Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation.

ABSTRACT: Neisseria meningitidis PglL belongs to a novel family of bacterial oligosaccharyltransferases (OTases) responsible for O-glycosylation of type IV pilins. Although members of this family are widespread among pathogenic bacteria, there is little known about their mechanism. Understanding the O-glycosylation process may uncover potential targets for therapeutic intervention, and can open new avenues for the exploitation of these pathways for biotechnological purposes. In this work, we demonstrate that PglL is able to transfer virtually any glycan from the undecaprenyl pyrophosphate (UndPP) carrier to pilin in engineered Escherichia coli and Salmonella cells. Surprisingly, PglL was also able to interfere with the peptidoglycan biosynthetic machinery and transfer peptidoglycan subunits to pilin

SUBMITTER: Faridmoayer A 

PROVIDER: S-EPMC3259870 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature