ArticlePLoS pathogens2015
Porphyromonas gingivalis Type IX Secretion Substrates Are Cleaved and Modified by a Sortase-Like Mechanism.
Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 110 citations in OpenAlex.
- A novel LPS-dependent outer membrane-anchoring mechanism for T9SS substrates enables engineered enzyme display and whole-cell PET degradation inSynthetic and systems biotechnology · 2026Article
- Cargo Secreted by the Type IX Secretion System of Porphyromonas gingivalis Are Tethered to O-Lipopolysaccharides via a Pentasaccharide Linker.MicrobiologyOpen · 2026Article
- Specialized shuttle proteins recognize Type IX secretion signals and target effectors to their final destinations in Flavobacterium johnsoniae.Communications biology · 2025Article
- Tyrosine phosphorylation coupling of one-carbon metabolism and virulence in an endogenous pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Insights into type IX secretion from PorKN cogwheel structure bound to PorG and attachment complexes.Nature communications · 2025Article
- PorA of the Type IX Secretion Is a Ligand of the PorXY Two-Component Regulatory System in Porphyromonas gingivalis.Molecular microbiology · 2025Article
- C-terminal glycosylation of type IX secretion system cargo proteins inOpen biology · 2025Article
- Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025Review
- TheJournal of oral microbiology · 2025Article
- Ecological, beneficial, and pathogenic functions of the Type 9 Secretion System.Microbial biotechnology · 2024Review
- Structural and functional insights into the C-terminal signal domain of the Bacteroidetes type-IX secretion system.Open biology · 2024Article
- Gliding motility proteins GldJ and SprB contribute toJournal of bacteriology · 2024Article
- Ultrastructural and glycoproteomic characterization of Prevotella intermedia: Insights into O-glycosylation and outer membrane vesicles.MicrobiologyOpen · 2024Article
- Structural insights into the mechanism of protein transport by the Type 9 Secretion System translocon.Nature microbiology · 2024Article
- A pleiotropic role of sialidase in the pathogenicity ofInfection and immunity · 2024Article
- Structural Modeling of T9SS Outer Membrane Proteins and Their Complexes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Characterization of theJournal of bacteriology · 2023Article
- A journey with type IX secretion system effectors: selection, transport, processing and activities.Microbiology (Reading, England) · 2023Article
- Bacterial secretion system functions: evidence of interactions and downstream implications.Microbiology (Reading, England) · 2023Article
11 more citing papers are in PubMed but not listed here.
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9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type IX secretion system (T9SS) of Porphyromonas gingivalis secretes proteins possessing a conserved C-terminal domain (CTD) to the cell surface. The C-terminal signal is essential for these proteins to translocate across the outer membrane via the T9SS. On the surface the CTD of these proteins is cleaved prior to extensive glycosylation. It is believed that the modification on these CTD proteins is anionic lipopolysaccharide (A-LPS), which enables the attachment of CTD proteins to the cell surface. However, the exact site of modification and the mechanism of attachment of CTD proteins to the cell surface are unknown. In this study we characterized two wbaP (PG1964) mutants that did not synthesise A-LPS and accumulated CTD proteins in the clarified culture fluid (CCF). The CTDs of the CTD proteins in the CCF were cleaved suggesting normal secretion, however, the CTD proteins were not glycosylated. Mass spectrometric analysis of CTD proteins purified from the CCF of the wbaP mutants revealed the presence of various peptide/amino acid modifications from the growth medium at the C-terminus of the mature CTD proteins. This suggested that modification occurs at the C-terminus of T9SS substrates in the wild type P. gingivalis. This was confirmed by analysis of CTD proteins from wild type, where a 648 Da linker was identified to be attached at the C-terminus of mature CTD proteins. Importantly, treatment with proteinase K released the 648 Da linker from the CTD proteins demonstrating a peptide bond between the C-terminus and the modification. Together, this is suggestive of a mechanism similar to sortase A for the cleavage and modification/attachment of CTD proteins in P. gingivalis. PG0026 has been recognized as the CTD signal peptidase and is now proposed to be the sortase-like protein in P. gingivalis. To our knowledge, this is the first biochemical evidence suggesting a sortase-like mechanism in Gram-negative bacteria.
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