Skip to Main content Skip to Navigation
Journal articles

An extracellular Leptospira interrogans leucine‐rich repeat protein binds human E‐ and VE‐cadherins

Abstract : Pathogenic Leptospira bacteria are the causative agents of leptospirosis, a zoonotic disease affecting animals and humans worldwide. These pathogenic species have the ability to rapidly cross host tissue barriers by a yet unknown mechanism. A comparative analysis of pathogens and saprophytes revealed a higher abundance of genes encoding proteins with leucine-rich repeat (LRR) domains in the genomes of pathogens. In other bacterial pathogens, proteins with LRR domains have been shown to be involved in mediating host cell attachment and invasion. One protein from the pathogenic species Leptospira interrogans, LIC10831, has been previously analysed via X-ray crystallography, with findings suggesting it may be an important bacterial adhesin. Herein we show that LIC10831 elicits an antibody response in infected animals, is actively secreted by the bacterium, and binds human E- and VE-cadherins. These results provide biochemical and cellular evidences of LRR protein-mediated host-pathogen interactions and identify a new multireceptor binding protein from this infectious Leptospira species.
Document type :
Journal articles
Complete list of metadatas

https://hal-pasteur.archives-ouvertes.fr/pasteur-02548693
Contributor : Sylvie Murguet <>
Submitted on : Monday, April 20, 2020 - 7:42:26 PM
Last modification on : Wednesday, June 17, 2020 - 6:18:03 PM

Licence


Distributed under a Creative Commons Attribution - NonCommercial - NoDerivatives 4.0 International License

Identifiers

Collections

Citation

Azad Eshghi, Robert A. Gaultney, Patrick England, Sébastien Brûlé, Isabelle Miras, et al.. An extracellular Leptospira interrogans leucine‐rich repeat protein binds human E‐ and VE‐cadherins. Cellular Microbiology, Wiley, 2019, 21 (2), pp.e12949. ⟨10.1111/cmi.12949⟩. ⟨pasteur-02548693⟩

Share

Metrics

Record views

40

Files downloads

95