5VKS

Crystal structure of P[19] rotavirus VP8* complexed with LNFPI

Summary for 5VKS

• Entry DOI: 10.2210/pdb5vks/pdb
• Related: 5VKI
• 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-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (5 entities in total)
• Functional Keywords: complex, p[19]vp8*, lnfpi, viral protein
• Biological source: Human rotavirus A
• Total number of polymer chains: 2
• Total formula weight: 38600.38

Authors

Xu, S.,Liu, Y.,Woodruff, A.,Zhong, W.,Jiang, X.,Kennedy, M.A. (deposition date: 2017-04-22, release date: 2017-11-08, Last modification date: 2023-10-04)

Primary citation

Liu, Y.,Xu, S.,Woodruff, A.L.,Xia, M.,Tan, M.,Kennedy, M.A.,Jiang, X.
Structural basis of glycan specificity of P[19] VP8*: Implications for rotavirus zoonosis and evolution.
PLoS Pathog., 13:e1006707-e1006707, 2017

PubMed Abstract: Recognition of specific cell surface glycans, mediated by the VP8* domain of the spike protein VP4, is the essential first step in rotavirus (RV) infection. Due to lack of direct structural information of virus-ligand interactions, the molecular basis of ligand-controlled host ranges of the major human RVs (P[8] and P[4]) in P[II] genogroup remains unknown. Here, through characterization of a minor P[II] RV (P[19]) that can infect both animals (pigs) and humans, we made an important advance to fill this knowledge gap by solving the crystal structures of the P[19] VP8* in complex with its ligands. Our data showed that P[19] RVs use a novel binding site that differs from the known ones of other genotypes/genogroups. This binding site is capable of interacting with two types of glycans, the mucin core and type 1 histo-blood group antigens (HBGAs) with a common GlcNAc as the central binding saccharide. The binding site is apparently shared by other P[II] RVs and possibly two genotypes (P[10] and P[12]) in P[I] as shown by their highly conserved GlcNAc-interacting residues. These data provide strong evidence of evolutionary connections among these human and animal RVs, pointing to a common ancestor in P[I] with a possible animal host origin. While the binding properties to GlcNAc-containing saccharides are maintained, changes in binding to additional residues, such as those in the polymorphic type 1 HBGAs may occur in the course of RV evolution, explaining the complex P[II] genogroup that mainly causes diseases in humans but also in some animals.

PubMed: 29136651
DOI: 10.1371/journal.ppat.1006707

Experimental method

X-RAY DIFFRACTION (1.94 Å)