ArticleInfection and immunity2012
OmpL1 is an extracellular matrix- and plasminogen-interacting protein of Leptospira spp.
Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 97 citations in OpenAlex.
- Immune mechanisms underlying endothelial and placental dysfunction in leptospirosis during pregnancy.Frontiers in cellular and infection microbiology · 2026Review
- The role of leptospiral proteins in immune evasion and inflammatory response stimulation in HEK293T cell monolayers.Frontiers in immunology · 2025Article
- Characterisation of Putative Outer Membrane Proteins fromMicroorganisms · 2024Article
- Leucine-rich repeat proteins ofFrontiers in microbiology · 2024Article
- Leptospiral adhesins: from identification to future perspectives.Frontiers in microbiology · 2024Review
- Proteomic profile of naturally released extracellular vesicles secreted from Leptospira interrogans serovar Pomona in response to temperature and osmotic stresses.Scientific reports · 2023Article
- LIC12254 Is a Leptospiral Protein That Interacts with Integrins via the RGD Motif.Tropical medicine and infectious disease · 2023Article
- In Silico Approaches for the Identification of Aptamer Binding Interactions toTropical medicine and infectious disease · 2023Article
- Evaluation ofFrontiers in microbiology · 2023Article
- Host Cell Binding Mediated byInternational journal of molecular sciences · 2022Article
- A New Recombinant Multiepitope Chimeric Protein ofTropical medicine and infectious disease · 2022Article
- Subversion of the immune response of human pathogenic spirochetes.Journal of clinical laboratory analysis · 2022Review
- Characterization of a virulence-modifying protein ofFrontiers in microbiology · 2022Article
- The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components.Virulence · 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
- Heterologous Expression of the Pathogen-Specific LIC11711 Gene in the SaprophytePathogens (Basel, Switzerland) · 2020Article
- Putative β-Barrel Outer Membrane Proteins of the Bovine Digital Dermatitis-Associated Treponemes: Identification, Functional Characterization, and Immunogenicity.Infection and immunity · 2020Article
- Crawling Motility on the Host Tissue Surfaces Is Associated With the Pathogenicity of the Zoonotic SpirocheteFrontiers in microbiology · 2020Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leptospirosis is a zoonosis with multisystem involvement caused by pathogenic strains of the genus Leptospira. OmpL1 is an outer membrane protein of Leptospira spp. that is expressed during infection. In this work, we investigated novel features of this protein. We describe that OmpL1 is a novel leptospiral extracellular matrix (ECM)-binding protein and a plasminogen (PLG) receptor. The recombinant protein was expressed in Escherichia coli BL21(DE3) Star/pLysS as inclusion bodies, refolded, and purified by metal-chelating chromatography. The protein presented a typical β-strand secondary structure, as evaluated by circular dichroism spectroscopy. The recombinant protein reacted with antibodies in serum samples from convalescent leptospirosis patients with a high specificity compared to serum samples from individuals with unrelated diseases. These data strengthen the usefulness of OmpL1 as a diagnostic marker of leptospirosis. The characterization of the immunogenicity of recombinant OmpL1 in inoculated BALB/c mice showed that the protein has the capacity to elicit humoral and cellular immune responses, as denoted by high antibody titers and the proliferation of lymphocytes. We demonstrate that OmpL1 has the ability to mediate attachment to laminin and plasma fibronectin, with K(D) (equilibrium dissociation constant) values of 2,099.93 ± 871.03 nM and 1,239.23 ± 506.85 nM, respectively. OmpL1 is also a PLG receptor, with a K(D) of 368.63 ± 121.23 nM, capable of generating enzymatically active plasmin. This is the first report that shows and characterizes OmpL1 as an ECM-interacting and a PLG-binding protein of Leptospira spp. that may play a role in bacterial pathogenesis when expressed during infection.
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