The abstract is read at the publisher; the summary is JClub's.
Cryo-EM of in vitro–assembled murine RegIIIγ filaments shows conserved hexamer stacking but a distinct protofilament arrangement, and structure-guided mutagenesis indicates monomeric function.
- Why it matters: RegIII proteins kill Gram-positive bacteria under acidic conditions, but the proposed hexameric pore mechanism for RegIIIγ’s homologs was unclear and needed direct structural and functional testing.
- What they did: The authors solved the cryo-EM structure of assembled RegIIIγ filaments, performed structure-guided mutagenesis to test oligomeric state, and assayed peptidoglycan degradation and bactericidal activity across acidic versus neutral conditions.
- The result: RegIIIγ catalyzes peptidoglycan degradation without requiring it for killing, and an assembly-deficient RegIIIγ mutant retains bactericidal activity in both acidic and neutral conditions.
The findingWhy it mattersWhat they didThe result
AI summary of the abstract · may contain errors · not medical advice · read the paper.