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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
