7F0H

Structural and functional characterization of bovine G1P[5] rotavirus VP8* protein

Summary for 7F0H

• Entry DOI: 10.2210/pdb7f0h/pdb
• Descriptor: Outer capsid protein VP8* (2 entities in total)
• Functional Keywords: glycan binding specificity, sialic acid, histo-blood group antigen, viral protein
• Biological source: Rotavirus A
• Total number of polymer chains: 2
• Total formula weight: 36174.85

Authors

Duan, Z.,Sun, X. (deposition date: 2021-06-04, release date: 2021-12-29, Last modification date: 2023-11-29)

Primary citation

Dang, L.,Su, Y.,Qi, J.,Wu, Z.,Li, D.,Wang, M.,Zhang, Q.,Wang, H.,Bai, R.,Duan, Z.,Sun, X.
Structural and functional characterization of bovine G1P[5] rotavirus VP8* protein.
Virology, 563:116-125, 2021

PubMed Abstract: The widely used rotavirus (RV) vaccine, Rotateq, contained reassortment strains of human and bovine G1/2/3/4P[5] RVs. The functional and structural features of bovine G1P[5] VP8* were investigated. Bovine G1P[5] VP8* was identified to interact with sialic acids and sialic acid-containing glycans. In addition, P[5] VP8* recognized α-Gal histo-blood group antigens (HBGAs). Bovine G1P[5] VP8* did not hemagglutinate the tested red blood cells. The crystal structure of P[5] VP8* was determined at 1.7 Å. Structural superimposition revealed that P[5] VP8* was most close to human P[8] VP8*, while much further to VP8*s of porcine P[7] and rhesus P[3]. Sequence alignment showed that amino acids of the putative glycan binding site in P[5] VP8* were different to those in P[3]/P[7] VP8*s, indicating that P[5] VP8* may interact with glycans using different mechanism. This study provided more understanding of P[5] RV infection and the interactions of RV VP8* and glycans.

PubMed: 34509703
DOI: 10.1016/j.virol.2021.08.009

Experimental method

X-RAY DIFFRACTION (1.695 Å)