ArticleScientific reports2017
PorV is an Outer Membrane Shuttle Protein for the Type IX Secretion System.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 72 citations in OpenAlex.
- Differential proteomics of bacteria grownmSystems · 2026Article
- Structural and mechanistic basis of ubiquitous bacterial kinase signaling identifies PorX as a noncanonical substrate in Porphyromonas gingivalis.The Journal of biological chemistry · 2026Article
- A shared mechanism for Bacteroidota protein transport and gliding motility.Nature communications · 2025Article
- Specialized shuttle proteins recognize Type IX secretion signals and target effectors to their final destinations in Flavobacterium johnsoniae.Communications biology · 2025Article
- Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota.Nature microbiology · 2025Article
- Insights into type IX secretion from PorKN cogwheel structure bound to PorG and attachment complexes.Nature communications · 2025Article
- PorV factor of the type IX secretion system and PosF porin act as adhesins in Riemerella anatipestifer infection.Veterinary research · 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
- TheJournal of oral microbiology · 2025Article
- Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025Review
- Structural and functional insights into the C-terminal signal domain of the Bacteroidetes type-IX secretion system.Open biology · 2024Article
- Surface colonization bymBio · 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
- 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
- Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage.International journal of molecular sciences · 2022Article
- A unique bacterial secretion machinery with multiple secretion centers.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porphyromonas gingivalis is a keystone pathogen associated with chronic periodontitis. Major virulence factors named gingipains (cysteine proteinases, RgpA, RgpB and Kgp) are secreted via the Type IX Secretion System (T9SS). These, together with approximately 30 other proteins, are secreted to the cell surface and anchored to the outer membrane by covalent modification to anionic lipopolysaccharide (A-LPS) via the novel Gram negative sortase, PorU. PorU is localised on the cell surface and cleaves the C-terminal domain signal (CTD) of T9SS substrates and conjugates their new C-termini to A-LPS. A 440 kDa-attachment complex was identified in the wild-type (WT) comprising of PorU:PorV:PorQ:PorZ. In mutant strains, sub-complexes comprising PorU:PorV or PorQ:PorZ were also identified at smaller native sizes suggesting that PorU and PorZ are anchored to the cell surface via interaction with the PorV and PorQ outer membrane proteins, respectively. Analysis of porU mutants and a CTD cleavage mutant revealed accumulation of immature T9SS substrates in a PorV-bound form. Quantitative label-free proteomics of WT whole cell lysates estimated that the proportion of secretion channels:attachment complexes:free PorV:T9SS substrates was 1:6:110:2000 supporting a role for PorV as a shuttle protein delivering secreted proteins to the attachment complex for CTD signal cleavage and A-LPS modification.
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