The abstract is read at the publisher; the summary is JClub's.
Sgl protein from the ssRNA phage varphiCb5 targets MraY, and its membrane topology and residue distribution parallel the varphiX174 E protein despite no detectable sequence similarity.
- Why it matters: Host lysis by single Sgl proteins can block peptidoglycan synthesis at distinct steps, but how an ssRNA phage Sgl can inhibit MraY—and whether this reflects convergence or crossover—was unknown.
- What they did: Physiological evidence was used to show Sgl< varphiCb5 inhibits MraY; the study compared hydrophobic/charged residue distribution and an N-out, C-in topology, and tested lytic activity in an Sgl< varphiCb5>-LacZ fusion.
- The result: Expression of the Caulobacter FKBP-type isomerase CC2799 enhances Sgl< varphiCb5–mediated lysis in E. coli, supporting functional parallels across the RNA–DNA phage boundary.
The findingWhy it mattersWhat they didThe result
AI summary of the abstract · may contain errors · not medical advice · read the paper.