4YG0: Structural Basis Of Glycan Recognition In Neonate-specific Rotaviruses

Citation:
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.
PDB ID: 4YG0Download
MMDB ID: 133086
PDB Deposition Date: 2015/2/25
Updated in MMDB: 2015/11
Experimental Method:
x-ray diffraction
Resolution: 1.29  Å
Source Organism:
Similar Structures:
Biological Unit for 4YG0: monomeric; determined by author and by software (PISA)
Molecular Components in 4YG0
Label Count Molecule
Protein (1 molecule)
1
Outer Capsid Protein VP4
Molecule annotation
Chemicals (4 molecules)
1
2
2
1
3
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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