title: Leptospira interrogans enolase is secreted extracellularly and interacts with plasminogen.
abstract: Leptospira interrogans is the agent for leptospirosis, an important zoonosis in humans and animals across the globe. Surface proteins of invading pathogens, such as L. interrogans, are thought to be responsible for successful microbial persistence in vivo via interaction with specific host components. In particular, a number of invasive infectious agents exploit host proteolytic pathways, such as one involving plasminogen (Pg), which aid in efficient pathogen dissemination within the host. Here we show that L. interrogans serovar Lai binds host Pg and that the leptospiral gene product LA1951, annotated as enolase, is involved in this interaction. Interestingly, unlike in related pathogenic Spirochetes, such as Borrelia burgdorferi, LA1951 is not readily detectable in the L. interrogans outer membrane. We show that the antigen is indeed secreted extracellularly; however, it can reassociate with the pathogen surface, where it displays Pg-binding and measurable enzymatic activity. Hamsters infected with L. interrogans also develop readily detectable antibody responses against enolase. Taken together, our results suggest that the L. interrogans enolase has evolved to play a role in pathogen interaction with host molecules, which may contribute to the pathogenesis of leptospirosis.
authors.affiliation: Department of Veterinary Medicine, University of Maryland, and Virginia-Maryland Regional College of Veterinary Medicine, College Park, Maryland, United States of America.
authors.forename: Sarah Veloso
authors.initials: SV
authors.lastname: Nogueira
authors.forename: Brian T
authors.initials: BT
authors.lastname: Backstedt
authors.forename: Alexis A
authors.initials: AA
authors.lastname: Smith
authors.forename: Jin-Hong
authors.initials: JH
authors.lastname: Qin
authors.forename: Elsio A
authors.initials: EA
authors.lastname: Wunder
authors.forename: Albert
authors.initials: A
authors.lastname: Ko
authors.forename: Utpal
authors.initials: U
authors.lastname: Pal
mesh_terms: D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D006224:Cricetinae; D007921:Leptospira interrogans / Q000201:enzymology*; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D010958:Plasminogen / Q000378:metabolism*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D010958:Plasminogen; D010751:Phosphopyruvate Hydratase