Interaction of Plasmodium falciparum M18 Aminopeptidase with Human Erythrocyte Spectrin
Author Information
Author(s): Lauterbach Sonja B, Coetzer Theresa L
Primary Institution: National Health Laboratory Service, School of Pathology, University of the Witwatersrand
Hypothesis
The study investigates the interaction between the M18 aspartyl aminopeptidase of Plasmodium falciparum and human erythrocyte spectrin.
Conclusion
The study found that PfM18AAP interacts with erythrocyte spectrin and other membrane proteins, suggesting its multifunctional role in the erythrocyte host.
Supporting Evidence
- PfM18AAP has a molecular weight of ~67 kDa and shows maximum enzymatic activity at pH 7.5 and 37°C.
- Blot overlays confirmed that PfM18AAP binds to spectrin and other erythrocyte membrane proteins.
- The spectrin-binding region of PfM18AAP is not found in human or other Plasmodium species homologues.
Takeaway
This study shows that a protein from the malaria parasite can stick to parts of our red blood cells, which might help the parasite survive and grow.
Methodology
Recombinant PfM18AAP was produced in E. coli, purified, and its interactions with erythrocyte proteins were analyzed using various biochemical assays.
Digital Object Identifier (DOI)
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