5JDB

Binding specificity of P[8] VP8* proteins of rotavirus vaccine strains with histo-blood group antigens

Summary for 5JDB

• Entry DOI: 10.2210/pdb5jdb/pdb
• Descriptor: Outer capsid protein VP4 (2 entities in total)
• Functional Keywords: rotavirus, vp8, vaccine, viral protein
• Biological source: Rotavirus A
• Cellular location: Host rough endoplasmic reticulum . Virion : E2EA82
• Total number of polymer chains: 6
• Total formula weight: 110924.26

Authors

Sun, X.,Guo, N.,Li, D.,Zhou, Y.,Jin, M.,Xie, G.,Pang, L.,Zhang, Q.,Cao, Y.,Duan, Z. (deposition date: 2016-04-16, release date: 2016-07-13, Last modification date: 2023-11-08)

Primary citation

Sun, X.,Guo, N.,Li, D.,Jin, M.,Zhou, Y.,Xie, G.,Pang, L.,Zhang, Q.,Cao, Y.,Duan, Z.J.
Binding specificity of P[8] VP8* proteins of rotavirus vaccine strains with histo-blood group antigens.
Virology, 495:129-135, 2016

PubMed Abstract: RotaTeq(®) and Rotarix™ are two common human rotavirus (RV) vaccines currently on the market worldwide. Recent studies indicate histo-blood group antigens (HBGAs) may be attachment factors for RVs. The P[8] VP8* proteins of RotaTeq and Rotarix were expressed and purified, and their binding specificities were evaluated. Saliva-based binding assays showed that the VP8* proteins bound to the saliva samples of secretors irrespective of ABO blood types. However, in the oligosaccharide binding assay, the VP8* proteins displayed no specific binding to the HBGAs tested, including Lewis b and H1. The structure of RotaTeq P[8] VP8* was solved at 1.9Å. Structural comparisons revealed that the putative receptor binding site was different to that of other genotypes and displayed a novel potential binding region. These findings indicate RotaTeq and Rotarix may have better efficiency in areas with a high percentage of secretors.

PubMed: 27209447
DOI: 10.1016/j.virol.2016.05.010

Experimental method

X-RAY DIFFRACTION (1.901 Å)