4RLZ

Crystal structure of Norovirus OIF P domain

Summary for 4RLZ

• Entry DOI: 10.2210/pdb4rlz/pdb
• Related: 4RM0
• Descriptor: Capsid protein, GLYCEROL (3 entities in total)
• Functional Keywords: mixed alpha/beta structure, receptor binding, hbga, virus caspid, viral protein
• Biological source: Norovirus NLV/IF1998/2003/Iraq
• Total number of polymer chains: 2
• Total formula weight: 69034.70

Authors

Liu, W.,Chen, Y.,Tan, M.,Xia, M.,Li, X.,Jiang, X.,Rao, Z. (deposition date: 2014-10-18, release date: 2015-06-24, Last modification date: 2023-11-08)

Primary citation

Liu, W.,Chen, Y.,Jiang, X.,Xia, M.,Yang, Y.,Tan, M.,Li, X.,Rao, Z.
A Unique Human Norovirus Lineage with a Distinct HBGA Binding Interface.
Plos Pathog., 11:e1005025-e1005025, 2015

PubMed Abstract: Norovirus (NoV) causes epidemic acute gastroenteritis in humans, whereby histo-blood group antigens (HBGAs) play an important role in host susceptibility. Each of the two major genogroups (GI and GII) of human NoVs recognizes a unique set of HBGAs through a distinct binding interface that is conserved within a genogroup, indicating a distinct evolutionary path for each genogroup. Here, we characterize a Lewis a (Lea) antigen binding strain (OIF virus) in the GII.21 genotype that does not share the conserved GII binding interface, revealing a new evolution lineage with a distinct HBGA binding interface. Sequence alignment showed that the major residues contributing to the new HBGA binding interface are conserved among most members of the GII.21, as well as a closely related GII.13 genotype. In addition, we found that glycerol inhibits OIF binding to HBGAs, potentially allowing production of cheap antivirals against human NoVs. Taken together, our results reveal a new evolutionary lineage of NoVs selected by HBGAs, a finding that is important for understanding the diversity and widespread nature of NoVs.

PubMed: 26147716
DOI: 10.1371/journal.ppat.1005025

Experimental method

X-RAY DIFFRACTION (1.19 Å)