ArticleScientific reports2016
Structural and functional probing of PorZ, an essential bacterial surface component of the type-IX secretion system of human oral-microbiomic Porphyromonas gingivalis.
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 56 papers.
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Who cites it
56 citing papers in PubMed.
- Interspecies regulation of virulence through gingipain inhibition by a Tannerella forsythia serpin.EMBO reports · 2026Article
- The Role ofAntibiotics (Basel, Switzerland) · 2026Review
- Structural and mechanistic basis of ubiquitous bacterial kinase signaling identifies PorX as a noncanonical substrate in Porphyromonas gingivalis.The Journal of biological chemistry · 2026Article
- Virulence diversity amongJournal of oral microbiology · 2026Review
- Periodontopathogens degrade angiotensin I from the human renin-angiotensin system through surface-attached proteases.Scientific reports · 2025Article
- 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
- PorA of the Type IX Secretion Is a Ligand of the PorXY Two-Component Regulatory System in Porphyromonas gingivalis.Molecular microbiology · 2025Article
- Structural studies of ribosome from an anaerobic Bacteroidetes human pathogen Porphyromonas gingivalis.Nucleic acids research · 2025Article
- C-terminal glycosylation of type IX secretion system cargo proteins inOpen biology · 2025Article
- TheJournal of oral microbiology · 2025Article
- Potential roles and mechanisms of bacterial peptidylarginine deiminase in dental biofilm mediated byJournal of oral microbiology · 2025Review
- Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025Review
- Unveiling the molecular mechanisms of the type IX secretion system's response regulator: Structural and functional insights.PNAS nexus · 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
- Structural Modeling of T9SS Outer Membrane Proteins and Their Complexes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A journey with type IX secretion system effectors: selection, transport, processing and activities.Microbiology (Reading, England) · 2023Article
- Protein interactome mapping of Porphyromonas gingivalis provides insights into the formation of the PorQ-Z complex of the type IX secretion system.Molecular oral microbiology · 2023Article
- A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogenChemical science · 2023Article
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23 authors.
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Abstract
Porphyromonas gingivalis is a member of the human oral microbiome abundant in dysbiosis and implicated in the pathogenesis of periodontal (gum) disease. It employs a newly described type-IX secretion system (T9SS) for secretion of virulence factors. Cargo proteins destined for secretion through T9SS carry a recognition signal in the conserved C-terminal domain (CTD), which is removed by sortase PorU during translocation. Here, we identified a novel component of T9SS, PorZ, which is essential for surface exposure of PorU and posttranslational modification of T9SS cargo proteins. These include maturation of enzyme precursors, CTD removal and attachment of anionic lipopolysaccharide for anchorage in the outer membrane. The crystal structure of PorZ revealed two β-propeller domains and a C-terminal β-sandwich domain, which conforms to the canonical CTD architecture. We further documented that PorZ is itself transported to the cell surface via T9SS as a full-length protein with its CTD intact, independently of the presence or activity of PorU. Taken together, our results shed light on the architecture and possible function of a novel component of the T9SS. Knowledge of how T9SS operates will contribute to our understanding of protein secretion as part of host-microbiome interactions by dysbiotic members of the human oral cavity.
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