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Lysogenic bacteriophage D3 causes seroconversion ofPseudomonas aeruginosa PAO1 from serotype O5 to O16 by inverting the linkage between O-specific antigen (OSA) repeat units from α to β. The OSA units are polymerized by Wzy to modal lengths regulated by Wzz1 and Wzz2 . A key component of the D3 seroconversion machinery is thei nhibitor ofα -p olymerase (Iap) peptide, which is able to solely suppress α-linked long-chain OSA production inP. aeruginosa PAO1. To establish the target specificity of Iap for Wzyα , changes in OSA phenotypes were examined via Western immunoblotting forwzz 1 andwzz 2 single-knockout strains, as well as awzz 1 wzz 2 double knockout, following the expression ofiap from a tuneable vector. Increased induction of Iap expression completely abrogated OSA production in thewzz 1 wzz 2 double mutant, while background levels of OSA production were still observed in either of the single mutants. Therefore, Iap inhibition of OSA biosynthesis was most effective in the absence of both Wzz proteins. Sequence alignment analyses revealed a high degree of similarity between Iap and the first transmembrane segment (TMS) of either Wzz1 or Wzz2 . Various topology prediction analyses of the Iap sequence consistently predicted the presence of a single TMS, suggesting a propensity for Iap to insert itself into the inner membrane (IM). The compromised ability of Iap to abrogate Wzyα function in the presence of Wzz1 or Wzz2 provides compelling evidence that inhibition occurs after Wzyα inserts itself into the IM and is achieved through mimicry of the first TMS from the Wzz proteins ofP. aeruginosa PAO1.

journal of bacteriology

The D3 Bacteriophage α-Polymerase Inhibitor (Iap) Peptide Disrupts O-Antigen Biosynthesis through Mimicry of the Chain Length Regulator Wzz in Pseudomonas aeruginosa