Plasmin, a host protease important in wound healing, has been shown to aid pathogen invasion and promote pathogen host evasion. However, the role of this protease during gut infection is not known. Clostridioides difficile enteric disease causes major morbidity and mortality globally. Spores are crucial for infection, however, their role in the host is poorly understood. Here we show that the zymogen human plasminogen is recruited to the toxin-damaged gut, resulting in immune dysregulation, tissue degradation and reduced survival. Plasminogen specifically binds to C. difficile spores and active plasmin degrades their surface, facilitating rapid germination. We developed and structurally characterized antibodies that inhibit human plasminogen activation and tested their therapeutic efficacy. Remarkably, plasminogen activation inhibition reduced disease severity. Collectively, our data reveal a new disease mechanism in which human plasminogen is recruited to the damaged gut during infection, exacerbating C. difficile-mediated disease in mice. Human plasminogen binds to C. difficile spores and upon activation to plasmin, remodels the spore surface, facilitating rapid spore germination. Finally, inhibitors of plasminogen activation may have utility for the treatment of C. difficile or other infection-mediated gastrointestinal diseases.