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Functional and Structural Characterization of P[19] Rotavirus VP8* Interaction with Histo-blood Group Antigens
Xiaoman Sun1, Dandi Li1, Ruchao Peng2
1Key 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.
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.
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.
Insights
Porcine rotavirus P[19] VP8* proteins bind broadly to human saliva, suggesting potential for widespread human transmission. Further surveillance of P[19] rotavirus evolution and prevalence is crucial.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- Rotaviruses (RVs) are a leading cause of gastroenteritis.
- Histo-blood group antigens (HBGAs) interact with human rotavirus VP8* proteins.
- The P[19] genotype, of porcine origin, is a rare cause of human rotavirus infections.
Purpose of the Study:
- To investigate the functional and structural characteristics of P[19] VP8* interaction with HBGAs.
- To determine the binding patterns of P[19] VP8* to human saliva and oligosaccharides.
- To elucidate the structure of human P[19] VP8* and its implications for ligand binding.
Main Methods:
- Expression and purification of human and porcine P[19] RV VP8* proteins.
- Oligosaccharide and saliva binding assays.
- X-ray crystallography to determine the 3D structure of human P[19] VP8*.
- Phylogenetic analysis and structural alignment.
Main Results:
- P[19] VP8* proteins exhibited broad binding to A-, B-, and O-type saliva, regardless of secretor status.
- No specific binding was observed with tested oligosaccharides.
- The solved structure of human P[19] VP8* revealed a galectin-like fold, similar to P[8] VP8*.
- Structural analysis suggested potential binding sites for other ligands.
Conclusions:
- P[19] rotaviruses possess broad binding capabilities, indicating potential for widespread human transmission.
- The lack of specific oligosaccharide binding suggests alternative attachment factors.
- Continued surveillance of P[19] rotavirus prevalence and evolution is recommended.
