Abstract
S-palmitoylation is a post-translational lipid modification that is widespread among Plasmodium proteins and essential for parasite development. Little is known about the contribution of palmitoylation to the function of individual parasite molecules and structures. Alveolins are major components of the subpellicular network (SPN), a cortical cytoskeleton primarily involved in providing mechanical strength to the cell. We show here that the alveolin IMC1c is palmitoylated on a conserved cysteine motif, and that non-palmitoylated IMC1c displays normal expression, stability and trafficking. However, mutant parasites exhibit reduced osmotic stress resistance and tensile strength. These findings support the hypothesis that alveolin palmitoylation enhances cytoskeletal function by strengthening the connection between the SPN and the adjoining inner membrane complex via lipid anchoring.
Highlights
Three invasive life stages: the ookinete, sporozoite and merozoite, feature among the many different developmental forms of the malaria parasite
It has been shown in the rodent malaria species Plasmodium berghei that disruption of alveolins is accompanied by reduced tensile strength of the zoite stages in which they are expressed [5,7,8,9,10]
The cysteine motif of IMC1c is dispensable for parasite development
Summary
Three invasive life stages: the ookinete, sporozoite and merozoite, feature among the many different developmental forms of the malaria parasite. These so-called ‘zoites’ are characterised by having specialised secretory organelles (e.g. rhoptries and micronemes) as well as a specialised cortical structure termed the pellicle, both of which are adaptations required for their motile and invasive properties. In the genus Plasmodium, 13 conserved and syntenic alveolin family members have been identified that are differentially expressed among the three zoites stages [6,7] It has been shown in the rodent malaria species Plasmodium berghei that disruption of alveolins is accompanied by reduced tensile strength of the zoite stages in which they are expressed [5,7,8,9,10]. In addition to these conserved ‘alveolin domains’, a subset of the alveolins possess conserved cysteine motifs close to their amino- or carboxy-terminus, which are predicted to act as substrates for post-translational S-palmitoylation [13,14]
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