ArticlePloS one2013
Interaction of Leptospira elongation factor Tu with plasminogen and complement factor H: a metabolic leptospiral protein with moonlighting activities.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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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Who cites it
34 citing papers in PubMed, 86 citations in OpenAlex.
- Leptospira glyceraldehyde-3-phosphate dehydrogenase (LiGAPDH): a cell-surface plasminogen binding protein.FEMS microbiology letters · 2026Article
- Unveiling the impact ofInfection and immunity · 2024Article
- 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
- The structure ofFrontiers in immunology · 2023Article
- Extraintestinal pathogenicVirulence · 2022Article
- The Exploration of Complement-Resistance Mechanisms of Pathogenic Gram-Negative Bacteria to Support the Development of Novel Therapeutics.Pathogens (Basel, Switzerland) · 2022Review
- Subversion of the immune response of human pathogenic spirochetes.Journal of clinical laboratory analysis · 2022Review
- Screening of Surface-Exposed Lipoproteins ofFrontiers in microbiology · 2022Article
- Immunogenic Proteins of Group B Streptococcus-Potential Antigens in Immunodiagnostic Assay for GBS Detection.Pathogens (Basel, Switzerland) · 2021Review
- Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona.PLoS neglected tropical diseases · 2021Article
- GroEL protein of the Leptospira spp. interacts with host proteins and induces cytokines secretion on macrophages.BMC microbiology · 2021Article
- Leptospiral Infection, Pathogenesis and Its Diagnosis-A Review.Pathogens (Basel, Switzerland) · 2021Review
- A Review on Host-Frontiers in cellular and infection microbiology · 2021Review
- Deciphering the Role ofFrontiers in immunology · 2021Article
- Hijacking Factor H for Complement Immune Evasion.Frontiers in immunology · 2021Review
- Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and OmpT Proteins of Shiga Toxin-ProducingMicroorganisms · 2020Article
- The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis.Frontiers in microbiology · 2019Review
- Monoclonal Antibody Preparation and Epitope Identification forFrontiers in microbiology · 2019Article
- Plasminogen-binding proteins as an evasion mechanism of the host's innate immunity in infectious diseases.Bioscience reports · 2018Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The elongation factor Tu (EF-Tu), an abundant bacterial protein involved in protein synthesis, has been shown to display moonlighting activities. Known to perform more than one function at different times or in different places, it is found in several subcellular locations in a single organism, and may serve as a virulence factor in a range of important human pathogens. Here we demonstrate that Leptospira EF-Tu is surface-exposed and performs additional roles as a cell-surface receptor for host plasma proteins. It binds plasminogen in a dose-dependent manner, and lysine residues are critical for this interaction. Bound plasminogen is converted to active plasmin, which, in turn, is able to cleave the natural substrates C3b and fibrinogen. Leptospira EF-Tu also acquires the complement regulator Factor H (FH). FH bound to immobilized EF-Tu displays cofactor activity, mediating C3b degradation by Factor I (FI). In this manner, EF-Tu may contribute to leptospiral tissue invasion and complement inactivation. To our knowledge, this is the first description of a leptospiral protein exhibiting moonlighting activities.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.