ArticleScientific reports2017
Active Components of Leptospira Outer Membrane Protein LipL32 to Toll-Like Receptor 2.
Article in Scientific reports, 2017. 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, 25 citations in OpenAlex.
- In Silico Approaches for the Identification of Aptamer Binding Interactions toTropical medicine and infectious disease · 2023Article
- Putative Pathogenic Genes ofTropical medicine and infectious disease · 2022Article
- Insight into the Structure, Functions, and Dynamics of theMembranes · 2022Review
- Host and Species-Specificities of Pattern Recognition Receptors Upon Infection WithFrontiers in cellular and infection microbiology · 2022Review
- Activation of Canine, Mouse and Human TLR2 and TLR4 by InactivatedFrontiers in immunology · 2022Article
- Alive Pathogenic and Saprophytic Leptospires Enter and Exit Human and Mouse Macrophages With No Intracellular Replication.Frontiers in cellular and infection microbiology · 2022Article
- Crosstalk between E-Cadherin/β-Catenin and NF-κB Signaling Pathways: The Regulation of Host-Pathogen Interaction during Leptospirosis.International journal of molecular sciences · 2021Article
- Peptidoglycan mediates Leptospira outer membrane protein Loa22 to toll-like receptor 2 for inflammatory interaction: a novel innate immune recognition.Scientific reports · 2021Article
- The Effect of Environmental Stresses onPolish journal of microbiology · 2020Article
- Leptospiral LPS escapes mouse TLR4 internalization and TRIF‑associated antimicrobial responses through O antigen and associated lipoproteins.PLoS pathogens · 2020Article
- S-Layer Protein ofFrontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins belonging to the toll-like receptor (TLR) family, particularly TLR2, are the major components of innate immunity against Leptospira infection. The ligands for TLR2 harbor several conserved patterns such as lipidation molecules, leucine-rich repeat (LRR) domains, TLR2 binding motifs, and TLR2 binding structure. In Leptospira, LipL32 interacts with TLR2 on human kidney cells concomitantly stimulating inflammatory responses. However, the binding mechanism of LipL32 to TLR2 is unknown. The computational prediction suggests that β1β2, loop-α3-loop, and α4 domains of LipL32 play vital roles in LipL32-TLR2 complex formation. To test these predictions, protein truncation experiments revealed that LipL32ΔNβ1β2 significantly decreased the affinity to TLR2 while LipL32ΔCα4 slightly reduced it. Interestingly, LipL32ΔCenα3 retained affinity to TLR2 in the absence of Ca
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