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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.

Leptospira interrogans Enolase Is Secreted Extracellularly and Interacts with Plasminogen