A bacterial phosphatase-like enzyme of the malaria parasite Plasmodium falciparum possesses tyrosine phosphatase activity and Is implicated in the regulation of band 3 dynamics during parasite invasion

Sebastian Fernandez-Pol, Zdenek Slouka, Souvik Bhattacharjee, Yana Fedotova, Stefan Freed, Xiuli An, Anthony A. Holder, Estela Campanella, Philip S. Low, Narla Mohandas, Kasturi Haldara

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Eukaryotic parasites of the genus Plasmodium cause malaria by invading and developing within host erythrocytes. Here, we demonstrate that PfShelph2, a gene product of Plasmodium falciparum that belongs to the Shewanella-like phosphatase (Shelph) subfamily, selectively hydrolyzes phosphotyrosine, as shown for other previously studied Shelph family members. In the extracellular merozoite stage, PfShelph2 localizes to vesicles that appear to be distinct from those of rhoptry, dense granule, or microneme organelles. During invasion, PfShelph2 is released from these vesicles and exported to the host erythrocyte. In vitro, PfShelph2 shows tyrosine phosphatase activity against the host erythrocyte protein Band 3, which is the most abundant tyrosine-phosphorylated species of the erythrocyte. During P. falciparum invasion, Band 3 undergoes dynamic and rapid clearance from the invasion junction within 1 to 2 s of parasite attachment to the erythrocyte. Release of Pfshelph2 occurs after clearance of Band 3 from the parasite-host cell interface and when the parasite is nearly or completely enclosed in the nascent vacuole. We propose a model in which the phosphatase modifies Band 3 in time to restore its interaction with the cytoskeleton and thus reestablishes the erythrocyte cytoskeletal network at the end of the invasion process.

Original languageEnglish (US)
Pages (from-to)1179-1191
Number of pages13
JournalEukaryotic Cell
Volume12
Issue number9
DOIs
StatePublished - Sep 2013

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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