Abstract
Pilin is the major subunit of the essential virulence factor pili and is glycosylated at Ser63. In this study we investigated the gene pglI to determine whether it is involved in the biosynthesis of the pilin-linked glycan of Neisseria meningitidis strain C311#3. A N. meningitidis C311#3pglI mutant resulted in a change of apparent molecular weight in SDS-PAGE and altered binding of antisera, consistent with a role in the biosynthesis of the pilin-linked glycan. These data, in conjunction with homology with well-characterised acyltransferases suggests a specific role for pglI in the biosynthesis of the basal 2,4-diacetamido-2,4,6-trideoxyhexose residue of the pilin-linked glycan.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetyltransferases / genetics
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Acetyltransferases / metabolism*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Cloning, Molecular
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DNA, Bacterial / genetics
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Fimbriae Proteins / metabolism*
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Fimbriae, Bacterial / metabolism*
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Genes, Bacterial
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Glycosylation
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Humans
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Immune Sera
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Lipopolysaccharides / biosynthesis
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Molecular Sequence Data
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Mutation
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Neisseria meningitidis / genetics
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Neisseria meningitidis / metabolism*
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Neisseria meningitidis / pathogenicity
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Phenotype
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Protein Processing, Post-Translational*
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Sequence Homology, Amino Acid
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Trisaccharides / immunology
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Virulence
Substances
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Bacterial Proteins
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DNA, Bacterial
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Immune Sera
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Lipopolysaccharides
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Trisaccharides
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Fimbriae Proteins
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Acetyltransferases
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pglI protein, Neisseria meningitidis