Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

The importance of protein glycosylation in the interaction of pathogenic bacteria with their host is becoming increasingly clear. Neisseria meningitidis , the etiological agent of cerebrospinal meningitis, crosses cellular barriers after adhering to host cells through type IV pili. Pilin glycosylation genes ( pgl ) are responsible for the glycosylation of PilE, the major subunit of type IV pili, with the 2,4-diacetamido-2,4,6-trideoxyhexose residue. Nearly half of the clinical isolates, however, display an insertion in the pglBCD operon, which is anticipated to lead to a different, unidentified glycosylation. Here the structure of pilin glycosylation was determined in such a strain by “top-down” MS approaches. MALDI-TOF, nanoelectrospray ionization Fourier transform ion cyclotron resonance, and nanoelectrospray ionization quadrupole TOF MS analysis of purified pili preparations originating from N. meningitidis strains, either wild type or deficient for pilin glycosylation, revealed a glycan mass inconsistent with 2,4-diacetamido-2,4,6-trideoxyhexose or any sugar in the databases. This unusual modification was determined by in-source dissociation of the sugar from the protein followed by tandem MS analysis with collision-induced fragmentation to be a hexose modified with a glyceramido and an acetamido group. We further show genetically that the nature of the sugar present on the pilin is determined by the carboxyl-terminal region of the pglB gene modified by the insertion in the pglBCD locus. We thus report a previously undiscovered monosaccharide involved in posttranslational modification of type IV pilin subunits by a MS-based approach and determine the molecular basis of its biosynthesis.

Bibliography

Chamot-Rooke, J., Rousseau, B., Lanternier, F., Mikaty, G., Mairey, E., Malosse, C., Bouchoux, G., Pelicic, V., Camoin, L., Nassif, X., & Duménil, G. (2007). Alternative Neisseria spp. type IV pilin glycosylation with a glyceramido acetamido trideoxyhexose residue. Proceedings of the National Academy of Sciences, 104(37), 14783–14788.

Dates
Type When
Created 17 years, 11 months ago (Sept. 5, 2007, 9:39 p.m.)
Deposited 3 years, 4 months ago (April 12, 2022, 4:17 p.m.)
Indexed 3 months ago (May 27, 2025, 8:58 a.m.)
Issued 17 years, 11 months ago (Sept. 11, 2007)
Published 17 years, 11 months ago (Sept. 11, 2007)
Published Online 17 years, 11 months ago (Sept. 11, 2007)
Published Print 17 years, 11 months ago (Sept. 11, 2007)
Funders 0

None

@article{Chamot_Rooke_2007, title={Alternative Neisseria spp. type IV pilin glycosylation with a glyceramido acetamido trideoxyhexose residue}, volume={104}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0705335104}, DOI={10.1073/pnas.0705335104}, number={37}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Chamot-Rooke, Julia and Rousseau, Benoit and Lanternier, Fanny and Mikaty, Guillain and Mairey, Emilie and Malosse, Christian and Bouchoux, Guy and Pelicic, Vladimir and Camoin, Luc and Nassif, Xavier and Duménil, Guillaume}, year={2007}, month=sep, pages={14783–14788} }