ArticleScientific reports2016
The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 69 citations in OpenAlex.
- Assembly, architecture and functional roles of microbial surface layers.Nature reviews. Microbiology · 2026Review
- Crystal structure of endo-β-N-acetylglucosaminidase HSα.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Pleiotropic effects of signal peptide peptidase A (Frontiers in veterinary science · 2026Article
- Specialized shuttle proteins recognize Type IX secretion signals and target effectors to their final destinations in Flavobacterium johnsoniae.Communications biology · 2025Article
- The Role ofCancers · 2025Review
- PorA of the Type IX Secretion Is a Ligand of the PorXY Two-Component Regulatory System in Porphyromonas gingivalis.Molecular microbiology · 2025Article
- Functional study of Bergeyella cardium KP-43 subfamily peptidases as putative T9SS cargo.Communications biology · 2025Article
- C-terminal glycosylation of type IX secretion system cargo proteins inOpen biology · 2025Article
- Dissecting Cytophagalysin: Structural and Biochemical Studies of a Bacterial Pappalysin-Family Metallopeptidase.Biomolecules · 2024Article
- Structural and functional insights into the C-terminal signal domain of the Bacteroidetes type-IX secretion system.Open biology · 2024Article
- Structural insights into the mechanism of protein transport by the Type 9 Secretion System translocon.Nature microbiology · 2024Article
- Article
- Bacterial surface-exposed lipoproteins and sortase-mediated anchored cell surface proteins in plant infection.MicrobiologyOpen · 2023Review
- Article
- A journey with type IX secretion system effectors: selection, transport, processing and activities.Microbiology (Reading, England) · 2023Article
- A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogenChemical science · 2023Article
- Riemerella anatipestifer AS87_RS02955 Acts as a Virulence Factor and Displays Endonuclease Activity.Applied and environmental microbiology · 2022Article
- The type IX secretion system: Insights into its function and connection to glycosylation inEngineering microbiology · 2022Review
- Genome-Wide Analysis and Characterization of the Riemerella anatipestifer Putative T9SS Secretory Proteins with a Conserved C-Terminal Domain.Journal of bacteriology · 2022Article
- Riemerella anatipestifer T9SS Effector SspA Functions in Bacterial Virulence and Defending Natural Host Immunity.Applied and environmental microbiology · 2022Article
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Authors and funding
19 authors at 7 institutions in 5 countries.
Funding
Abstract
In the recently characterized Type IX Secretion System (T9SS), the conserved C-terminal domain (CTD) in secreted proteins functions as an outer membrane translocation signal for export of virulence factors to the cell surface in the Gram-negative Bacteroidetes phylum. In the periodontal pathogen Porphyromonas gingivalis, the CTD is cleaved off by PorU sortase in a sequence-independent manner, and anionic lipopolysaccharide (A-LPS) is attached to many translocated proteins, thus anchoring them to the bacterial surface. Here, we solved the atomic structure of the CTD of gingipain B (RgpB) from P. gingivalis, alone and together with a preceding immunoglobulin-superfamily domain (IgSF). The CTD was found to possess a typical Ig-like fold encompassing seven antiparallel β-strands organized in two β-sheets, packed into a β-sandwich structure that can spontaneously dimerise through C-terminal strand swapping. Small angle X-ray scattering (SAXS) revealed no fixed orientation of the CTD with respect to the IgSF. By introducing insertion or substitution of residues within the inter-domain linker in the native protein, we were able to show that despite the region being unstructured, it nevertheless is resistant to general proteolysis. These data suggest structural motifs located in the two adjacent Ig-like domains dictate the processing of CTDs by the T9SS secretion pathway.
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