Download MendeleyFunctional and Structural Characterization of P[19] Rotavirus VP8* Interaction with Histo-blood Group Antigens.
Sun, X., Li, D., Peng, R., Guo, N., Jin, M., Zhou, Y., Xie, G., Pang, L., Zhang, Q., Qi, J., Duan, Z.J.(2016) J Virol 90: 9758-9765
- PubMed: 27535055
- DOI: https://doi.org/10.1128/JVI.01566-16
- Primary Citation of Related Structures:
5GJ6 - PubMed Abstract:
Rotaviruses (RVs) of species A (RVA) are a major causative agent of acute gastroenteritis. Recently, histo-blood group antigens (HBGAs) have been reported to interact with human RVA VP8* proteins. Human P[19] is a rare P genotype of porcine origin that infects humans sporadically. The functional and structural characteristics of P[19] VP8* interaction with HBGAs are unknown. In this study, we expressed and purified the VP8* proteins of human and porcine P[19] RVs. In oligosaccharide and saliva binding assays, P[19] VP8* proteins showed obvious binding to A-, B-, and O-type saliva samples irrespective of the secretor status, implying broad binding patterns. However, they did not display specific binding to any of the oligosaccharides tested. In addition, we solved the structure of human P[19] VP8* at 2.4 Å, which revealed a typical galectin-like fold. The structural alignment demonstrated that P[19] VP8* was most similar to that of P[8], which was consistent with the phylogenetic analysis. Structure superimposition revealed the basis for the lack of binding to the oligosaccharides. Our study indicates that P[19] RVs may bind to other oligosaccharides or ligands and may have the potential to spread widely among humans. Thus, it is necessary to place the prevalence and evolution of P[19] RVs under surveillance.
Organizational Affiliation:
Key Laboratory of Medical Virology and Viral Diseases, Ministry of Health of the People's Republic of China, Beijing, China National Institute for Viral Disease Control and Prevention, China CDC, Beijing, China.
