant in bovine and human milk provides a basis for age-restricted tropism and zoonotic transmission of G10P[11] rotaviruses.

Date: 2015
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DOI: 10.1038/ncomms9346

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