In 2009, apicortin was identified in silico as a characteristic protein of apicomplexans that also occurs in the placozoa, . Since then, it has been found that apicortin also occurs in free-living cousins of apicomplexans (chromerids) and in flagellated fungi. It contains a partial p25-α domain and a doublecortin (DCX) domain, both of which have tubulin/microtubule binding properties. Apicortin has been studied experimentally in two very important apicomplexan pathogens, and . It is localized in the apical complex in both parasites. In , apicortin plays a key role in shaping the structure of a special tubulin polymer, conoid. In both parasites, its absence or downregulation has been shown to impair pathogen-host interactions. Based on these facts, it has been suggested as a therapeutic target for treatment of malaria and toxoplasmosis.
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