Glycan recognition in globally dominant human rotaviruses

Hu, Liya; 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

doi:10.1038/s41467-018-05098-4

Title: Glycan recognition in globally dominant human rotaviruses

Journal Article · Fri Jul 06 00:00:00 EDT 2018 · Nature Communications

DOI:https://doi.org/10.1038/s41467-018-05098-4· OSTI ID:1478359

Hu, Liya ^[1]; Sankaran, Banumathi ^[2]; Laucirica, Daniel R. ^[1]; Patil, Ketki ^[1]; Salmen, Wilhelm ^[1]; Ferreon, Allan Chris M. ^[1]; Tsoi, Phoebe S. ^[1]; Lasanajak, Yi ^[3]; Smith, David F. ^[3]; Ramani, Sasirekha ^[1]; Atmar, Robert L. ^[1]; Estes, Mary K. ^[1]; Ferreon, Josephine C. ^[1]; Prasad, B. V. Venkataram ^[1]

Baylor College of Medicine, Houston, TX (United States)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Emory Univ. School of Medicine, Atlanta, GA (United States)

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.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1478359

Journal Information:: Nature Communications, Vol. 9, Issue 1; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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