4YG0
Structural basis of glycan recognition in neonate-specific rotaviruses
Summary for 4YG0
Entry DOI | 10.2210/pdb4yg0/pdb |
Related | 4YE2 4YFW 4YFZ 4YG3 4YG6 |
Descriptor | Outer capsid protein VP4, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | rotavirus, structural biology, glycan, viral protein |
Biological source | Human rotavirus A |
Total number of polymer chains | 1 |
Total formula weight | 19391.10 |
Authors | Hu, L.,Prasad, B.V.V. (deposition date: 2015-02-25, release date: 2015-09-30, Last modification date: 2023-09-27) |
Primary citation | Hu, L.,Ramani, S.,Czako, R.,Sankaran, B.,Yu, Y.,Smith, D.F.,Cummings, R.D.,Estes, M.K.,Venkataram Prasad, B.V. Structural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus. Nat Commun, 6:8346-8346, 2015 Cited by PubMed 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. PubMed: 26420502DOI: 10.1038/ncomms9346 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.285 Å) |
Structure validation
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