4YG3

Structural basis of glycan recognition in neonate-specific rotaviruses

Summary for 4YG3

• Entry DOI: 10.2210/pdb4yg3/pdb
• Related: 4YE2 4YEZ 4YFW 4YG0 4YG6
• Descriptor: Outer capsid protein VP4, SULFATE ION (3 entities in total)
• Functional Keywords: rotavirus, structural biology, glycan, viral protein
• Biological source: Rotavirus A (RV-A)
• Total number of polymer chains: 1
• Total formula weight: 18351.76

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

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: 26420502
DOI: 10.1038/ncomms9346

Experimental method

X-RAY DIFFRACTION (2.285 Å)