Profiling of myristoylation in <i>Toxoplasma gondii</i> reveals an <i>N</i>-myristoylated protein important for host cell penetration.

ABSTRACT: N-myristoylation is a ubiquitous class of protein lipidation across eukaryotes and N-myristoyl transferase (NMT) has been proposed as an attractive drug target in several pathogens. Myristoylation often primes for subsequent palmitoylation and stable membrane attachment, however, growing evidence suggests additional regulatory roles for myristoylation on proteins. Here we describe the myristoylated proteome of Toxoplasma gondii using chemoproteomic methods and show that a small-molecule NMT inhibitor developed against related Plasmodium spp. is also functional in Toxoplasma. We identify myristoylation on a transmembrane protein, the microneme protein 7 (MIC7), which enters the secretory pathway in an unconventional fashion with the myristoylated N-terminu

SUBMITTER: Broncel M 

PROVIDER: S-EPMC7373427 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature