Murine norovirus allosteric escape mutants mimic gut activation.

ABSTRACT: Murine norovirus (MNV) undergoes large conformational changes in response to the environment. The T=3 icosahedral capsid is composed of 180 copies of ~58 kDa VP1 that has N-terminal (N), shell (S), and C-terminal protruding (P) domains. In phosphate-buffered saline, the P domains are loosely tethered to the shell and float ~15 Å above the surface. At conditions found in the gut (i.e., low pH with high metal ion and bile salt concentrations), the P domain rotates and drops onto the shell with intra P domain changes that enhance receptor interactions while blocking antibody binding. Two of our monoclonal antibodies (2D3 and 4F9) have broad strain recognition, and the only escape mutants, V339I and D348E, are located on the C'D' loop and ~20 Å from the epitope. Here, we determined the cryo-EM

SUBMITTER: Sherman MB 

PROVIDER: S-EPMC12172446 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature