Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antigens, Bacterial / chemistry
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Antigens, Bacterial / genetics
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Antigens, Bacterial / immunology
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Antigens, Bacterial / metabolism*
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Bacterial Outer Membrane Proteins / chemistry
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Bacterial Outer Membrane Proteins / genetics
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Bacterial Outer Membrane Proteins / immunology
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Bacterial Outer Membrane Proteins / metabolism*
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Fimbriae Proteins / metabolism*
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Glycosylation
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Molecular Sequence Data
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Neisseria gonorrhoeae / enzymology*
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Neisseria gonorrhoeae / immunology
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Neisseria gonorrhoeae / pathogenicity
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Neisseria meningitidis / enzymology*
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Neisseria meningitidis / pathogenicity
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Nitrite Reductases / chemistry
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Nitrite Reductases / genetics
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Nitrite Reductases / immunology
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Nitrite Reductases / metabolism*
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Protein Conformation
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Protein Processing, Post-Translational*
Substances
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Antigens, Bacterial
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Bacterial Outer Membrane Proteins
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aniA protein, Neisseria gonorrhoeae
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Fimbriae Proteins
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Nitrite Reductases