4RLZ: Crystal Structure Of Norovirus Oif P Domain

Citation:
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.
PDB ID: 4RLZDownload
MMDB ID: 130259
PDB Deposition Date: 2014/10/18
Updated in MMDB: 2015/11
Experimental Method:
x-ray diffraction
Resolution: 1.19  Å
Source Organism:
Similar Structures:
Biological Unit for 4RLZ: dimeric; determined by author and by software (PISA)
Molecular Components in 4RLZ
Label Count Molecule
Proteins (2 molecules)
2
Capsid Protein
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

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