Related Experiment Video
Updated: Dec 21, 2025

Author Spotlight: Identifying Compensatory Pathways in Malaria Parasites Containing Hypomorphic Allele of Essential Protein Kinases
Published on: November 22, 2024
Directing traffic: Chaperone-mediated protein transport in malaria parasites
Anat Florentin1,2, David W Cobb1,2, Heather M Kudyba1,2
1Department of Cellular Biology, University of Georgia, Athens, Georgia, USA.
Abstract:
The ability of eukaryotic parasites from the phylum Apicomplexa to cause devastating diseases is predicated upon their ability to maintain faithful and precise protein trafficking mechanisms. Their parasitic life cycle depends on the trafficking of effector proteins to the infected host cell, transport of proteins to several critical organelles required for survival, as well as transport of parasite and host proteins to the digestive organelles to generate the building blocks for parasite growth. Several recent studies have shed light on the molecular mechanisms parasites utilise to transform the infected host cells, transport proteins to essential metabolic organelles and for biogenesis of organelles required for continuation of their life cycle. Here, we review key pathways of protein transport originating and branching from the endoplasmic reticulum, focusing on the essential roles of chaperones in these processes. Further, we highlight key gaps in our knowledge that prevents us from building a holistic view of protein trafficking in these deadly human pathogens.
Insights
Apicomplexa parasites rely on precise protein transport for survival and disease. Understanding these mechanisms, particularly endoplasmic reticulum pathways and chaperones, is crucial for combating these pathogens.
Area of Science:
- Parasitology
- Cell Biology
- Molecular Biology
Background:
- Apicomplexa parasites cause severe diseases by manipulating host cells.
- Efficient protein trafficking is essential for parasite survival, growth, and pathogenesis.
- Key processes include effector protein delivery, organelle transport, and digestive organelle function.
Purpose of the Study:
- To review protein transport pathways in Apicomplexa, originating from the endoplasmic reticulum.
- To highlight the critical roles of molecular chaperones in these trafficking routes.
- To identify knowledge gaps hindering a comprehensive understanding of protein trafficking in these parasites.
Main Methods:
- Literature review of recent studies on Apicomplexa protein trafficking.
- Focus on pathways branching from the endoplasmic reticulum.
- Emphasis on the involvement of chaperones.
Main Results:
- Recent studies illuminate molecular mechanisms for host cell transformation and organelle biogenesis.
- Key pathways involve effector protein transport and delivery to digestive organelles.
- Chaperones play essential roles in ensuring correct protein folding and transport.
Conclusions:
- Protein trafficking is fundamental to Apicomplexa pathogenesis.
- Further research is needed to fully elucidate endoplasmic reticulum-derived pathways and chaperone functions.
- A holistic view of protein trafficking is critical for developing therapeutic strategies against these deadly pathogens.
More Related Videos
07:27A Simple Protocol for Platelet-mediated Clumping of Plasmodium falciparum-infected Erythrocytes in a Resource Poor Setting
Published on: May 16, 2013
10:22Methods to Investigate the Regulatory Role of Small RNAs and Ribosomal Occupancy of Plasmodium falciparum
Published on: December 4, 2015
Related Concept Videos
Overview of Protein Sorting and Transport
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation. In gated transport, folded...
Protein Transport to the Inner Chloroplast Membrane
Protein Transport to the Outer Chloroplast Membrane
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.
Molecular Chaperones and Protein Folding
The...
Cotranslational Protein Translocation
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Protein Transport to the Stroma
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...