4yfz | pdb_00004yfz

Structural basis of glycan recognition in neonate-specific rotaviruses

spinqualitylabelsall models 4yfz, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yfz is a 1 chain structure with sequence from Human group a rotavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, GAL, NAG Related: 4yfw, 4ye2, 4yg0, 4yg3, 4yg6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [B6RGK2_9REOV] Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment (By similarity).[SAAS:SAAS00209906] VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact (By similarity).[SAAS:SAAS00209911] Publication Abstract from PubMed 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. Structural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus.,Hu L, Ramani S, Czako R, Sankaran B, Yu Y, Smith DF, Cummings RD, Estes MK, Venkataram Prasad BV Nat Commun. 2015 Sep 30;6:8346. doi: 10.1038/ncomms9346. PMID:26420502 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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