Related Experiment Video
Updated: Jun 18, 2025

Deciphering the Molecular Mechanism and Function of Pore-Forming Toxins Using Leishmania major
Published on: October 28, 2022
Apicomplexan Pore-Forming Toxins
1Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan, USA;
Abstract:
Pore-forming toxins (PFTs) are released by one cell to directly inflict damage on another cell. Hosts use PFTs, including members of the membrane attack complex/perforin protein family, to fight infections and cancer, while bacteria and parasites deploy PFTs to promote infection. Apicomplexan parasites secrete perforin-like proteins as PFTs to egress from infected cells and traverse tissue barriers. Other protozoa, along with helminth parasites, utilize saposin-like PFTs prospectively for nutrient acquisition during infection. This review discusses seminal and more recent advances in understanding how parasite PFTs promote infection and describes how they are regulated and fulfill their roles without causing parasite self-harm. Although exciting progress has been made in defining mechanisms of pore formation by PFTs, many open questions remain to be addressed to gain additional key insights into these remarkable determinants of parasitic infections.
Insights
Pore-forming toxins (PFTs) are crucial for host defense and pathogen invasion. This review explores how parasite PFTs facilitate infection, regulate their function, and avoid self-harm, highlighting open questions in parasitic disease research.
Area of Science:
- Molecular Biology
- Parasitology
- Immunology
Background:
- Pore-forming toxins (PFTs) are effector molecules used by both hosts and pathogens.
- Hosts utilize PFTs for defense against infections and cancer.
- Pathogens, including bacteria, parasites, and protozoa, deploy PFTs to establish and promote infections.
Purpose of the Study:
- To review advances in understanding parasite PFTs.
- To elucidate mechanisms by which parasite PFTs promote infection.
- To describe the regulation of parasite PFTs and their role in host-pathogen interactions.
Main Methods:
- Literature review of seminal and recent research on PFTs in parasitic infections.
- Analysis of PFT mechanisms, including pore formation and cellular egress.
- Discussion of regulatory mechanisms controlling PFT activity in parasites.
Main Results:
- Apicomplexan parasites use perforin-like PFTs for cell egress and tissue invasion.
- Protozoa and helminths employ saposin-like PFTs for nutrient acquisition.
- Parasite PFTs are regulated to perform functions without causing self-harm.
Conclusions:
- Parasite PFTs are key virulence factors essential for parasitic infection.
- Understanding PFT regulation and function offers potential therapeutic targets.
- Further research is needed to fully elucidate the complexities of parasite PFTs in disease.
More Related Videos
18:25Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds
Published on: August 25, 2013
10:21Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
Published on: November 16, 2016
Related Concept Videos
Structure of Porins
Coat Assembly and GTPases
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Glycocalyx and its Functions
Fusion of Secretory Vesicles with the Plasma Membrane
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
Receptor-mediated Endocytosis
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
SNAREs and Membrane Fusion
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...