Comprehensive Lysine Ubiquitome Profiling Reveals Diverse Functions of Lysine Ubiquitination in Eimeria tenella

Eimeria tenella is a parasitic
protozoan
with a direct lifecycle in a single host, but with diverse intermediate
stages while developing in the host. Each E. tenella developmental stage has distinct structural, pathogenic, genetic,
and protein expression, emerging from gene modifications and post-translational
modifications (PTMs) of proteins. Ubiquitination regulates diverse
cellular functions and activities. Until now, however, there have
been sparse data on E. tenella ubiquitination
except on some ubiquitin-related enzymes. It is pertinent to unveil
the mechanism through which E. tenella developmental stages convert ubiquitin to its development. Herein,
the ubiquitome of five life-stages (unsporulated oocyst, early stage
of sporulation (i.e., 7 h into sporulation of the oocyst), sporulated
oocyst, sporozoite, and second-generation merozoite) of E. tenella was investigated and compared. Correlation
analysis of label-free quantitative proteomic and ubiquitomic data
was performed. Ubiquitin proteomes were detected and dynamically expressed
during the E. tenella oocyst sporulation
process and other developmental stages. This implies that protein
ubiquitination is perhaps a key regulator of parasite developmental
transitions, biology, and pathogenicity. In brief, this study lays
the foundation for future in-depth analysis and functional validation
of the ubiquitin proteome and modified proteins in the life cycle
of the avian parasite. The raw ubiquitome and parallel reaction monitoring
(PRM) data sets are accessible via the iProX repository, assigned
with accession numbers PXD043159 and PXD067512, respectively.