The pilin O-glycosylation pathway of pathogenic Neisseria is a general system that glycosylates AniA, an outer membrane nitrite reductase.
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Outer Membrane Proteins
/
Protein Processing, Post-Translational
/
Fimbriae Proteins
/
Antigens, Bacterial
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Neisseria gonorrhoeae
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Neisseria meningitidis
/
Nitrite Reductases
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
2009
Document type:
Article
Affiliation country:
Australia
Country of publication:
United States