Human group A rotavirus P[25] VP8* specifically binds to A-type histo-blood group antigen

Highlights: • Determine the crystal structure of human P[25] RV VP8* and uncover the VP8* structural characteristics. • Confirm that human P[25] VP8* specifically interacted with A-type histo-blood group antigen. • P[25] VP8* was most close to P[14] VP8* and possessed basically the same residues and conformation as that in P[14] VP8*. • A-type histo-blood group antigen may play an important role in the RV prevalence and transmission. 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.