Apicortin defines the Plasmodium apical conoid body but is dispensable for the parasite life cycle

TL;DR

Apicortin is found at the apical end of Plasmodium parasites but is not essential for their life cycle.

Contribution

The study reveals that Apicortin is localized to the apical complex but is not required for parasite development.

Findings

Apicortin localizes to the apical end in invasive parasite stages.

Apicortin forms a ringlike structure in the apical complex region.

Deletion of Apicortin does not affect parasite development.

Abstract

Apicortin shapes the Plasmodium cytoskeleton at the apical end without impacting transmission.

Apicomplexan parasites such as Plasmodium spp. and Toxoplasma gondii possess unique tubulin-based structures, including subpellicular microtubules and apical polar rings, which are essential for parasite motility, host cell invasion, and replication. Apicortin, a microtubule-associated protein, contains a doublecortin (DC) domain and a partial tubulin polymerization-promoting protein (TPPP) domain, both implicated in microtubule binding and stabilization. How tubulin-based structures are maintained is poorly understood, but it may involve Apicortin, so far found only in apicomplexans and the placozoan Trichoplax adhaerens. Here, we investigated the location and function of Apicortin in Plasmodium berghei. Live-cell imaging of a transgenic parasite line expressing GFP-tagged Apicortin showed its location at the apical end of invasive parasite stages within the mosquito vector. Super-resolution and expansion microscopy revealed that Apicortin forms a distinct ringlike structure in the apical complex region at the apical end. However, deletion of the Apicortin gene had no effect on parasite development, indicating that this protein is not essential. This suggests that there may be redundancy or compensatory functions in the mechanisms that stabilize the apical complex.

Figures