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Published on: May 16, 2013
Plasmodium alveolins possess distinct but structurally and functionally related multi-repeat domains
Fatimah S Al-Khattaf1, Annie Z Tremp, Johannes T Dessens
1Pathogen Molecular Biology Department, Faculty of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine, Keppel Street, London, WC1E 7HT, UK.
Abstract:
The invasive and motile life stages of malaria parasites (merozoite, ookinete and sporozoite) possess a distinctive cortical structure termed the pellicle. The pellicle is characterised by a double-layered 'inner membrane complex' (IMC) located underneath the plasma membrane, which is supported by a cytoskeletal structure termed the subpellicular network (SPN). The SPN consists of intermediate filaments, whose major constituents include a family of proteins called alveolins. Here, we re-appraise the alveolins in the genus Plasmodium with respect to their repertoire, structure and interrelatedness. Amongst 13 family members identified, we distinguish two domain types that, albeit distinct at the primary structure level, are structurally related and contain tandem repeats with a consensus 12-amino acid periodicity. Analysis in Plasmodium berghei of the most divergent alveolin, PbIMC1d, reveals a zoite-specific expression in ookinetes and a subcellular localisation in the pellicle, consistent with its predicted role as a SPN component. Knockout of PbIMC1d gives rise to a wild-type phenotype with respect to ookinete morphogenesis, tensile strength, gliding motility and infectivity, presenting the first example of apparent functional redundancy amongst alveolin family members.
Insights
Malaria parasites have a unique pellicle structure. Researchers studied alveolins, key proteins in this structure, finding functional redundancy in Plasmodium berghei, suggesting complex parasite biology.
Area of Science:
- Cell biology
- Parasitology
- Protein structure
Background:
- Malaria parasites possess a pellicle, a critical cortical structure for invasive stages.
- The pellicle is supported by a subpellicular network (SPN) composed of intermediate filaments, primarily alveolins.
- Understanding alveolin family members is crucial for comprehending parasite structure and function.
Purpose of the Study:
- To re-appraise alveolins within the Plasmodium genus, examining their repertoire, structure, and relationships.
- To investigate the expression, localization, and function of a divergent alveolin, PbIMC1d, in Plasmodium berghei.
Main Methods:
- Bioinformatic analysis to identify and classify alveolin family members.
- Expression and localization studies of PbIMC1d in Plasmodium berghei ookinetes.
- Gene knockout experiments to assess the in vivo phenotype of PbIMC1d deficiency.
Main Results:
- Identified 13 alveolin family members in Plasmodium, distinguishing two structurally related domain types with tandem repeats.
- PbIMC1d is expressed specifically in ookinetes and localizes to the pellicle, consistent with a SPN component role.
- PbIMC1d knockout parasites exhibited wild-type characteristics in ookinete development, motility, and infectivity, indicating functional redundancy.
Conclusions:
- Alveolins form a structurally conserved family with distinct domain types within Plasmodium.
- PbIMC1d is a functional component of the Plasmodium berghei pellicle, but its absence does not impair parasite fitness.
- This study presents the first evidence of functional redundancy among alveolins, highlighting the complexity of the parasite cytoskeleton.
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