ArticleThe Journal of biological chemistry2009
Repeated domains of leptospira immunoglobulin-like proteins interact with elastin and tropoelastin.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 125 citations in OpenAlex.
- Host adaptation drives genome evolution and virulence diversification in a bacterial zoonotic pathogen.bioRxiv : the preprint server for biology · 2026Article
- TheInfection and immunity · 2026Article
- In vitro and in vivo endothelial interactions of Leptospira species are markers of virulence.PLoS neglected tropical diseases · 2026Article
- Characterisation of Putative Outer Membrane Proteins fromMicroorganisms · 2024Article
- GroEL protein of the Leptospira spp. interacts with host proteins and induces cytokines secretion on macrophages.BMC microbiology · 2021Article
- Evaluation of LipL32 and LigA/LigB Knockdown Mutants inFrontiers in microbiology · 2021Article
- A Review on Host-Frontiers in cellular and infection microbiology · 2021Review
- Comparative genomic analysis of Chinese human leptospirosis vaccine strain and circulating isolate.Human vaccines & immunotherapeutics · 2020Article
- Strain-specific joint invasion and colonization by Lyme disease spirochetes is promoted by outer surface protein C.PLoS pathogens · 2020Article
- The Factor H-Binding Site of CspZ as a Protective Target against Multistrain, Tick-Transmitted Lyme Disease.Infection and immunity · 2020Article
- Putative β-Barrel Outer Membrane Proteins of the Bovine Digital Dermatitis-Associated Treponemes: Identification, Functional Characterization, and Immunogenicity.Infection and immunity · 2020Article
- Leptospiral Immunoglobulin-Like Domain Proteins: Roles in Virulence and Immunity.Frontiers in immunology · 2020Review
- Cloning and sequencing of theIranian journal of microbiology · 2019Article
- RNA Thermometers in Bacterial Pathogens.Microbiology spectrum · 2018Review
- 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
- Eliminating Factor H-Binding Activity ofFrontiers in immunology · 2018Article
- Extended low-resolution structure of aeLife · 2017Article
- Borrelia burgdorferi outer surface protein C (OspC) binds complement component C4b and confers bloodstream survival.Cellular microbiology · 2017Article
- Article
- Immunoprotective properties of recombinant LigA and LigB in a hamster model of acute leptospirosis.PloS one · 2017Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leptospira spp., the causative agents of leptospirosis, adhere to components of the extracellular matrix, a pivotal role for colonization of host tissues during infection. Previously, we and others have shown that Leptospira immunoglobulin-like proteins (Lig) of Leptospira spp. bind to fibronectin, laminin, collagen, and fibrinogen. In this study, we report that Leptospira can be immobilized by human tropoelastin (HTE) or elastin from different tissues, including lung, skin, and blood vessels, and that Lig proteins can bind to HTE or elastin. Moreover, both elastin and HTE bind to the same LigB immunoglobulin-like domains, including LigBCon4, LigBCen7'-8, LigBCen9, and LigBCen12 as demonstrated by enzyme-linked immunosorbent assay (ELISA) and competition ELISAs. The LigB immunoglobulin-like domain binds to the 17th to 27th exons of HTE (17-27HTE) as determined by ELISA (LigBCon4, K(D) = 0.50 microm; LigBCen7'-8, K(D) = 0.82 microm; LigBCen9, K(D) = 1.54 microm; and LigBCen12, K(D) = 0.73 microm). The interaction of LigBCon4 and 17-27HTE was further confirmed by steady state fluorescence spectroscopy (K(D) = 0.49 microm) and ITC (K(D) = 0.54 microm). Furthermore, the binding was enthalpy-driven and affected by environmental pH, indicating it is a charge-charge interaction. The binding affinity of LigBCon4D341N to 17-27HTE was 4.6-fold less than that of wild type LigBCon4. In summary, we show that Lig proteins of Leptospira spp. interact with elastin and HTE, and we conclude this interaction may contribute to Leptospira adhesion to host tissues during infection.
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