ArticleJournal of bacteriology2006
The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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91 citing papers in PubMed.
- 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
- 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
- Ugd Is Involved in the Synthesis of Glycans of Glycoprotein and LPS and Is Important for Cellulose Degradation inMicroorganisms · 2025Article
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- Article
- Identification of nanaomycin A and its analogs by a newly established screening method for functional inhibitors of the type IX secretion system in Porphyromonas gingivalis.The Journal of antibiotics · 2025Article
- Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025Review
- First crystal structure of the DUF2436 domain of virulence proteins from Porphyromonas gingivalis.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Structural and functional insights into the C-terminal signal domain of the Bacteroidetes type-IX secretion system.Open biology · 2024Article
- Structural Modeling of T9SS Outer Membrane Proteins and Their Complexes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Production and properties of adhesin-free gingipain proteinase RgpA.Scientific reports · 2023Article
- 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
- Secreted peptidases contribute to virulence of fish pathogenFrontiers in cellular and infection microbiology · 2023Article
- Transposon mutagenesis and genome sequencing identify two novel, tandem genes involved in the colony spreading ofFrontiers in cellular and infection microbiology · 2023Article
- The type IX secretion system: Insights into its function and connection to glycosylation inEngineering microbiology · 2022Review
31 more citing papers are in PubMed but not listed here.
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7 authors.
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Abstract
Porphyromonas gingivalis produces outer membrane-attached proteins that include the virulence-associated proteinases RgpA and RgpB (Arg-gingipains) and Kgp (Lys-gingipain). We analyzed the P. gingivalis outer membrane proteome and identified numerous proteins with C-terminal domains similar in sequence to those of RgpB, RgpA, and Kgp, indicating that these domains may have a common function. Using RgpB as a model to investigate the role of the C-terminal domain, we expressed RgpB as a full-length zymogen (recombinant RgpB [rRgpB]), with a catalytic Cys244Ala mutation [rRgpB(C244A)], or with the C-terminal 72 amino acids deleted (rRgpB435) in an Arg-gingipain P. gingivalis mutant (YH522AB) and an Arg- and Lys-gingipain mutant (YH522KAB). rRgpB was catalytically active and located predominantly attached to the outer membrane of both background strains. rRgpB(C244A) was inactive and outer membrane attached, with a typical attachment profile for both background strains according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, but in YH522KAB, the prodomain was not removed. Thus, in vivo, RgpB export and membrane attachment are independent of the proteolytic activity of RgpA, RgpB, or Kgp. However, for maturation involving proteolytic processing of RgpB, the proteolytic activity of RgpB, RgpA, or Kgp is required. The C-terminally-truncated rRgpB435 was not attached to the outer membrane and was located as largely inactive, discrete 71-kDa and 48-kDa isoforms in the culture supernatant and the periplasm. These results suggest that the C-terminal domain is essential for outer membrane attachment and may be involved in a coordinated process of export and attachment to the cell surface.
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