ArticleProceedings of the National Academy of Sciences of the United States of America2009
Broad spectrum O-linked protein glycosylation in the human pathogen Neisseria gonorrhoeae.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.
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Who cites it
92 citing papers in PubMed, 151 citations in OpenAlex.
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- Sweet complexity:Frontiers in cellular and infection microbiology · 2024Review
- Insights into the recognition of hypermucoviscousFrontiers in immunology · 2024Article
- Genetic, Functional, and Immunogenic Analyses of theJournal of bacteriology · 2023Article
- Discovery and characterization of a new class of O-linking oligosaccharyltransferases from the Moraxellaceae family.Glycobiology · 2023Article
- Clinical Value of Glycan Changes in Cerebrospinal Fluid for Evaluation of Post-Neurosurgical Bacterial Meningitis with Hemorrhagic Stroke Patients.Diagnostics (Basel, Switzerland) · 2023Article
- Glycosylation of bacterial antigens changes epitope patterns.Frontiers in immunology · 2023Article
- Complete genome sequence and comparative analysis of aFrontiers in microbiology · 2023Article
- Genomic and phenotypic comparison ofVirulence · 2022Article
- Sculpting the BacterialmBio · 2022Article
- Phosphonate production by marine microbes: Exploring new sources and potential function.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Update on theFrontiers in cellular and infection microbiology · 2022Review
- A minimal sequon sufficient for O-linked glycosylation by the versatile oligosaccharyltransferase PglS.Glycobiology · 2021Article
- Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus.Communications biology · 2021Article
- Allelic polymorphisms in a glycosyltransferase gene shape glycan repertoire in the O-linked protein glycosylation system of Neisseria.Glycobiology · 2021Article
- Linking inherent O-Linked Protein Glycosylation of YghJ to Increased Antigen Potential.Frontiers in cellular and infection microbiology · 2021Article
- Bacterial Glycoengineering as a Biosynthetic Route to Customized Glycomolecules.Advances in biochemical engineering/biotechnology · 2021Article
32 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein glycosylation is an important element of biologic systems because of its significant effects on protein properties and functions. Although prominent within all domains of life, O-linked glycosylation systems modifying serine and threonine residues within bacteria and eukaryotes differ substantially in target protein selectivity. In particular, well-characterized bacterial systems have been invariably dedicated to modification of individual proteins or related subsets thereof. Here we characterize a general O-linked glycosylation system that targets structurally and functionally diverse groups of membrane-associated proteins in the gram-negative bacterium Neisseria gonorrhoeae, the etiologic agent of the human disease gonorrhea. The 11 glycoproteins identified here are implicated in activities as varied as protein folding, disulfide bond formation, and solute uptake, as well as both aerobic and anaerobic respiration. Along with their common trafficking within the periplasmic compartment, the protein substrates share quasi-related domains bearing signatures of low complexity that were demonstrated to encompass sites of glycan occupancy. Thus, as in eukaryotes, the broad scope of this system is dictated by the relaxed specificity of the glycan transferase as well as the bulk properties and context of the protein-targeting signal rather than by a strict amino acid consensus sequence. Together, these findings reveal previously unrecognized commonalities linking O-linked protein glycosylation in distantly related life forms.
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