A viral protein antibiotic inhibits lipid II flippase activity.

ABSTRACT: For bacteriophage infections, the cell walls of bacteria, consisting of a single highly polymeric molecule of peptidoglycan (PG), pose a major problem for the release of progeny virions. Phage lysis proteins that overcome this barrier can point the way to new antibacterial strategies ¹ , especially small lytic single-stranded DNA (the microviruses) and RNA phages (the leviviruses) that effect host lysis using a single non-enzymatic protein ² . Previously, the A₂ protein of levivirus Qβ and the E protein of the microvirus ϕX174 were shown to be 'protein antibiotics' that inhibit the MurA and MraY steps of the PG synthesis pathway ^2-4 . Here, we investigated the mechanism of action of an unrelated lysis protein, Lys^M, of the Escherichia

SUBMITTER: Chamakura KR 

PROVIDER: S-EPMC5764540 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature