ArticleThe Journal of biological chemistry2014
Crystal structures of the Toll/Interleukin-1 receptor (TIR) domains from the Brucella protein TcpB and host adaptor TIRAP reveal mechanisms of molecular mimicry.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 74 citations in OpenAlex.
- Review
- Complementary Use of Probiotics and Their Antimicrobial Proteins in Brucellosis: A Comprehensive Review of Mechanisms and Clinical Benefits.Probiotics and antimicrobial proteins · 2026Review
- TIR-domain-containing protein C as modulator of innate immune checkpoints.Scientific reports · 2025Article
- Review
- Structure-guided insights into TIR-mediated bacterial and eukaryotic immunity.Structure (London, England : 1993) · 2025Review
- ThemicroLife · 2025Review
- o-Vanillin binds covalently to MAL/TIRAP Lys-210 but independently inhibits TLR2.Journal of enzyme inhibition and medicinal chemistry · 2024Article
- Review
- Characterization of the Structural Requirements for the NADase Activity of Bacterial Toll/IL-1R domains in a Course-based Undergraduate Research Experience.ImmunoHorizons · 2024Article
- Review
- Cyclic ADP ribose isomers: Production, chemical structures, and immune signaling.Science (New York, N.Y.) · 2022Article
- Article
- Human and Bacterial Toll-Interleukin Receptor Domains Exhibit Distinct Dynamic Features and Functions.Molecules (Basel, Switzerland) · 2022Article
- Assessment of Association between miR-146a Polymorphisms and Expression of miR-146a, TRAF-6, and IRAK-1 Genes in Patients with Brucellosis.Molecular biology reports · 2022Article
- Activation of mucosal immunity as a novel therapeutic strategy for combating brucellosis.Frontiers in microbiology · 2022Review
- Using a Relative Quantitative Proteomic Method to Identify Differentially Abundant Proteins inFrontiers in immunology · 2022Article
- microRNAs in human brucellosis: A promising therapeutic approach and biomarker for diagnosis and treatment.Immunity, inflammation and disease · 2021Review
- Undercover Agents of Infection: The Stealth Strategies of T4SS-Equipped Bacterial Pathogens.Toxins · 2021Review
- Tauroursodeoxycholic acid prevents Burkholderia pseudomallei-induced endoplasmic reticulum stress and is protective during melioidosis in mice.BMC microbiology · 2021Article
- Regulation of Expression of thePathogens (Basel, Switzerland) · 2021Article
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Authors and funding
16 authors at 5 institutions in 2 countries.
Funding
Abstract
The Toll/IL-1 receptor (TIR) domains are crucial innate immune signaling modules. Microbial TIR domain-containing proteins inhibit Toll-like receptor (TLR) signaling through molecular mimicry. The TIR domain-containing protein TcpB from Brucella inhibits TLR signaling through interaction with host adaptor proteins TIRAP/Mal and MyD88. To characterize the microbial mimicry of host proteins, we have determined the X-ray crystal structures of the TIR domains from the Brucella protein TcpB and the host adaptor protein TIRAP. We have further characterized homotypic interactions of TcpB using hydrogen/deuterium exchange mass spectrometry and heterotypic TcpB and TIRAP interaction by co-immunoprecipitation and NF-κB reporter assays. The crystal structure of the TcpB TIR domain reveals the microtubule-binding site encompassing the BB loop as well as a symmetrical dimer mediated by the DD and EE loops. This dimerization interface is validated by peptide mapping through hydrogen/deuterium exchange mass spectrometry. The human TIRAP TIR domain crystal structure reveals a unique N-terminal TIR domain fold containing a disulfide bond formed by Cys(89) and Cys(134). A comparison between the TcpB and TIRAP crystal structures reveals substantial conformational differences in the region that encompasses the BB loop. These findings underscore the similarities and differences in the molecular features found in the microbial and host TIR domains, which suggests mechanisms of bacterial mimicry of host signaling adaptor proteins, such as TIRAP.
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