ArticleScientific reports2015
Structure and mechanism of a bacterial host-protein citrullinating virulence factor, Porphyromonas gingivalis peptidylarginine deiminase.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers, 1 of them a synthesis that pooled it.
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Who cites it
66 citing papers in PubMed, 1 synthesis or guideline pooled it, 97 citations in OpenAlex.
- Serum antibody levels against Porphyromonas gingivalis in patients with and without rheumatoid arthritis - a systematic review and meta-analysis.Clinical oral investigations · 2017Pooled it
- Article
- Autoantibodies and T Cells Target Citrullinated and Homocitrullinated Antigens in Rheumatoid Arthritis.Immunological reviews · 2026Review
- Peptidylarginine deiminase in Porphyromonas gingivalis-derived outer membrane vesicles exacerbates metabolic dysfunction-associated steatotic liver disease through the NPAS2/CYP4A10 pathway.Journal of nanobiotechnology · 2026Article
- Preclinical Rheumatoid Arthritis: Pathogenesis, Risk Stratification, and Therapeutic Interception.Journal of clinical medicine · 2026Review
- Pathogenesis ofFrontiers in cellular and infection microbiology · 2026Review
- Macrophage activation and invasion byJournal of oral microbiology · 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
- Biofilms and oral health: nanotechnology for biofilm control.Discover nano · 2025Review
- Citrullination in health and disease: From physiological function to gene regulation.Genes & diseases · 2025Review
- Polymorphic Variants of Peptidylarginine Deiminase Gene fromInternational journal of molecular sciences · 2025Article
- 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
- Oral Microbiome Dysbiosis and Citrullination in Rheumatoid Arthritis.Advances in experimental medicine and biology · 2025Review
- Oral Pathobiont-Derived Outer Membrane Vesicles in the Oral-Gut Axis.International journal of molecular sciences · 2024Review
- The peculiar features, diversity and impact of citrulline-reactive autoantibodies.Nature reviews. Rheumatology · 2024Review
- Structural and functional insights into the C-terminal signal domain of the Bacteroidetes type-IX secretion system.Open biology · 2024Article
- Crystal structure of human peptidylarginine deiminase type VI (PAD6) provides insights into its inactivity.IUCrJ · 2024Article
- Evolutionary analysis reveals the role of a non-catalytic domain of peptidyl arginine deiminase 2 in transcriptional regulation.iScience · 2024Article
- Identification of a new genetic variant (G231N, E232T, N235D) of peptidylarginine deiminase fromFrontiers in immunology · 2024Article
6 more citing papers are in PubMed but not listed here.
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Authors and funding
15 authors at 3 institutions in 3 countries.
Funding
Abstract
Citrullination is a post-translational modification of higher organisms that deiminates arginines in proteins and peptides. It occurs in physiological processes but also pathologies such as multiple sclerosis, fibrosis, Alzheimer's disease and rheumatoid arthritis (RA). The reaction is catalyzed by peptidylarginine deiminases (PADs), which are found in vertebrates but not in lower organisms. RA has been epidemiologically associated with periodontal disease, whose main infective agent is Porphyromonas gingivalis. Uniquely among microbes, P. gingivalis secretes a PAD, termed PPAD (Porphyromonas peptidylarginine deiminase), which is genetically unrelated to eukaryotic PADs. Here, we studied function of PPAD and its substrate-free, substrate-complex, and substrate-mimic-complex structures. It comprises a flat cylindrical catalytic domain with five-fold α/β-propeller architecture and a C-terminal immunoglobulin-like domain. The PPAD active site is a funnel located on one of the cylinder bases. It accommodates arginines from peptide substrates after major rearrangement of a "Michaelis loop" that closes the cleft. The guanidinium and carboxylate groups of substrates are tightly bound, which explains activity of PPAD against arginines at C-termini but not within peptides. Catalysis is based on a cysteine-histidine-asparagine triad, which is shared with human PAD1-PAD4 and other guanidino-group modifying enzymes. We provide a working mechanism hypothesis based on 18 structure-derived point mutants.
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