ArticlePLoS neglected tropical diseases2013
Adhesins of Leptospira interrogans mediate the interaction to fibrinogen and inhibit fibrin clot formation in vitro.
Article in PLoS neglected tropical diseases, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 55 citations in OpenAlex.
- The role of leptospiral proteins in immune evasion and inflammatory response stimulation in HEK293T cell monolayers.Frontiers in immunology · 2025Article
- Unveiling the impact ofInfection and immunity · 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
- 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
- GroEL protein of the Leptospira spp. interacts with host proteins and induces cytokines secretion on macrophages.BMC microbiology · 2021Article
- A NovelFrontiers in cellular and infection microbiology · 2021Article
- Evaluation of LipL32 and LigA/LigB Knockdown Mutants inFrontiers in microbiology · 2021Article
- A Review on Host-Frontiers in cellular and infection microbiology · 2021Review
- In Silico Structural and Functional Characterization of HtrA Proteins ofTropical medicine and infectious disease · 2020Article
- Hemostatic derangement in leptospirosis: A prospective cross-sectional study.International journal of critical illness and injury science · 2020Article
- Putative β-Barrel Outer Membrane Proteins of the Bovine Digital Dermatitis-Associated Treponemes: Identification, Functional Characterization, and Immunogenicity.Infection and immunity · 2020Article
- Leptospira interrogans Bat proteins impair host hemostasis by fibrinogen cleavage and platelet aggregation inhibition.Medical microbiology and immunology · 2020Article
- Role of Supramolecule ErpY-Like Lipoprotein ofInfection and immunity · 2019Article
- The interaction of two novel putative proteins ofVirulence · 2019Article
- Leptospira Immunoglobulin-Like Protein B (LigB) Binds to Both the C-Terminal 23 Amino Acids of Fibrinogen αC Domain and Factor XIII: Insight into the Mechanism of LigB-Mediated Blockage of Fibrinogen α Chain Cross-Linking.PLoS neglected tropical diseases · 2016Article
- What Makes a Bacterial Species Pathogenic?:Comparative Genomic Analysis of the Genus Leptospira.PLoS neglected tropical diseases · 2016Article
- Features of two new proteins with OmpA-like domains identified in the genome sequences of Leptospira interrogans.PloS one · 2015Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report in this work that Leptospira strains, virulent L. interrogans serovar Copenhageni, attenuated L. interrogans serovar Copenhageni and saprophytic L. biflexa serovar Patoc are capable of binding fibrinogen (Fg). The interaction of leptospires with Fg inhibits thrombin- induced fibrin clot formation that may affect the haemostatic equilibrium. Additionally, we show that plasminogen (PLG)/plasmin (PLA) generation on the surface of Leptospira causes degradation of human Fg. The data suggest that PLA-coated leptospires were capable to employ their proteolytic activity to decrease one substrate of the coagulation cascade. We also present six leptospiral adhesins and PLG- interacting proteins, rLIC12238, Lsa33, Lsa30, OmpL1, rLIC11360 and rLIC11975, as novel Fg-binding proteins. The recombinant proteins interact with Fg in a dose-dependent and saturable fashion when increasing protein concentration was set to react to a fix human Fg concentration. The calculated dissociation equilibrium constants (K D ) of these reactions ranged from 733.3 ± 276.8 to 128 ± 89.9 nM for rLIC12238 and Lsa33, respectively. The interaction of recombinant proteins with human Fg resulted in inhibition of fibrin clot by thrombin-catalyzed reaction, suggesting that these versatile proteins could mediate Fg interaction in Leptospira. Our data reveal for the first time the inhibition of fibrin clot by Leptospira spp. and presents adhesins that could mediate these interactions. Decreasing fibrin clot would cause an imbalance of the coagulation cascade that may facilitate bleeding and help bacteria dissemination.
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