ArticlePLoS neglected tropical diseases2014
Leptospira interrogans binds to cadherins.
Article in PLoS neglected tropical diseases, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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
42 citing papers in PubMed, 63 citations in OpenAlex.
- Bioinformatics-based B-cell epitope identification from Leptospira interrogans outer membrane proteins LIC11574 and LIC13411 for the rational development of a multi-epitope anti-Leptospira vaccine.Archives of microbiology · 2026Article
- Leptospirosis-associated pulmonary hemorrhagic syndrome: immune mechanisms, clinical manifestations, and experimental models.Revista do Instituto de Medicina Tropical de Sao Paulo · 2026Review
- In vitro and in vivo endothelial interactions of Leptospira species are markers of virulence.PLoS neglected tropical diseases · 2026Article
- 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
- Role of E-cadherin in epithelial barrier dysfunction: implications for bacterial infection, inflammation, and disease pathogenesis.Frontiers in cellular and infection microbiology · 2025Review
- Cleavage of cell junction proteins as a host invasion strategy in leptospirosis.Applied microbiology and biotechnology · 2024Review
- Recombinant fusion protein LipL41-OmpL1 as a Potential Candidate for a Cost-effective Vaccine against Leptospirosis.Archives of Razi Institute · 2024Article
- Leucine-rich repeat proteins ofFrontiers in microbiology · 2024Article
- Leptospiral adhesins: from identification to future perspectives.Frontiers in microbiology · 2024Review
- LIC12254 Is a Leptospiral Protein That Interacts with Integrins via the RGD Motif.Tropical medicine and infectious disease · 2023Article
- Editorial: Leptospirosis: pathogenesis, clinical and epidemiological aspects.Frontiers in cellular and infection microbiology · 2023Article
- Host Cell Binding Mediated byInternational journal of molecular sciences · 2022Article
- Weil's Disease-Immunopathogenesis, Multiple Organ Failure, and Potential Role of Gut Microbiota.Biomolecules · 2022Review
- Pulmonary haemorrhage as the earliest sign of severe leptospirosis in hamster model challenged with Leptospira interrogans strain HP358.PLoS neglected tropical diseases · 2022Article
- Rapid and sensitive point-of-care detection of Leptospira by RPA-CRISPR/Cas12a targeting lipL32.PLoS neglected tropical diseases · 2022Article
- Heterologous production of the adhesin LIC13411 from pathogenicFrontiers in cellular and infection microbiology · 2022Article
- Crosstalk between E-Cadherin/β-Catenin and NF-κB Signaling Pathways: The Regulation of Host-Pathogen Interaction during Leptospirosis.International journal of molecular sciences · 2021Article
- Microscale communication between bacterial pathogens and the host epithelium.Genes and immunity · 2021Review
- Serine 26 in Early Growth Response-1 Is Critical for Endothelial Proliferation, Migration, and Network Formation.Journal of the American Heart Association · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Leptospirosis, caused by pathogenic species of Leptospira, is the most widespread zoonosis and has emerged as a major public health problem worldwide. The adhesion of pathogenic Leptospira to host cells, and to extracellular matrix (ECM) components, is likely to be necessary for the ability of leptospires to penetrate, disseminate and persist in mammalian host tissues. Previous work demonstrated that pathogenic L. interrogans binds to host cells more efficiently than to ECM. Using two independent screening methods, mass spectrometry and protein arrays, members of the cadherin family were identified as potential L. interrogans receptors on mammalian host surfaces. We focused our investigation on vascular endothelial (VE)-cadherin, which is widely expressed on endothelia and is primarily responsible for endothelial cell-cell adhesion. Monolayers of EA.hy926 and HMEC-1 endothelial cells produce VE-cadherin, bind L. interrogans in vitro, and are disrupted upon incubation with the bacteria, which may reflect the endothelial damage seen in vivo. Dose-dependent and saturable binding of L. interrogans to the purified VE-cadherin receptor was demonstrated and pretreatment of purified receptor or endothelial cells with function-blocking antibody against VE-cadherin significantly inhibited bacterial attachment. The contribution of VE-cadherin to leptospiral adherence to host endothelial cell surfaces is biologically significant because VE-cadherin plays an important role in maintaining the barrier properties of the vasculature. Attachment of L. interrogans to the vasculature via VE-cadherin may result in vascular damage, facilitating the escape of the pathogen from the bloodstream into different tissues during disseminated infection, and may contribute to the hemorrhagic manifestations of leptospirosis. This work is first to describe a mammalian cell surface protein as a receptor for L. interrogans.
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Registered trials
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.