Genome-Wide Prediction and Analysis of Secreted Proteins of Enterocytozoon hepatopenaei

Abstract:

Secreted proteins are synthesized in cells and secreted to function outside the cell. They play an important role in the manipulation of host cells and the virulence of many eukaryotic protozoan parasites. Enterocytozoon hepatopenaei (EHP) is an obligate intracellular parasite that can infect a variety of economically valuable shrimp species, and is one of the most serious diseases affecting global shrimp production. Here, we predict the secreted proteins of the EHP genome with the EuSecPred2.0 pipeline and analyzed the length of these secreted proteins, the length of the signal peptide, and the amino acid distribution at the cleavage site, and annotated the function of secreted proteins. The results show that the length of the secreted proteins ranged from 30 to 400 amino acid residues, the signal peptides covered approximately 9~32 amino acids, and the cleavage sites of the signal peptides were mainly composed of hydrophobic amino acids. Motif analysis revealed a NV[VT][IK]CA[ED][SA] motif in signal peptides. Functional annotation of proteins revealed that a variety of key proteins are involved in adhesion and infection of microsporidia, regulation of cell cycle, and immune response. The results shed light on the infection mechanism of EHP and provide a theoretical basis for further defining the pathogenic factors of EHP.