ArticlePLoS pathogens2009
Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3.
Article in PLoS pathogens, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 65 papers, 1 of them a synthesis that pooled it.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
65 citing papers in PubMed, 1 synthesis or guideline pooled it, 117 citations in OpenAlex.
- A systematic review and critical appraisal of metagenomic and culture studies in hidradenitis suppurativa.Experimental dermatology · 2021Pooled it
- Trial
- Interspecies regulation of virulence through gingipain inhibition by a Tannerella forsythia serpin.EMBO reports · 2026Article
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- No serological association between Porphyromonas gingivalis or Prevotella intermedia and early spondyloarthritis: analysis from the DESIR cohort.Clinical and experimental medicine · 2026Article
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- Effects ofAnimals : an open access journal from MDPI · 2025Article
- Rumen metagenome reveals the mechanism of mitigation methane emissions by unsaturated fatty acid while maintaining the performance of dairy cows.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2024Article
- Ecological, beneficial, and pathogenic functions of the Type 9 Secretion System.Microbial biotechnology · 2024Review
- Antibiofilm activity ofBiofilm · 2024Article
- Functional and structural analyses reveal that a dual domain sialidase protects bacteria from complement killing through desialylation of complement factors.PLoS pathogens · 2023Article
- Designing Novel Multi-Epitope Vaccine Construct againstMedicina (Kaunas, Lithuania) · 2023Article
- Isolation, identification, and significance of salivaryFrontiers in cellular and infection microbiology · 2023Article
- Insertional Inactivation and Gene Complementation of Prevotella intermedia Type IX Secretion System Reveals Its Indispensable Roles in Black Pigmentation, Hemagglutination, Protease Activity of Interpain A, and Biofilm Formation.Journal of bacteriology · 2022Article
- Novel Insight into the Mechanisms of the Bidirectional Relationship between Diabetes and Periodontitis.Biomedicines · 2022Review
- Gut Microbes and Eye Disease.Ophthalmic research · 2022Review
- Understanding the Role ofAnimals : an open access journal from MDPI · 2021Article
- Polymicrobial communities in periodontal disease: Their quasi-organismal nature and dialogue with the host.Periodontology 2000 · 2021Review
- Potential Contributions of Anaerobes in Cystic Fibrosis Airways.Journal of clinical microbiology · 2021Review
- Effects of Essential Oils-Based Supplement andAnimals : an open access journal from MDPI · 2021Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
10 authors at 5 institutions in 5 countries.
Funding
Abstract
Periodontitis is an inflammatory disease of the supporting structures of the teeth caused by, among other pathogens, Prevotella intermedia. Many strains of P. intermedia are resistant to killing by the human complement system, which is present at up to 70% of serum concentration in gingival crevicular fluid. Incubation of human serum with recombinant cysteine protease of P. intermedia (interpain A) resulted in a drastic decrease in bactericidal activity of the serum. Furthermore, a clinical strain 59 expressing interpain A was more serum-resistant than another clinical strain 57, which did not express interpain A, as determined by Western blotting. Moreover, in the presence of the cysteine protease inhibitor E64, the killing of strain 59 by human serum was enhanced. Importantly, we found that the majority of P. intermedia strains isolated from chronic and aggressive periodontitis carry and express the interpain A gene. The protective effect of interpain A against serum bactericidal activity was found to be attributable to its ability to inhibit all three complement pathways through the efficient degradation of the alpha-chain of C3 -- the major complement factor common to all three pathways. P. intermedia has been known to co-aggregate with P. gingivalis, which produce gingipains to efficiently degrade complement factors. Here, interpain A was found to have a synergistic effect with gingipains on complement degradation. In addition, interpain A was able to activate the C1 complex in serum, causing deposition of C1q on inert and bacterial surfaces, which may be important at initial stages of infection when local inflammatory reaction may be beneficial for a pathogen. Taken together, the newly characterized interpain A proteinase appears to be an important virulence factor of P. intermedia.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.