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.

Parasitology Research
|December 6, 2014
PubMed

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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