ArticlePloS one2010
In vitro identification of novel plasminogen-binding receptors of the pathogen Leptospira interrogans.
Article in PloS one, 2010. 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, 98 citations in OpenAlex.
- The grand escape - how pathogens outsmart the human complement system.Immunobiology · 2025Review
- Design, Development and Immunogenic Evaluation of a Novel Lipl32 Recombinant Protein of Local Pathogenic Leptospira Serovars.Archives of Razi Institute · 2025Article
- 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
- SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens.International journal of molecular sciences · 2022Review
- A Review on Host-Frontiers in cellular and infection microbiology · 2021Review
- A NovelFrontiers in cellular and infection microbiology · 2021Article
- Role of Supramolecule ErpY-Like Lipoprotein ofInfection and immunity · 2019Article
- The interaction of two novel putative proteins ofVirulence · 2019Article
- Plasminogen-binding proteins as an evasion mechanism of the host's innate immunity in infectious diseases.Bioscience reports · 2018Review
- Role of Murine Complement Component C5 in AcuteFrontiers in cellular and infection microbiology · 2018Article
- Article
- Complement Evasion by PathogenicFrontiers in immunology · 2016Review
- The Miller Hypothesis.Forum on immunopathological diseases and therapeutics · 2016Article
- Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding protein.BMC microbiology · 2015Article
- Features of two new proteins with OmpA-like domains identified in the genome sequences of Leptospira interrogans.PloS one · 2015Article
- Translation Elongation Factor Tuf of Acinetobacter baumannii Is a Plasminogen-Binding Protein.PloS one · 2015Article
- Induction of boosted immune response in mice by leptospiral surface proteins expressed in fusion with DnaK.BioMed research international · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLeptospirosis is a multisystem disease caused by pathogenic strains of the genus Leptospira. We have reported that Leptospira are able to bind plasminogen (PLG), to generate active plasmin in the presence of activator, and to degrade purified extracellular matrix fibronectin. METHODOLOGY/PRINCIPAL
findingsWe have now cloned, expressed and purified 14 leptospiral recombinant proteins. The proteins were confirmed to be surface exposed by immunofluorescence microscopy and were evaluated for their ability to bind plasminogen (PLG). We identified eight as PLG-binding proteins, including the major outer membrane protein LipL32, the previously published rLIC12730, rLIC10494, Lp29, Lp49, LipL40 and MPL36, and one novel leptospiral protein, rLIC12238. Bound PLG could be converted to plasmin by the addition of urokinase-type PLG activator (uPA), showing specific proteolytic activity, as assessed by its reaction with the chromogenic plasmin substrate, D-Val-Leu-Lys 4-nitroanilide dihydrochloride. The addition of the lysine analog 6-aminocaproic acid (ACA) inhibited the protein-PLG interaction, thus strongly suggesting the involvement of lysine residues in plasminogen binding. The binding of leptospiral surface proteins to PLG was specific, dose-dependent and saturable. PLG and collagen type IV competed with LipL32 protein for the same binding site, whereas separate binding sites were observed for plasma fibronectin. CONCLUSIONS/SIGNIFICANCE: PLG-binding/activation through the proteins/receptors on the surface of Leptospira could help the bacteria to specifically overcome tissue barriers, facilitating its spread throughout the host.
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