Lysine acetylation in the spargana of Spirometra mansoni: Insights into glycolysis and EF-hand domain proteins.

Protein post-translational modifications (PTMs) refer to the covalent attachment of chemical groups to polypeptide chains after protein synthesis, which expands protein chemical diversity and enhances functional versatility. Common PTM types include phosphorylation, glycosylation, and lysine acetylation (Kac), a major, reversible PTM regulated by lysine acetyltransferases (KATs) and lysine deacetylases (KDACs). Kac cross-regulates with other modifications to govern chromatin transcription and epigenetic programs, and occurs in histones, nucleoproteins, and cytoplasmic regulatory factors. In this study, we employed proteomic approaches to investigate lysine acetylation in proteins derived from snake-borne spargana for the first time. A total of 390 acetylated proteins and 655 Kac sites were identified. Subcellular localization analysis revealed these acetylated proteins were predominantly localized in the cytoplasm, followed by the mitochondria, nucleus, extracellular matrix, and plasma membrane. This study aims to expand our understanding of protein acetylation in Spirometra mansoni plerocercoid larvae and provide valuable information for designing effective drugs or vaccines to control sparganosis.