ArticleBiochemical and biophysical research communications2012
Identification of a unique TLR2-interacting peptide motif in a microbial leucine-rich repeat protein.
Article in Biochemical and biophysical research communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- The intriguing strategies ofFrontiers in oral health · 2024Article
- Unusual structural and functional features of TpLRR/BspA-like LRR proteins.Journal of structural biology · 2023Review
- BacSp222 bacteriocin as a novel ligand for TLR2/TLR6 heterodimer.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2023Article
- Article
- Peptidoglycan mediates Leptospira outer membrane protein Loa22 to toll-like receptor 2 for inflammatory interaction: a novel innate immune recognition.Scientific reports · 2021Article
- S-Layer Protein ofFrontiers in microbiology · 2019Article
- Exposure to wild-type AAV drives distinct capsid immunity profiles in humans.The Journal of clinical investigation · 2018Article
- Active Components of Leptospira Outer Membrane Protein LipL32 to Toll-Like Receptor 2.Scientific reports · 2017Article
- Early Secretory Antigenic Target-6 Drives Matrix Metalloproteinase-10 Gene Expression and Secretion in Tuberculosis.American journal of respiratory cell and molecular biology · 2017Article
- An emerging mycoplasma associated with trichomoniasis, vaginal infection and disease.PloS one · 2014Article
- Protein-linked glycans in periodontal bacteria: prevalence and role at the immune interface.Frontiers in microbiology · 2013Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
Abstract
Pathogenesis of many bacterially-induced inflammatory diseases is driven by Toll-like receptor (TLR) mediated immune responses following recognition of bacterial factors by different TLRs. Periodontitis is a chronic inflammation of the tooth supporting apparatus often leading to tooth loss, and is caused by a Gram-negative bacterial consortium that includes Tannerella forsythia. This bacterium expresses a virulence factor, the BspA, which drives periodontal inflammation by activating TLR2. The N-terminal portion of the BspA protein comprises a leucine-rich repeat (LRR) domain previously shown to be involved in the binding and activation of TLR2. The objective of the current study was to identify specific epitopes in the LRR domain of BspA that interact with TLR2. Our results demonstrate that a sequence motif GC(S/T)GLXSIT is involved in mediating the interaction of BspA with TLR2. Thus, our study has identified a peptide motif that mediates the binding of a bacterial protein to TLR2 and highlights the promiscuous nature of TLR2 with respect to ligand binding. This work could provide a structural basis for designing peptidomimetics to modulate the activity of TLR2 in order to block bacterially-induced inflammation.
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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.