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- Title
Glycan recognition in globally dominant human rotaviruses.
- Authors
Liya Hu; Sankaran, Banumathi; Laucirica, Daniel R.; Patil, Ketki; Salmen, Wilhelm; Ferreon, Allan Chris M.; Tsoi, Phoebe S.; Lasanajak, Yi; Smith, David F.; Ramani, Sasirekha; Atmar, Robert L.; Estes, Mary K.; Ferreon, Josephine C.; Prasad, B. V. Venkataram
- Abstract
Rotaviruses (RVs) cause life-threatening diarrhea in infants and children worldwide. Recent biochemical and epidemiological studies underscore the importance of histo-blood group antigens (HBGA) as both cell attachment and susceptibility factors for the globally dominant P[4], P[6], and P[8] genotypes of human RVs. How these genotypes interact with HBGA is not known. Here, our crystal structures of P[4] and a neonate-specific P[6] VP8*s alone and in complex with H-type I HBGA reveal a unique glycan binding site that is conserved in the globally dominant genotypes and allows for the binding of ABH HBGAs, consistent with their prevalence. Remarkably, the VP8* of P[6] RVs isolated from neonates displays subtle structural changes in this binding site that may restrict its ability to bind branched glycans. This provides a structural basis for the age-restricted tropism of some P[6] RVs as developmentally regulated unbranched glycans are more abundant in the neonatal gut.
- Publication
Nature Communications, 2018, Vol 9, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-018-05098-4