3sld | pdb_00003sld

Structural characterization of a GII.4 2004 norovirus variant (TCH05) bound to A trisaccharide

spinqualitylabelsall models 3sld, resolution 2.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sld is a 10 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: A2G, FUC, GAL Related: 3sej, 3sjp, 3skb, 3sln Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Susceptibility to norovirus (NoV), a major pathogen of epidemic gastroenteritis, is associated with histo-blood group antigens (HBGAs), which are also cell attachment factors for this virus. GII.4 NoV strains are predominantly associated with worldwide NoV epidemics with a periodic emergence of new variants. The sequence variations in the surface exposed P domain of the capsid protein resulting in differential HBGA binding patterns and antigenicity are suggested to drive GII.4 epochal evolution. To understand how temporal sequence variations affect the P domain structure and contribute to epochal evolution, we determined the P domain structure of a 2004 variant with ABH and secretor Lewis HBGAs and compared it with the previously determined structure of a 1996 variant. We show that temporal sequence variations do not affect the binding of monofucosyl ABH HBGAs but they can modulate the binding strength of difucosyl Lewis HBGAs and thus could contribute to epochal evolution by potentiated targeting of new variants to Lewis-positive secretor-positive individuals. The temporal variations also result in significant differences in the electrostatic landscape likely reflecting antigenic variations. The proximity of some of these changes to the HBGA binding sites suggests the possibility of a coordinated interplay between antigenicity and HBGA binding in epochal evolution. From the observation that the regions involved in the formation of the HBGA binding sites can be conformationally flexible, we suggest a plausible mechanism for how norovirus disassociates from salivary mucin-linked HBGA before re-associating with HBGAs linked to intestinal epithelial cells during its passage through the gastrointestinal tract. Structural Analysis of HBGA Binding Specificity in a Norovirus GII.4 Epidemic Variant: Implications for Epochal Evolution.,Shanker S, Choi JM, Sankaran B, Atmar RL, Estes MK, Prasad BV J Virol. 2011 Jun 29. PMID:21715503 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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