ArticlePloS one2015
Features of two new proteins with OmpA-like domains identified in the genome sequences of Leptospira interrogans.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 42 citations in OpenAlex.
- Functional Validation of the Proteome-Identified LIC_13056 Putative Lipoprotein ofInternational journal of molecular sciences · 2026Article
- Cell Adhesion Assays to Investigate Leptospiral Protein Interactions with ECM, Cell Receptors, and Cultured Mammalian Cells: Methods for Understanding Host-Leptospira Interactions.Methods in molecular biology (Clifton, N.J.) · 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
- 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
- Evaluation ofFrontiers in microbiology · 2023Article
- The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components.Virulence · 2021Article
- Revisiting the Development of Vaccines Against PathogenicFrontiers in immunology · 2021Review
- A NovelFrontiers in cellular and infection microbiology · 2021Article
- A Review on Host-Frontiers in cellular and infection microbiology · 2021Review
- The interaction of two novel putative proteins ofVirulence · 2019Article
- MAT cross-reactions or vaccine cross-protection: retrospective study of 863 leptospirosis canine cases.Heliyon · 2018Article
- Evaluation of Lsa46 and Lsa77 Leptospiral Proteins for Their Immunoprotective Activities in Hamster Model of Leptospirosis.BioMed research international · 2018Article
- Complement Evasion by PathogenicFrontiers in immunology · 2016Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leptospirosis is an acute febrile disease caused by pathogenic spirochetes of the genus Leptospira. It is considered an important re-emerging infectious disease that affects humans worldwide. The knowledge about the mechanisms by which pathogenic leptospires invade and colonize the host remains limited since very few virulence factors contributing to the pathogenesis of the disease have been identified. Here, we report the identification and characterization of two new leptospiral proteins with OmpA-like domains. The recombinant proteins, which exhibit extracellular matrix-binding properties, are called Lsa46 - LIC13479 and Lsa77 - LIC10050 (Leptospiral surface adhesins of 46 and 77 kDa, respectively). Attachment of Lsa46 and Lsa77 to laminin was specific, dose dependent and saturable, with KD values of 24.3 ± 17.0 and 53.0 ± 17.5 nM, respectively. Lsa46 and Lsa77 also bind plasma fibronectin, and both adhesins are plasminogen (PLG)-interacting proteins, capable of generating plasmin (PLA) and as such, increase the proteolytic ability of leptospires. The proteins corresponding to Lsa46 and Lsa77 are present in virulent L. interrogans L1-130 and in saprophyte L. biflexa Patoc 1 strains, as detected by immunofluorescence. The adhesins are recognized by human leptospirosis serum samples at the onset and convalescent phases of the disease, suggesting that they are expressed during infection. Taken together, our data could offer valuable information to the understanding of leptospiral pathogenesis.
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