Author
Listed:
- 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
Baylor College of Medicine)
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.
Suggested Citation
Liya Hu & Sasirekha Ramani & Rita Czako & Banumathi Sankaran & Ying Yu & David F. Smith & Richard D. Cummings & Mary K. Estes & B. V. Venkataram Prasad, 2015.
"Structural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus,"
Nature Communications, Nature, vol. 6(1), pages 1-10, December.
Handle:
RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9346
DOI: 10.1038/ncomms9346
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