ArticleInfection and immunity2009
Plasminogen acquisition and activation at the surface of leptospira species lead to fibronectin degradation.
Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
41 citing papers in PubMed, 94 citations in OpenAlex.
- Functional Validation of the Proteome-Identified LIC_13056 Putative Lipoprotein ofInternational journal of molecular sciences · 2026Article
- The grand escape - how pathogens outsmart the human complement system.Immunobiology · 2025Review
- Revisiting Host-Binding Properties of LigA and LigB Recombinant Domains.Microorganisms · 2025Article
- 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
- Leucine-rich repeat proteins ofFrontiers in microbiology · 2024Article
- MPL36, a major plasminogen (PLG) receptor in pathogenic Leptospira, has an essential role during infection.PLoS pathogens · 2023Article
- Evaluation ofFrontiers in microbiology · 2023Article
- The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components.Virulence · 2021Article
- In Vitro Study of the Fibrinolytic Activity via Single Chain Urokinase-Type Plasminogen Activator and Molecular Docking of FGFC1.Molecules (Basel, Switzerland) · 2021Article
- Leptospiral Infection, Pathogenesis and Its Diagnosis-A Review.Pathogens (Basel, Switzerland) · 2021Review
- A NovelFrontiers in cellular and infection microbiology · 2021Article
- Structural Insights into the Interactions of Candidal Enolase with Human Vitronectin, Fibronectin and Plasminogen.International journal of molecular sciences · 2020Article
- AAA+ Molecular Chaperone ClpB inInternational journal of molecular sciences · 2020Review
- Heterologous Expression of the Pathogen-Specific LIC11711 Gene in the SaprophytePathogens (Basel, Switzerland) · 2020Article
- Leptospira interrogans Bat proteins impair host hemostasis by fibrinogen cleavage and platelet aggregation inhibition.Medical microbiology and immunology · 2020Article
- Leptospiral Immunoglobulin-Like Domain Proteins: Roles in Virulence and Immunity.Frontiers in immunology · 2020Review
- The interaction of two novel putative proteins ofVirulence · 2019Article
- Temperature and Oxidative Stress as Triggers for Virulence Gene Expression in PathogenicFrontiers in microbiology · 2017Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pathogenic Leptospira species are the etiological agents of leptospirosis, a widespread disease of human and veterinary concern. In this study, we report that Leptospira species are capable of binding plasminogen (PLG) in vitro. The binding to the leptospiral surface was demonstrated by indirect immunofluorescence confocal microscopy with living bacteria. The PLG binding to the bacteria seems to occur via lysine residues because the ligation is inhibited by addition of the lysine analog 6-aminocaproic acid. Exogenously provided urokinase-type PLG activator (uPA) converts surface-bound PLG into enzymatically active plasmin, as evaluated by the reaction with the chromogenic plasmin substrate d-Val-Leu-Lys 4-nitroanilide dihydrochloridein. The PLG activation system on the surface of Leptospira is PLG dose dependent and does not cause injury to the organism, as cellular growth in culture was not impaired. The generation of active plasmin within Leptospira was observed with several nonvirulent high-passage strains and with the nonpathogenic saprophytic organism Leptospira biflexa. Statistically significant higher activation of plasmin was detected with a low-passage infectious strain of Leptospira. Plasmin-coated virulent Leptospira interrogans bacteria were capable of degrading purified extracellular matrix fibronectin. The breakdown of fibronectin was not observed with untreated bacteria. Our data provide for the first time in vitro evidence for the generation of active plasmin on the surface of Leptospira, a step that may contribute to leptospiral invasiveness.
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Registered trials
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