Related Experiment Video

Updated: Jul 31, 2026

Methods to Investigate the Regulatory Role of Small RNAs and Ribosomal Occupancy of Plasmodium falciparum
10:22

Methods to Investigate the Regulatory Role of Small RNAs and Ribosomal Occupancy of Plasmodium falciparum

Published on: December 4, 2015

9.4K

Proteomic analysis of exported chaperone/co-chaperone complexes of P. falciparum reveals an array of complex

Qi Zhang1, Cheng Ma2, Alexander Oberli3,4

  • 1Department of Parasitology, Philipps University Marburg, Marburg, Germany.

Scientific Reports
|February 21, 2017
PubMed

Insights

Malaria parasites export proteins to alter host cells, causing disease. Researchers identified novel high-molecular-weight protein complexes involving exported Hsp40 and Hsp70, potentially key to this modification process.

Area of Science:

  • Cell biology
  • Parasitology
  • Molecular biology

Background:

  • Malaria parasites extensively modify infected human erythrocytes, leading to disease pathology.
  • Exported parasite proteins mediate these modifications, but the molecular machinery remains largely unknown.
  • Heat shock proteins (Hsp40 and Hsp70) are among the exported proteins implicated in host cell processes.

Purpose of the Study:

  • To identify and characterize protein complexes involving exported Hsp40 (PFE55) and Hsp70 (PfHsp70x) in Plasmodium falciparum-infected erythrocytes.
  • To elucidate the molecular players and potential functions of these protein complexes in host cell modification.

Main Methods:

  • Chemical cross-linking followed by mass spectrometry to isolate protein complexes.
  • Immunoblotting to confirm the presence and interactions of specific proteins.
  • Analysis of protein complexes within infected erythrocytes and the parasitophorous vacuole.

Main Results:

  • Both exported PFE55 (Hsp40) and PfHsp70x (Hsp70) exist within high molecular weight protein complexes.
  • These complexes are localized within the infected erythrocyte and the parasitophorous vacuole.
  • PfHsp70x was found associated with components of PTEX, a putative protein translocon in the parasitophorous vacuole membrane.

Conclusions:

  • The infected erythrocyte contains numerous high molecular weight protein complexes involving exported Hsp40 and Hsp70.
  • These complexes, including potential interactions with PTEX, are likely involved in the parasite-mediated modification of the human host cell.
  • Further investigation is warranted to fully understand the role of these complexes in malaria pathogenesis.

More Related Videos

Plasmodium falciparum Gametocyte Culture and Mosquito Infection Through Artificial Membrane Feeding09:23

Plasmodium falciparum Gametocyte Culture and Mosquito Infection Through Artificial Membrane Feeding

Published on: July 3, 2020

8.5K
Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections07:14

Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections

Published on: March 8, 2024

2.0K

Related Concept Videos

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...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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.
Malaria01:29

Malaria

Malaria pathogenesis in humans reflects a delicate interplay between parasite biology and host response. Clinical illness reflects a host’s immune response to the parasite’s asexual replication cycle, which is often asymptomatic in individuals with partial immunity. From the parasite's perspective, transmission between mosquito and human with minimal host pathology is evolutionarily advantageous. Among the six Plasmodium species infecting humans, P. falciparum and P. vivax dominate in global...