Related Experiment Video

Updated: Feb 27, 2026

A Simple Protocol for Platelet-mediated Clumping of Plasmodium falciparum-infected Erythrocytes in a Resource Poor Setting
07:27

A Simple Protocol for Platelet-mediated Clumping of Plasmodium falciparum-infected Erythrocytes in a Resource Poor Setting

Published on: May 16, 2013

19.1K

An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected

Steven Batinovic1, Emma McHugh1, Scott A Chisholm2

  • 1Department of Biochemistry and Molecular Biology, Bio21 Institute, The University of Melbourne, Parkville, Victoria 3010, Australia.

Nature Communications
|July 11, 2017
PubMed

Insights

Malaria parasite protein PfEMP1 trafficking was investigated. We identified novel protein interactions and found that PV1 depletion alters infected red blood cell properties and reduces virulence.

Area of Science:

  • Cell Biology
  • Parasitology
  • Molecular Biology

Background:

  • Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) is crucial for malaria parasite virulence.
  • Understanding PfEMP1 trafficking is key to developing new antimalarial strategies.

Purpose of the Study:

  • To investigate the physical organization and interacting partners of PfEMP1 trafficking intermediates.
  • To define the EPIC (Exported Protein-Interacting Complex) interactome and its role in PfEMP1 transport.

Main Methods:

  • Used an epitope-tagged minimal PfEMP1 construct (PfEMP1B) in infected red blood cells (RBCs).
  • Investigated protein interactions within the parasitophorous vacuole (PV) and RBC cytoplasm.
  • Employed inducible knockdown of PV1 and deletion studies in Plasmodium berghei.

Main Results:

  • Identified interactions of PfEMP1B with PTEX and the novel EPIC complex in the PV.
  • Discovered interactions with Maurer's clefts and RBC chaperonins in the cytoplasm.
  • Depletion of PV1 led to altered knob morphology, reduced RBC rigidity, and decreased CD36 binding.
  • Deletion of the P. berghei PV1 homolog attenuated parasite virulence in vivo.

Conclusions:

  • PfEMP1 trafficking involves interactions with PTEX, EPIC, Maurer's clefts, and chaperonins.
  • PV1 is essential for PfEMP1 display, RBC modification, and parasite virulence.

More Related Videos

Author Spotlight: Identifying Compensatory Pathways in Malaria Parasites Containing Hypomorphic Allele of Essential Protein Kinases09:13

Author Spotlight: Identifying Compensatory Pathways in Malaria Parasites Containing Hypomorphic Allele of Essential Protein Kinases

Published on: November 22, 2024

1.9K
Evaluation of Extracellular Vesicle Function During Malaria Infection13:45

Evaluation of Extracellular Vesicle Function During Malaria Infection

Published on: February 14, 2018

8.1K

Related Concept Videos

Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
2.5K
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
17.0K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
10.4K
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
7.1K
Intracellular Movement of Viruses and Bacteria01:10

Intracellular Movement of Viruses and Bacteria

Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a...
3.7K
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
2.4K