Host protein eEF1A1 affected the infection of Cryptosporidium parvum through interacting with CpHSP90

Cryptosporidium parvum is a common protozoan pathogen that causes severe diarrhea in humans and animals. HSP90 plays a key role in eukaryotic growth and development. Previous studies have revealed the presence of C. parvum heat shock protein 90 (CpHSP90) in extracellular vesicles derived from sporozoites, suggesting its potential involvement in host-parasite interactions. In this study, we employed purified CpHSP90 as bait to identify interacting host cell proteins through pull-down assays coupled with mass spectrometry. The interaction between CpHSP90 and host elongation factor 1-alpha 1 (eEF1A1) was confirmed by co-immunoprecipitation and bimolecular fluorescence complementation assays. RNA silencing of eEF1A1 led to a significant reduction in C. parvum burden, whereas overexpression of EEF1A1 markedly enhanced parasite infection. These findings demonstrate that the host protein eEF1A1 participates in C. parvum infection by promoting parasite growth and is critical for the endogenous development of the parasite. This study provides new insights into the role of CpHSP90 in C. parvum pathogenesis and highlights the potential of host-parasite protein interactions as novel targets for cryptosporidiosis intervention