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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-terminus facing the lumen of the micronemes. MIC7 and its myristoylation play a crucial role in the initial steps of invasion, likely during the interaction with and penetration of the host cell. Myristoylation of secreted eukaryotic proteins represents a substantial expansion of the functional repertoire of this co-translational modification.

Profiling of myristoylation in Toxoplasma gondii reveals an N -myristoylated protein important for host cell penetration