ArticlePloS one2009
A comprehensive approach to identification of surface-exposed, outer membrane-spanning proteins of Leptospira interrogans.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 86 citations in OpenAlex.
- Unveiling the impact ofInfection and immunity · 2024Article
- Immunological characterization of recombinant outer membrane Loa22 protein of local pathogenicVeterinary research forum : an international quarterly journal · 2024Article
- Leptospiral adhesins: from identification to future perspectives.Frontiers in microbiology · 2024Review
- Components Subcellular Localization: Cell Surface Exposure.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Leptospiral imelysin (LIC_10713) is secretory, immunogenic and binds to laminin, fibronectin, and collagen IV.Applied microbiology and biotechnology · 2023Article
- Characterization of Treponema denticola Major Surface Protein (Msp) by Deletion Analysis and Advanced Molecular Modeling.Journal of bacteriology · 2022Article
- Insight into the Structure, Functions, and Dynamics of theMembranes · 2022Review
- Identification of Leptospiral Protein Antigens Recognized by WC1Infection and immunity · 2022Article
- Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona.PLoS neglected tropical diseases · 2021Article
- The Leptospiral General Secretory Protein D (GspD), a secretin, elicits complement-independent bactericidal antibody against diverseVaccine: X · 2021Article
- Leptospiral Infection, Pathogenesis and Its Diagnosis-A Review.Pathogens (Basel, Switzerland) · 2021Review
- Revisiting the Development of Vaccines Against PathogenicFrontiers in immunology · 2021Review
- GspD, The Type II Secretion System Secretin ofVaccines · 2020Article
- Role of Supramolecule ErpY-Like Lipoprotein ofInfection and immunity · 2019Article
- The interaction of two novel putative proteins ofVirulence · 2019Article
- Isolation and Identification of Putative Protein Substrates of the AAA+ Molecular Chaperone ClpB from the Pathogenic SpirochaeteInternational journal of molecular sciences · 2018Article
- Catecholamine-Modulated Novel Surface-Exposed Adhesin LIC20035 of Leptospira spp. Binds Host Extracellular Matrix Components and Is Recognized by the Host during Infection.Applied and environmental microbiology · 2018Article
- A Universal Vaccine against Leptospirosis: Are We Going in the Right Direction?Frontiers in immunology · 2017Article
- Proteomics-driven Antigen Discovery for Development of Vaccines Against Gonorrhea.Molecular & cellular proteomics : MCP · 2016Article
- Life Stage-specific Proteomes of Legionella pneumophila Reveal a Highly Differential Abundance of Virulence-associated Dot/Icm effectors.Molecular & cellular proteomics : MCP · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Leptospirosis is a zoonosis with worldwide distribution caused by pathogenic spirochetes belonging to the genus Leptospira. The leptospiral life cycle involves transmission via fresh water and colonization of the renal tubules of their reservoir hosts or infection of accidental hosts, including humans. Bacterial outer membrane proteins (OMPs), particularly those with surface-exposed regions, play crucial roles in virulence mechanisms of pathogens and the adaptation to various environmental conditions, including those of the mammalian host. Little is known about the surface-exposed OMPs in Leptospira, particularly those with outer membrane-spanning domains. Herein, we describe a comprehensive strategy for identification and characterization of leptospiral transmembrane OMPs. The genomic sequence of L. interrogans serovar Copenhageni strain Fiocruz L1-130 allowed us to employ the beta-barrel prediction programs, PRED-TMBB and TMBETA-NET, to identify potential transmembrane OMPs. Several complementary methods were used to characterize four novel OMPs, designated OmpL36, OmpL37, OmpL47 and OmpL54. In addition to surface immunofluorescence and surface biotinylation, we describe surface proteolysis of intact leptospires as an improved method for determining the surface exposure of leptospiral proteins. Membrane integration was confirmed using techniques for removal of peripheral membrane proteins. We also demonstrate deficiencies in the Triton X-114 fractionation method for assessing the outer membrane localization of transmembrane OMPs. Our results establish a broadly applicable strategy for the elucidation of novel surface-exposed outer membrane-spanning proteins of Leptospira, an essential step in the discovery of potential virulence factors, diagnostic antigens and vaccine candidates.
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