ArticleBMC microbiology2012
Features of two proteins of Leptospira interrogans with potential role in host-pathogen interactions.
Article in BMC microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed, 88 citations in OpenAlex.
- Functional Validation of the Proteome-Identified LIC_13056 Putative Lipoprotein ofInternational journal of molecular sciences · 2026Article
- Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs.Scientific reports · 2024Article
- Leptospiral adhesins: from identification to future perspectives.Frontiers in microbiology · 2024Review
- Improvement the expression and purification of Loa22: a lipoprotein with OmpA domain from pathogenicIranian journal of microbiology · 2023Article
- Weil's Disease-Immunopathogenesis, Multiple Organ Failure, and Potential Role of Gut Microbiota.Biomolecules · 2022Review
- Subversion of the immune response of human pathogenic spirochetes.Journal of clinical laboratory analysis · 2022Review
- The oxidative stress response of pathogenic Leptospira is controlled by two peroxide stress regulators which putatively cooperate in controlling virulence.PLoS pathogens · 2021Article
- Leptospiral Infection, Pathogenesis and Its Diagnosis-A Review.Pathogens (Basel, Switzerland) · 2021Review
- A Review on Host-Frontiers in cellular and infection microbiology · 2021Review
- A NovelFrontiers in cellular and infection microbiology · 2021Article
- The interaction of two novel putative proteins ofVirulence · 2019Article
- Role of Supramolecule ErpY-Like Lipoprotein ofInfection and immunity · 2019Article
- Vaccine potential of LenA and LcpA proteins ofIranian journal of microbiology · 2019Article
- Catecholamine-Modulated Novel Surface-Exposed Adhesin LIC20035 of Leptospira spp. Binds Host Extracellular Matrix Components and Is Recognized by the Host during Infection.Applied and environmental microbiology · 2018Article
- PathogenicOpen veterinary journal · 2018Review
- Pathogenic Leptospires Modulate Protein Expression and Post-translational Modifications in Response to Mammalian Host Signals.Frontiers in cellular and infection microbiology · 2017Article
- What Makes a Bacterial Species Pathogenic?:Comparative Genomic Analysis of the Genus Leptospira.PLoS neglected tropical diseases · 2016Article
- Complement Evasion by PathogenicFrontiers in immunology · 2016Review
- Evaluation of cell binding activities of Leptospira ECM adhesins.PLoS neglected tropical diseases · 2015Article
- Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding protein.BMC microbiology · 2015Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLeptospirosis is considered a re-emerging infectious disease caused by pathogenic spirochaetes of the genus Leptospira. Pathogenic leptospires have the ability to survive and disseminate to multiple organs after penetrating the host. Leptospires were shown to express surface proteins that interact with the extracellular matrix (ECM) and to plasminogen (PLG). This study examined the interaction of two putative leptospiral proteins with laminin, collagen Type I, collagen Type IV, cellular fibronectin, plasma fibronectin, PLG, factor H and C4bp.
resultsWe show that two leptospiral proteins encoded by LIC11834 and LIC12253 genes interact with laminin in a dose - dependent and saturable mode, with dissociation equilibrium constants (KD) of 367.5 and 415.4 nM, respectively. These proteins were named Lsa33 and Lsa25 (Leptospiral surface adhesin) for LIC11834 and LIC12253, respectively. Metaperiodate - treated laminin reduced Lsa25 - laminin interaction, suggesting that sugar moieties of this ligand participate in this interaction. The Lsa33 is also PLG - binding receptor, with a KD of 23.53 nM, capable of generating plasmin in the presence of an activator. Although in a weak manner, both proteins interact with C4bp, a regulator of complement classical route. In silico analysis together with proteinase K and immunoflorescence data suggest that these proteins might be surface exposed. Moreover, the recombinant proteins partially inhibited leptospiral adherence to immobilized laminin and PLG.
conclusionsWe believe that these multifunctional proteins have the potential to participate in the interaction of leptospires to hosts by mediating adhesion and by helping the bacteria to escape the immune system and to overcome tissue barriers. To our knowledge, Lsa33 is the first leptospiral protein described to date with the capability of binding laminin, PLG and C4bp in vitro.
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