Functional and Structural Characterization of P[19] Rotavirus VP8* Interaction with Histo-blood Group Antigens

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 2016 Aug 19

PMID 27535055

Citations 13

Authors

Xiaoman Sun

Dandi Li

Ruchao Peng

Nijun Guo

Miao Jin

Yongkang Zhou

Guangcheng Xie

Lili Pang

Qing Zhang

Jianxun Qi

Zhao-Jun Duan

Affiliations

Soon will be listed here.

Abstract

Importance: Human P[19] is a rare P genotype of porcine origin. Based on phylogenetic analysis of VP8* sequences, P[19] was classified in the P[II] genogroup, together with P[4], P[6], and P[8], which have been reported to interact with HBGAs in a genotype-dependent manner. In this study, we explored the functional and structural characteristics of P[19] VP8* interaction with HBGAs. P[19] VP8* showed binding to A-, B-, and O-type saliva samples, as well as saliva of nonsecretors. This implies that P[19] has the potential to spread among humans with a broad binding range. Careful attention should be paid to the evolution and prevalence of P[19] RVs. Furthermore, we solved the structure of P[19] VP8*. Structure superimposition indicated that P[19] may bind to other oligosaccharides or ligands using potential binding sites, suggesting that further investigation of the specific cell attachment factors is warranted.

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