7C8P

Structural and functional characterization of human group A rotavirus P[25] VP8*

Summary for 7C8P

• Entry DOI: 10.2210/pdb7c8p/pdb
• Descriptor: Outer capsid protein VP4 (2 entities in total)
• Functional Keywords: human p[25] rotavirus, glycan binding specificity, vp8*, histo-blood group antigen (hbga), protein binding
• Biological source: Rotavirus A
• Total number of polymer chains: 2
• Total formula weight: 36927.27

Authors

Duan, Z.,Dandi, L. (deposition date: 2020-06-03, release date: 2021-04-14, Last modification date: 2023-11-29)

Primary citation

Li, D.,Wang, M.,Qi, J.,Zhang, Q.,Wang, H.,Pang, L.,Sun, X.,Duan, Z.
Human group A rotavirus P[25] VP8* specifically binds to A-type histo-blood group antigen.
Virology, 555:56-63, 2021

PubMed 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.

PubMed: 33453651
DOI: 10.1016/j.virol.2020.12.016

Experimental method

X-RAY DIFFRACTION (2.6 Å)