TY - JOUR TI - Profiling of myristoylation in Toxoplasma gondii reveals an N-myristoylated protein important for host cell penetration AU - Broncel, Malgorzata AU - Dominicus, Caia AU - Vigetti, Luis AU - Nofal, Stephanie D AU - Bartlett, Edward J AU - Touquet, Bastien AU - Hunt, Alex AU - Wallbank, Bethan A AU - Federico, Stefania AU - Matthews, Stephen AU - Young, Joanna C AU - Tate, Edward W AU - Tardieux, Isabelle AU - Treeck, Moritz A2 - Soldati-Favre, Dominique VL - 9 PY - 2020 DA - 2020/07/03 SP - e57861 C1 - eLife 2020;9:e57861 DO - 10.7554/eLife.57861 UR - https://doi.org/10.7554/eLife.57861 AB - 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. KW - toxoplasma KW - myristoylation KW - proteomics KW - host cell invasion JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -