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Parasite Calcineurin Regulates Host Cell Recognition and Attachment by Apicomplexans
Aditya S Paul1, Sudeshna Saha2, Klemens Engelberg2
1Department of Immunology and Infectious Diseases, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA.
Cell Host & Microbe
|June 30, 2015
Summary
The malaria parasite Plasmodium uses calcineurin, a key signaling enzyme, to attach to host cells. This finding reveals an ancient parasitic mechanism crucial for apicomplexan invasion.
Area of Science:
- Parasitology
- Cell Biology
- Biochemistry
Background:
- Apicomplexan parasites invade host cells via receptor engagement and secreted factors.
- Calcineurin, a calcium-regulated phosphatase, is vital for eukaryotic signal transduction.
Purpose of the Study:
- To investigate the role of parasite calcineurin in host cell invasion by Plasmodium falciparum and Toxoplasma gondii.
- To elucidate the mechanism by which calcineurin facilitates apicomplexan attachment and entry.
Main Methods:
- Reverse-genetic approaches to manipulate calcineurin function.
- Chemical-genetic methods to inhibit calcineurin activity.
- Analysis of host-parasite interactions during invasion.
Main Results:
- Calcineurin is essential for stabilizing extracellular Plasmodium falciparum attachment to host erythrocytes.
- Calcineurin plays a similar role in host cell engagement by Toxoplasma gondii.
- Calcineurin-mediated invasion is linked to host receptors, distinguishing it from receptor-independent adhesion.
Conclusions:
- Parasite calcineurin is a critical regulator of host cell attachment and invasion in apicomplexans.
- Calcineurin's function highlights an ancestral mechanism for parasitism.
- This discovery offers insights into apicomplexan pathogenesis and potential therapeutic targets.
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