ArticleProceedings of the National Academy of Sciences of the United States of America2011
Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 48 citations in OpenAlex.
- Review
- Cryo-EM structures of type IV pili complexed with nanobodies reveal immune escape mechanisms.Nature communications · 2024Article
- Sweet complexity:Frontiers in cellular and infection microbiology · 2024Review
- Genetic, Functional, and Immunogenic Analyses of theJournal of bacteriology · 2023Article
- Sculpting the BacterialmBio · 2022Article
- Allelic polymorphisms in a glycosyltransferase gene shape glycan repertoire in the O-linked protein glycosylation system of Neisseria.Glycobiology · 2021Article
- Neisseria meningitidis: using genomics to understand diversity, evolution and pathogenesis.Nature reviews. Microbiology · 2020Review
- Genetic determinants of genus-level glycan diversity in a bacterial protein glycosylation system.PLoS genetics · 2019Article
- Disrupted Synthesis of a Di-Journal of bacteriology · 2019Article
- Phase-Variable Genotypes Sweetened by Glycosylation Phenotypes.Journal of bacteriology · 2018Article
- Genotypic and Phenotypic Characterization of theJournal of bacteriology · 2018Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum.Glycobiology · 2016Article
- Characterization of a Unique Tetrasaccharide and Distinct Glycoproteome in the O-Linked Protein Glycosylation System of Neisseria elongata subsp. glycolytica.Journal of bacteriology · 2016Article
- Neisseria meningitidis Type IV Pili Composed of Sequence Invariable Pilins Are Masked by Multisite Glycosylation.PLoS pathogens · 2015Article
- Article
- The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014Review
- Diversity within the O-linked protein glycosylation systems of acinetobacter species.Molecular & cellular proteomics : MCP · 2014Article
- Targeted identification of glycosylated proteins in the gastric pathogen Helicobacter pylori (Hp).Molecular & cellular proteomics : MCP · 2013Article
- Allelic variation in a simple sequence repeat element of neisserial pglB2 and its consequences for protein expression and protein glycosylation.Journal of bacteriology · 2013Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
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Abstract
Although protein glycosylation systems are becoming widely recognized in bacteria, little is known about the mechanisms and evolutionary forces shaping glycan composition. Species within the genus Neisseria display remarkable glycoform variability associated with their O-linked protein glycosylation (pgl) systems and provide a well developed model system to study these phenomena. By examining the potential influence of two ORFs linked to the core pgl gene locus, we discovered that one of these, previously designated as pglH, encodes a glucosyltransferase that generates unique disaccharide products by using polyprenyl diphosphate-linked monosaccharide substrates. By defining the function of PglH in the glycosylation pathway, we identified a metabolic conflict related to competition for a shared substrate between the opposing glycosyltransferases PglA and PglH. Accordingly, we propose that the presence of a stereotypic, conserved deletion mutation inactivating pglH in strains of Neisseria gonorrhoeae, Neisseria meningitidis, and related commensals, reflects a resolution of this conflict with the consequence of reduced glycan diversity. This model of genetic détente is supported by the characterization of pglH "missense" alleles encoding proteins devoid of activity or reduced in activity such that they cannot exert their effect in the presence of PglA. Thus, glucose-containing glycans appear to be a trait undergoing regression at the genus level. Together, these findings document a role for intrinsic genetic interactions in shaping glycan evolution in protein glycosylation systems.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.