4rm0
Crystal structure of Norovirus OIF P domain in complex with Lewis a trisaccharideCrystal structure of Norovirus OIF P domain in complex with Lewis a trisaccharide
Structural highlights
Publication Abstract from PubMedNorovirus (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. A Unique Human Norovirus Lineage with a Distinct HBGA Binding Interface.,Liu W, Chen Y, Jiang X, Xia M, Yang Y, Tan M, Li X, Rao Z PLoS Pathog. 2015 Jul 6;11(7):e1005025. doi: 10.1371/journal.ppat.1005025., eCollection 2015 Jul. PMID:26147716[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||