6K2O

Structural basis of glycan recognition in globally predominant human P[8] rotavirus

Summary for 6K2O

• Entry DOI: 10.2210/pdb6k2o/pdb
• Descriptor: Outer capsid protein VP4, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose, SODIUM ION, ... (4 entities in total)
• Functional Keywords: glycan binding specificity, vp8* structure, mucin core 2, lacto-n-fucopentaose 1 (lnfp1), viral protein
• Biological source: Rotavirus A
• Total number of polymer chains: 1
• Total formula weight: 19607.40

Authors

Duan, Z.,Sun, X. (deposition date: 2019-05-15, release date: 2019-10-09, Last modification date: 2023-11-22)

Primary citation

Sun, X.,Dang, L.,Li, D.,Qi, J.,Wang, M.,Chai, W.,Zhang, Q.,Wang, H.,Bai, R.,Tan, M.,Duan, Z.
Structural Basis of Glycan Recognition in Globally Predominant Human P[8] Rotavirus.
Virol Sin, 35:156-170, 2020

PubMed Abstract: Rotavirus (RV) causes acute gastroenteritis in infants and children worldwide. Recent studies showed that glycans such as histo-blood group antigens (HBGAs) function as cell attachment factors affecting RV host susceptibility and prevalence. P[8] is the predominant RV genotype in humans, but the structural basis of how P[8] RVs interact with glycan ligands remains elusive. In this study, we characterized the interactions between P[8] VP8*s and glycans which showed that VP8*, the RV glycan binding domain, recognized both mucin core 2 and H type 1 antigens according to the ELISA-based oligosaccharide binding assays. Importantly, we determined the structural basis of P[8] RV-glycans interaction from the crystal structures of a Rotateq P[8] VP8* in complex with core 2 and H type 1 glycans at 1.8 Å and 2.3 Å, respectively, revealing a common binding pocket and similar binding mode. Structural and sequence analysis demonstrated that the glycan binding site is conserved among RVs in the P[II] genogroup, while genotype-specific amino acid variations determined different glycan binding preference. Our data elucidated the detailed structural basis of the interactions between human P[8] RVs and different host glycan factors, shedding light on RV infection, epidemiology, and development of anti-viral agents.

PubMed: 31620994
DOI: 10.1007/s12250-019-00164-7

Experimental method

X-RAY DIFFRACTION (2.296 Å)