ArticlePloS one2010
The terminal immunoglobulin-like repeats of LigA and LigB of Leptospira enhance their binding to gelatin binding domain of fibronectin and host cells.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 71 citations in OpenAlex.
- In vitro and in vivo endothelial interactions of Leptospira species are markers of virulence.PLoS neglected tropical diseases · 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
- Navigating infection by pathogenic spirochetes: The host-bacteria interface at the atomic level.Protein science : a publication of the Protein Society · 2025Review
- Host Cell Binding Mediated byInternational journal of molecular sciences · 2022Article
- A Review on Host-Frontiers in cellular and infection microbiology · 2021Review
- Deciphering the Role ofFrontiers in immunology · 2021Article
- Article
- Leptospiral Immunoglobulin-Like Domain Proteins: Roles in Virulence and Immunity.Frontiers in immunology · 2020Review
- Blp1 protein shows virulence-associated features and elicits protective immunity to Acinetobacter baumannii infection.BMC microbiology · 2019Article
- RNA Thermometers in Bacterial Pathogens.Microbiology spectrum · 2018Review
- Extractable Bacterial Surface Proteins in Probiotic-Host Interaction.Frontiers in microbiology · 2018Review
- Article
- Immunoprotective properties of recombinant LigA and LigB in a hamster model of acute leptospirosis.PloS one · 2017Article
- Acquisition of negative complement regulators by the saprophyte Leptospira biflexa expressing LigA or LigB confers enhanced survival in human serum.Immunology letters · 2016Article
- A novel adhesive factor contributing to the virulence of Vibrio parahaemolyticus.Scientific reports · 2015Article
- Fine Mapping of the Interaction between C4b-Binding Protein and Outer Membrane Proteins LigA and LigB of Pathogenic Leptospira interrogans.PLoS neglected tropical diseases · 2015Article
- Evaluation of pre-induction temperature, cell growth at induction and IPTG concentration on the expression of a leptospiral protein in E. coli using shaking flasks and microbioreactor.BMC research notes · 2014Article
- NMR solution structure of the terminal immunoglobulin-like domain from the leptospira host-interacting outer membrane protein, LigB.Biochemistry · 2014Article
- Isolation and characterization of two novel plasmids from pathogenic Leptospira interrogans serogroup Canicola Serovar Canicola strain Gui44.PLoS neglected tropical diseases · 2014Article
- B-cell-specific peptides of leptospira interrogans LigA for diagnosis of patients with acute leptospirosis.Clinical and vaccine immunology : CVI · 2014Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leptospira spp. are pathogenic spirochetes that cause the zoonotic disease leptospirosis. Leptospiral immunoglobulin (Ig)-like protein B (LigB) contributes to the binding of Leptospira to extracellular matrix proteins such as fibronectin, fibrinogen, laminin, elastin, tropoelastin and collagen. A high-affinity Fn-binding region of LigB has been localized to LigBCen2, which contains the partial 11th and full 12th Ig-like repeats (LigBCen2R) and 47 amino acids of the non-repeat region (LigBCen2NR) of LigB. In this study, the gelatin binding domain of fibronectin was shown to interact with LigBCen2R (K(D) = 1.91+/-0.40 microM). Not only LigBCen2R but also other Ig-like domains of Lig proteins including LigAVar7'-8, LigAVar10, LigAVar11, LigAVar12, LigAVar13, LigBCen7'-8, and LigBCen9 bind to GBD. Interestingly, a large gain in affinity was achieved through an avidity effect, with the terminal domains, 13th (LigA) or 12th (LigB) Ig-like repeat of Lig protein (LigAVar7'-13 and LigBCen7'-12) enhancing binding affinity approximately 51 and 28 fold, respectively, compared to recombinant proteins without this terminal repeat. In addition, the inhibited effect on MDCKs cells can also be promoted by Lig proteins with terminal domains, but these two domains are not required for gelatin binding domain binding and cell adhesion. Interestingly, Lig proteins with the terminal domains could form compact structures with a round shape mediated by multidomain interaction. This is the first report about the interaction of gelatin binding domain of Fn and Lig proteins and provides an example of Lig-gelatin binding domain binding mediating bacterial-host interaction.
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