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Identification of peptides targeting the surface of Plasmodium falciparum-infected erythrocytes using a phage display
Keiko Eda1, Shigetoshi Eda, Irwin W Sherman
1Department of Biology, University of California, Riverside, California 92521, USA.
Abstract:
Drastic changes in the plasma membrane of Plasmodium falciparum-infected red blood cells (iRBCs) make the surface of iRBCs distinct from that of the uninfected erythrocyte. To identify small peptides that would specifically recognize the altered surface of iRBCs, we screened a phage display peptide library (PDL) on the surface of iRBCs. After the sixth panning of the PDL, eight phage clones of 18 sequenced clones had the same sequence, LVDAAAL (named P1) and specific binding of P1 to the surface of iRBCs was confirmed using phage expressing P1 peptides and synthetic P1 peptide. When P1 peptide was conjugated with a peptide having moderate hemolytic activity, the peptide conjugate inhibited the growth of intracellular parasites in a dose-dependent manner, whereas control peptides were without effect. Our results demonstrate that the P1 peptide may be a lead compound for the development of anti-malarial agents targeting the surface of iRBCs.
Insights
Researchers identified a novel peptide (P1) that specifically binds to malaria-infected red blood cells. This P1 peptide, when combined with another, inhibits parasite growth, showing potential as a new anti-malarial drug lead.
Area of Science:
- Malariology
- Medicinal Chemistry
- Molecular Biology
Background:
- Infected red blood cells (iRBCs) exhibit distinct surface changes compared to uninfected erythrocytes.
- Identifying specific surface markers on iRBCs is crucial for developing targeted therapies.
Purpose of the Study:
- To discover small peptides that specifically recognize and bind to the altered surface of Plasmodium falciparum-infected red blood cells.
- To evaluate the anti-malarial potential of identified peptides.
Main Methods:
- Screening of a phage display peptide library (PDL) against iRBCs.
- Confirmation of specific peptide binding using phage display and synthetic peptides.
- Assessment of parasite growth inhibition by peptide conjugates.
Main Results:
- A specific peptide sequence, LVDAAAL (P1), was identified with high affinity for iRBC surfaces.
- The P1 peptide, when conjugated with a hemolytic peptide, demonstrated dose-dependent inhibition of intracellular parasite growth.
- Control peptides showed no significant effect on parasite growth.
Conclusions:
- The P1 peptide is a promising lead compound for developing novel anti-malarial agents.
- Targeting the distinct surface of iRBCs offers a viable strategy for malaria treatment.
- Further development of P1 peptide conjugates could lead to effective anti-malarial therapies.
