ArticleVirulence2017
A novel intrinsically disordered outer membrane lipoprotein of Aggregatibacter actinomycetemcomitans binds various cytokines and plays a role in biofilm response to interleukin-1β and interleukin-8.
Article in Virulence, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Microbial adaptive pathogenicity strategies to the host inflammatory environment.FEMS microbiology reviews · 2025Review
- Virulence Factors of the Periodontal Pathogens: Tools to Evade the Host Immune Response and Promote Carcinogenesis.Microorganisms · 2023Review
- Aggregatibacter actinomycetemcomitans: From Basic to Advanced Research.Advances in experimental medicine and biology · 2022Article
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- The Hunger Games:Frontiers in immunology · 2021Article
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- Dispersion from CJournal of biomolecular NMR · 2020Article
- Virulence and Pathogenicity Properties ofPathogens (Basel, Switzerland) · 2019Review
- Commensal and pathogenic biofilms differently modulate peri-implant oral mucosa in an organotypic model.Cellular microbiology · 2019Article
- Tools ofJournal of clinical medicine · 2019Review
- Article
- Role of OmpA1 and OmpA2 inJournal of oral microbiology · 2019Article
- Article
- Functional and structural characteristics of bacterial proteins that bind host cytokines.Virulence · 2017Review
- Virulence factors associated with Aggregatibacter actinomycetemcomitans and their role in promoting periodontal diseases.Virulence · 2017Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered proteins (IDPs) do not have a well-defined and stable 3-dimensional fold. Some IDPs can function as either transient or permanent binders of other proteins and may interact with an array of ligands by adopting different conformations. A novel outer membrane lipoprotein, bacterial interleukin receptor I (BilRI) of the opportunistic oral pathogen Aggregatibacter actinomycetemcomitans binds a key gatekeeper proinflammatory cytokine interleukin (IL)-1β. Because the amino acid sequence of the novel lipoprotein resembles that of fibrinogen binder A of Haemophilus ducreyi, BilRI could have the potential to bind other proteins, such as host matrix proteins. However, from the tested host matrix proteins, BilRI interacted with neither collagen nor fibrinogen. Instead, the recombinant non-lipidated BilRI, which was intrinsically disordered, bound various pro/anti-inflammatory cytokines, such as IL-8, tumor necrosis factor (TNF)-α, interferon (IFN)-γ and IL-10. Moreover, BilRI played a role in the in vitro sensing of IL-1β and IL-8 because low concentrations of cytokines did not decrease the amount of extracellular DNA in the matrix of bilRI
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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.