Structural basis of glycan specificity of P[19] VP8*: Implications for rotavirus zoonosis and evolution

@inproceedings{Liu2017StructuralBO,
  title={Structural basis of glycan specificity of P[19] VP8*: Implications for rotavirus zoonosis and evolution},
  author={Yang Liu and Shenyuan Xu and Andrew L Woodruff and Ming Xia and Ming Tan and Michael A Kennedy and Xi Jiang},
  booktitle={PLoS pathogens},
  year={2017}
}
Recognition of specific cell surface glycans, mediated by the VP8* domain of the spike protein VP4, is the essential first step in rotavirus (RV) infection. Due to lack of direct structural information of virus-ligand interactions, the molecular basis of ligand-controlled host ranges of the major human RVs (P[8] and P[4]) in P[II] genogroup remains unknown. Here, through characterization of a minor P[II] RV (P[19]) that can infect both animals (pigs) and humans, we made an important advance to… CONTINUE READING
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Both Lewis and secretor status mediate susceptibility to rotavirus infections in a rotavirus genotype-dependent manner.

Clinical infectious diseases : an official publication of the Infectious Diseases Society of America • 2014

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