Background: Lysine lactylation (Kla) is a novelposttranslational modification (PTM) identified in histone and nonhistone proteins of several eukaryotic cells that directly activates gene expression and DNA replication. However, very little is known about the scope and cellular distribution of Kla in apicomplexan parasites despite its significance in public and animal health care.
Methods: Toxoplasma gondii, the causative agent of toxoplasmosis, is an obligate intracellular apicomplexan parasite that can infect different nucleated cell types of animals and humans.
Toxoplasmosis, caused by , is a common disease worldwide and could be severe and even fatal in immunocompromised individuals and fetuses. Limitation in current available treatment options drives the need to develop novel therapeutics. This study assessed the anti- potential of 103 marine natural products.
View Article and Find Full Text PDFThe apicoplast, which harbors key pathways involved in biosynthesis of vital metabolites, is a unique and essential nonphotosynthetic plastid organelle in apicomplexan parasites. Intriguingly, autophagy-related protein 8 (Atg8), a highly conserved eukaryotic protein, can localize to the outermost membrane of the apicoplast and modulate its inheritance in both and parasites. The Atg8-Atg3 interaction plays a key role in Atg8 lipidation and localization, and our previously work in has suggested that the core Atg8-family interacting motif (AIM) in TgAtg3, FADI, and the R27 residue of TgAtg8 contribute to TgAtg8-TgAtg3 interaction .
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