title: Pilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzy-dependent O-antigen biosynthesis in Escherichia coli.
abstract: Pili (type IV fimbriae) of Neisseria meningitidis are glycosylated by the addition of O-linked sugars. Recent work has shown that PglF, a protein with homology to O-antigen 'flippases', is required for the biosynthesis of the pilin-linked glycan and suggests pilin glycosylation occurs in a manner analogous to the wzy-dependent addition of O-antigen to the core-LPS. O-Antigen ligases are crucial in this pathway for the transfer of undecraprenol-linked sugars to the LPS-core in Gram-negative bacteria. An O-antigen ligase homologue, pglL, was identified in N. meningitidis. PglL mutants showed no change in LPS phenotypes but did show loss of pilin glycosylation, confirming PglL is essential for pilin O-linked glycosylation in N. meningitidis.
authors.affiliation: School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Qld 4072, Australia.
authors.forename: Peter M
authors.initials: PM
authors.lastname: Power
authors.forename: Kate L
authors.initials: KL
authors.lastname: Seib
authors.forename: Michael P
authors.initials: MP
authors.lastname: Jennings
mesh_terms: D004926:Escherichia coli / Q000378:metabolism*; D036781:Fimbriae Proteins / Q000378:metabolism*; D006031:Glycosylation; D008025:Ligases / Q000378:metabolism*; D009345:Neisseria meningitidis / Q000378:metabolism*; D019081:O Antigens / Q000096:biosynthesis*
chemical_list: D019081:O Antigens; D036781:Fimbriae Proteins; D008025:Ligases