Open AccessAn extracellular Leptospira interrogans leucine‐rich repeat protein binds human E‐ and VE‐cadherins
Author(s) -
Eshghi Azad,
Gaultney Robert A.,
England Patrick,
Brûlé Sébastien,
Miras Isabelle,
Sato Hiromi,
Coburn Jenifer,
Bellalou Jacques,
Moriarty Tara J.,
Haouz Ahmed,
Picardeau Mathieu
Publication year - 2019
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/cmi.12949
Subject(s) - biology , bacterial adhesin , leptospira , leptospira interrogans , microbiology and biotechnology , pathogen , bacteria , human pathogen , gene , antibody , genetics , virulence , serotype
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.