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rdf:type |
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lifeskim:mentions |
umls-concept:C0018494,
umls-concept:C0020792,
umls-concept:C0031921,
umls-concept:C0033666,
umls-concept:C0041102,
umls-concept:C0071061,
umls-concept:C0080194,
umls-concept:C0205214,
umls-concept:C0205419,
umls-concept:C0521018,
umls-concept:C1555721,
umls-concept:C1706204
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pubmed:dateCreated |
1997-1-31
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pubmed:databankReference |
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pubmed:abstractText |
Neisseria meningitidis pili are filamentous protein structures that are essential adhesins in capsulate bacteria. Pili of adhesion variants of meningococcal strain C311 contain glycosyl residues on pilin (PilE), their major structural subunit. Recent studies have shown that a novel O-linked trisaccharide substituent, not previously found as a constituent of glycoproteins, is present within a peptide spanning amino acid residues 50 to 73 of the PilE molecule. The structure was shown to be Gal beta 1-4 Gal alpha 1-3 diacetamidotrideoxyhexose which is directly attached to pilin. Pilins derived from galactose epimerase (galE) mutants lack the digalactosyl moiety, but retain the diacetamidotrideoxyhexose substitution. These studies confirm our previous observations that meningococcal pili are glycosylated and provide the first structural evidence for the presence of covalently linked carbohydrate on pili. We have identified a completely novel protein/carbohydrate linkage on a multimeric protein that is an essential virulence determinant in N. meningitidis.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0077-8923
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
797
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
53-64
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:8993351-Amino Acid Sequence,
pubmed-meshheading:8993351-Bacterial Proteins,
pubmed-meshheading:8993351-Fimbriae, Bacterial,
pubmed-meshheading:8993351-Fimbriae Proteins,
pubmed-meshheading:8993351-Galactose,
pubmed-meshheading:8993351-Genetic Variation,
pubmed-meshheading:8993351-Glycosylation,
pubmed-meshheading:8993351-Membrane Glycoproteins,
pubmed-meshheading:8993351-Molecular Sequence Data,
pubmed-meshheading:8993351-Molecular Weight,
pubmed-meshheading:8993351-Mutation,
pubmed-meshheading:8993351-Neisseria meningitidis,
pubmed-meshheading:8993351-Protein Processing, Post-Translational,
pubmed-meshheading:8993351-Spectrometry, Mass, Fast Atom Bombardment,
pubmed-meshheading:8993351-Trisaccharides,
pubmed-meshheading:8993351-UDPglucose 4-Epimerase,
pubmed-meshheading:8993351-Virulence
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pubmed:year |
1996
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pubmed:articleTitle |
Posttranslational modifications of meningococcal pili. Identification of a common trisaccharide substitution on variant pilins of strain C311.
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pubmed:affiliation |
Department of Peadiatrics, University of Oxford, John Radcliffe Hospital, UK. mumtaz.virji@paediatrics.oxford.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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