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The pilin O-glycosylation pathway of pathogenic Neisseria is a general system that glycosylates AniA, an outer membrane nitrite reductase.
Ku, S C; Schulz, B L; Power, P M; Jennings, M P.
Affiliation
  • Ku SC; School of Molecular and Microbial Sciences, The University of Queensland, St. Lucia, Brisbane, Qld 4072, Australia.
Biochem Biophys Res Commun ; 378(1): 84-9, 2009 Jan 02.
Article in En | MEDLINE | ID: mdl-19013435
O-Glycosylation is emerging as a common posttranslational modification of surface exposed proteins in bacterial mucosal pathogens. In pathogenic Neisseria an O-glycosylation pathway modifies a single abundant protein, pilin, the subunit protein that forms pili. Here, we identify an additional outer membrane glycoprotein in pathogenic Neisseria, the nitrite reductase AniA, that is glycosylated in its C-terminal repeat region by the pilin glycosylation pathway. To our knowledge, this is the first report of a general O-glycosylation pathway in a prokaryote. We also show that AniA displays polymorphisms in residues that map to the surface of the protein. A frame-shift mutation abolishes AniA expression in 34% of Neisseria meningitidis strains surveyed, however, all Neisseria gonorrhoeae strains examined are predicted to express AniA, implying a crucial role for AniA in gonococcal biology.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Outer Membrane Proteins / Protein Processing, Post-Translational / Fimbriae Proteins / Antigens, Bacterial / Neisseria gonorrhoeae / Neisseria meningitidis / Nitrite Reductases Language: En Journal: Biochem Biophys Res Commun Year: 2009 Document type: Article Affiliation country: Australia Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Outer Membrane Proteins / Protein Processing, Post-Translational / Fimbriae Proteins / Antigens, Bacterial / Neisseria gonorrhoeae / Neisseria meningitidis / Nitrite Reductases Language: En Journal: Biochem Biophys Res Commun Year: 2009 Document type: Article Affiliation country: Australia Country of publication: United States