ArticlePLoS neglected tropical diseases2010
The OmpL37 surface-exposed protein is expressed by pathogenic Leptospira during infection and binds skin and vascular elastin.
Article in PLoS neglected tropical diseases, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.
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Who cites it
40 citing papers in PubMed, 1 synthesis or guideline pooled it, 88 citations in OpenAlex.
- Trends and advances inFrontiers in microbiology · 2024Pooled it
- In vitro and in vivo endothelial interactions of Leptospira species are markers of virulence.PLoS neglected tropical diseases · 2026Article
- Leptospirosis.Nature reviews. Disease primers · 2025Review
- Evaluation of binding activities of a putative lipoprotein LIC_13355 of Leptospira spp.FEBS open bio · 2025Article
- The role of leptospiral proteins in immune evasion and inflammatory response stimulation in HEK293T cell monolayers.Frontiers in immunology · 2025Article
- Cleavage of cell junction proteins as a host invasion strategy in leptospirosis.Applied microbiology and biotechnology · 2024Review
- Characterisation of Putative Outer Membrane Proteins fromMicroorganisms · 2024Article
- Leptospiral adhesins: from identification to future perspectives.Frontiers in microbiology · 2024Review
- Seroprevalence and associated risk factors of leptospirosis in bovine dairy farms in Telangana state, India.Tropical animal health and production · 2023Article
- Role of elastic fiber degradation in disease pathogenesis.Biochimica et biophysica acta. Molecular basis of disease · 2023Review
- LIC12254 Is a Leptospiral Protein That Interacts with Integrins via the RGD Motif.Tropical medicine and infectious disease · 2023Article
- Evaluation ofFrontiers in microbiology · 2023Article
- Host Cell Binding Mediated byInternational journal of molecular sciences · 2022Article
- The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components.Virulence · 2021Article
- Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona.PLoS neglected tropical diseases · 2021Article
- Leptospiral Infection, Pathogenesis and Its Diagnosis-A Review.Pathogens (Basel, Switzerland) · 2021Review
- A Review on Host-Frontiers in cellular and infection microbiology · 2021Review
- Revisiting the Development of Vaccines Against PathogenicFrontiers in immunology · 2021Review
- Putative β-Barrel Outer Membrane Proteins of the Bovine Digital Dermatitis-Associated Treponemes: Identification, Functional Characterization, and Immunogenicity.Infection and immunity · 2020Article
- Role of Supramolecule ErpY-Like Lipoprotein ofInfection and immunity · 2019Article
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3 authors at 2 institutions in 1 country.
Funding
Abstract
Pathogenic Leptospira spp. shed in the urine of reservoir hosts into freshwater can be transmitted to a susceptible host through skin abrasions or mucous membranes causing leptospirosis. The infection process involves the ability of leptospires to adhere to cell surface and extracellular matrix components, a crucial step for dissemination and colonization of host tissues. Therefore, the elucidation of novel mediators of host-pathogen interaction is important in the discovery of virulence factors involved in the pathogenesis of leptospirosis. In this study, we assess the functional roles of transmembrane outer membrane proteins OmpL36 (LIC13166), OmpL37 (LIC12263), and OmpL47 (LIC13050), which we recently identified on the leptospiral surface. We determine the capacity of these proteins to bind to host tissue components by enzyme-linked immunosorbent assay. OmpL37 binds elastin preferentially, exhibiting dose-dependent, saturating binding to human skin (K(d), 104±19 nM) and aortic elastin (K(d), 152±27 nM). It also binds fibrinogen (K(d), 244±15 nM), fibrinogen fragment D (K(d), 132±30 nM), plasma fibronectin (K(d), 359±68 nM), and murine laminin (K(d), 410±81 nM). The binding to human skin elastin by both recombinant OmpL37 and live Leptospira interrogans is specifically enhanced by rabbit antiserum for OmpL37, suggesting the involvement of OmpL37 in leptospiral binding to elastin and also the possibility that host-generated antibodies may promote rather than inhibit the adherence of leptospires to elastin-rich tissues. Further, we demonstrate that OmpL37 is recognized by acute and convalescent leptospirosis patient sera and also by Leptospira-infected hamster sera. Finally, OmpL37 protein is detected in pathogenic Leptospira serovars and not in saprophytic Leptospira. Thus, OmpL37 is a novel elastin-binding protein of pathogenic Leptospira that may be promoting attachment of Leptospira to host tissues.
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