Structural Basis for Parasite-Specific Functions of the Divergent Profilin of Plasmodium falciparum

Inari Kursula, Petri Kursula, Markus Ganter, Santosh Panjikar, Kai Matuschewski, Herwig Schüler

Research output: Contribution to journalArticleResearchpeer-review

49 Citations (Scopus)

Abstract

Profilins are key regulators of actin dynamics. They sequester actin monomers, forming a pool for rapid polymer formation stimulated by proteins such as formins. Apicomplexan parasites utilize a highly specialized microfilament system for motility and host cell invasion. Their genomes encode only a small number of divergent actin regulators. We present the first crystal structure of an apicomplexan profilin, that of the malaria parasite Plasmodium falciparum, alone and in complex with a polyproline ligand peptide. The most striking feature of Plasmodium profilin is a unique minidomain consisting of a large β-hairpin extension common to all apicomplexan parasites, and an acidic loop specific for Plasmodium species. Reverse genetics in the rodent malaria model, Plasmodium berghei, suggests that profilin is essential for the invasive blood stages of the parasite. Together, our data establish the structural basis for understanding the functions of profilin in the malaria parasite.

Original languageEnglish
Pages (from-to)1638-1648
Number of pages11
JournalStructure
Volume16
Issue number11
DOIs
Publication statusPublished - 12 Nov 2008
Externally publishedYes

Keywords

  • MICROBIO
  • PROTEINS

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