Cryptosporidium parvum is a common waterborne parasite that causes a life-threatening intestinal disease in people with a weak immune system. Currently, there is no effective treatment. Bioinformatics data and staining assays have shown the presence of amyloid-forming sequences in C. parvum. Amyloids influence intercellular and surface adhesion in microbes. Here, we demonstrate that functional amyloids in C. parvum also play a critical role in the parasite’s adhesion to host cells. Inhibiting a parasite’s adhesion mechanisms to its host is a crucial step in order to prevent parasitic infections. C. parvum’s illness-inducing sporozoites fluoresce when stained with amyloid-perturbing dyes. We show that sporozoites can be detected with amyloid dyes. Additionally, inhibitory concentrations of anti-amyloid compounds were shown to decrease infection levels of C. parvum to host cells using direct immunofluorescence assays, which are gold standards for the detection of C. parvum oocysts, but not the infectious sporozoites. Taken together, these results suggest that C. parvum has functional amyloids that significantly mediate the parasite’s infection process. A stronger understanding of the role amyloids play C. parvum’s parasite-host adhesion can aid in the development of a targeted therapeutic against this disease.

Cryptosporidium parvum has functional amyloids that impact adhesion and infection

251st National Meeting (2016)

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