Abstract
Pili, which are filamentous protein structures on the surface of the meningitis-causing organism Neisseria meningitidis, are known to be post-translationally modified with substituents that affect their mobility in SDS/PAGE and which might play a crucial role in adherence and bloodstream invasion. Tryptic digests of pili were analysed by fast atom bombardment and electrospray MS to identify putative modifications. Serine-93 was found to carry a novel modification of alpha-glycerophosphate. This is the first time that alpha-glycerophosphate has been observed as a substituent of a prokaryotic or eukaryotic protein.
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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Bacterial Outer Membrane Proteins / chemistry*
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Bacterial Outer Membrane Proteins / isolation & purification
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Chromatography, High Pressure Liquid
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Electrophoresis, Polyacrylamide Gel
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Fimbriae Proteins
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Glycerophosphates / analysis*
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Humans
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Mass Spectrometry
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Molecular Sequence Data
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Neisseria meningitidis / chemistry
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Neisseria meningitidis / pathogenicity*
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Pancreatic Elastase
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification
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Pili, Sex / chemistry
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Spectrometry, Mass, Fast Atom Bombardment
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Trypsin
Substances
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Bacterial Outer Membrane Proteins
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Glycerophosphates
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Peptide Fragments
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Fimbriae Proteins
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alpha-glycerophosphoric acid
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Pancreatic Elastase
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Trypsin