PbSR is synthesized in macrogametocytes and involved in formation of the malaria crystalloids

Victoria Carter1, Shoichi Shimizu, Meiji Arai

  • 1Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK.

Insights

The malaria parasite Plasmodium berghei scavenger receptor-like protein (PbSR) is crucial for crystalloid formation in developing ookinetes. This protein is essential for successful sporozoite development within the oocyst, impacting malaria transmission.

Area of Science:

  • Malariology
  • Cell Biology
  • Parasitology

Background:

  • Crystalloids are transient organelles in malaria ookinetes with unknown origins and functions.
  • The Plasmodium berghei scavenger receptor-like protein (PbSR) is vital for parasite transmission from mosquito to host.
  • PbSR knockout parasites exhibit normal oocyst numbers but lack sporozoites, indicating a role in oocyst sporogony.

Purpose of the Study:

  • To investigate the role of PbSR in malaria parasite development, specifically its involvement with crystalloids.
  • To elucidate the synthesis, targeting, and function of PbSR during the parasite lifecycle.

Main Methods:

  • Fluorescent protein tagging was employed to track PbSR localization.
  • Targeted gene disruption (knockout) was used to assess PbSR function.
  • Oocyst sporulation rates were analyzed in both infected mosquitoes and in vitro conditions.

Main Results:

  • PbSR is synthesized in macrogametocytes and targeted to crystalloids in developing ookinetes, contributing to their formation.
  • PbSR knockout parasites show significantly reduced oocyst sporulation rates in infected mosquitoes.
  • In vitro sporulation rates of PbSR knockout parasites were unaffected, suggesting mosquito-specific factors influence the phenotype.

Conclusions:

  • PbSR is the first identified parasite protein associated with the crystalloid organelle.
  • PbSR plays a critical role in crystalloid formation and subsequent sporozoite development within the oocyst.
  • A novel protein-trafficking mechanism for delivering PbSR to oocysts is suggested, potentially influenced by mosquito factors.

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