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An extracellular Leptospira interrogans leucine-rich repeat protein binds human E- and VE-cadherins. Cell Microbiol 2018 Sep 01:e12949 PMID: 30171791

Pubmed ID



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 L. interrogans, LIC10831, has been previously analyzed 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 evidence of LRR protein-mediated host-pathogen interactions and identify a new multi-receptor binding protein from this infectious Leptospira species.

Author List

Eshghi A, Gaultney R, England P, Brûlé S, Miras I, Sato H, Coburn J, Bellalou J, Moriarty TJ, Haouz A, Picardeau M


Jenifer Coburn PhD Professor in the Medicine department at Medical College of Wisconsin

jenkins-FCD Prod-271 16cb5dcaa6d2cfe4986875aea432578e3ad30554