Catecholamine-Modulated Novel Surface-Exposed Adhesin LIC20035 of Leptospira Spp. Binds Host Extracellular Matrix Components and Is Recognized by the Host During Infection

In this study, the effect of the host stress hormone catecholamine on gene transcripts encoding outer membrane proteins was investigated. There was no impact of catecholamine supplementation on the growth pattern of ; however, 7 genes out of 41 were differentially transcribed, and the effect was reversed to the basal level in the presence of the antagonist propranolol. Comprehensive analysis of one of the differentially regulated proteins, LIC20035 (in serovar Copenhageni)/LB047 (in serovar Lai) (due to catecholamine supplementation), revealed immunogenicity and ability to adhere to host extracellular matrices. Protease accessibility assay and phase partition of integral membrane proteins of showed LIC20035/LB047 to be an outer membrane surface-exposed protein. The recombinant LIC20035 protein can be serologically detected using human/bovine sera positive for leptospirosis. Moreover, the recombinant LIC20035 can bind to diverse host extracellular matrices, with a higher affinity toward collagen and chondroitin sulfate. Leptospirosis is a neglected tropical disease of global importance. This study aimed to identify outer membrane proteins of pathogenic responding to host chemical signals like catecholamines, with the potential to serve as virulence factors, new serodiagnostic antigens, and vaccine candidates. This study mimicked the plausible means by which during infection and hormonal stress intercepts host catecholamines to disseminate in host tissues.