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Updated: Nov 21, 2025
Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus
Published on: January 28, 2019
Human group A rotavirus P[25] VP8* specifically binds to A-type histo-blood group antigen
Dandi Li1, Mengxuan Wang1, Jianxun Qi2
1National Health Commission Key Laboratory for Medical Virology and Viral Diseases, Beijing, 102206, China; National Institute for Viral Disease Control and Prevention, China CDC, Beijing, 102206, China.
Abstract:
Rotavirus (RV) is a common cause of acute gastroenteritis in young children. While P[8] and P[4] are the most prevalent RV genotypes in humans, other genotypes are also reported in human infections occasionally, including human P[25]. The glycan binding and structural characteristics of human P[25] were explored in our study. Human P[25] VP8* recognized type A histo-blood group antigen (HBGA) in the glycan microarray/oligosaccharide binding assay and could specifically hemagglutinate type A blood cells. Moreover, the P[25] VP8* structure was determined at 2.6 Å, revealing a similar conformation and a conserved putative glycan binding site as that of P[14] VP8*. This study provided further knowledge of the glycan binding and structural features of P[25] RV VP8*, promoting our understanding of the infection, prevalence, and host range of the P[III] RVs.
Insights
This study investigated human P[25] rotavirus (RV) VP8*, finding it binds to type A histo-blood group antigens. Understanding these glycan interactions advances knowledge of rotavirus infection and host range.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- Rotavirus (RV) is a leading cause of gastroenteritis in children.
- P[8] and P[4] are common RV genotypes, but others like P[25] also occur in human infections.
Purpose of the Study:
- To explore the glycan binding and structural characteristics of human P[25] RV VP8*.
- To understand the molecular basis for P[25] RV interactions with host cells.
Main Methods:
- Glycan microarray and oligosaccharide binding assays were used to determine glycan specificity.
- X-ray crystallography was employed to determine the structure of P[25] VP8*.
Main Results:
- Human P[25] VP8* specifically recognized and bound to type A histo-blood group antigens (HBGAs).
- P[25] VP8* demonstrated hemagglutination activity specific to type A blood cells.
- The determined structure of P[25] VP8* revealed a conformation and glycan binding site similar to P[14] VP8*.
Conclusions:
- This research elucidates the glycan binding and structural features of human P[25] RV VP8*.
- Findings contribute to understanding the infection mechanisms, prevalence, and host tropism of P[III] rotaviruses.
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