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Published on: May 4, 2018
Effect of synthetic antimicrobial peptides on Naegleria fowleri trophozoites
Abstract:
We evaluated the effect of tritrpticin, lactoferrin, killer decapeptide and scrambled peptide in vitro against Naegleria fowleri trophozoites compared with amphotericin B. Tritrpticin (100 microg/ml) caused apoptosis of N. fowleri trophozoites (2x10(5) cells/ml), while lactoferrin, killer decapeptide and scrambled peptide did not. On Gormori trichrome staining, tritrpticin affected the elasticity of the surface membrane and reduced the size of the nuclei of N. fowleri trophozoites. The ultrastructure surface membrane and food cup formation of the trophozoites were 100% inhibited. These results are consistent with inhibition of the nfa1, Mp2CL5 of the treated trophozoite, which plays a role in food cup formation. Tritrpticin 100 microg/ml was not toxic against SK-N-MC cells. Our findings suggest tritrpticin has activity against the surface membrane and nfa1 and Mp2CL5 of N. fowleri trophozoites and could be developed as a potential therapeutic agent.
Insights
Tritrpticin effectively induced apoptosis in Naegleria fowleri trophozoites in vitro. This peptide showed potential as a therapeutic agent by targeting the parasite
Area of Science:
- Parasitology
- Drug Discovery
- Molecular Biology
Background:
- Naegleria fowleri is a free-living amoeba causing primary amoebic meningoencephalitis, a rare but highly fatal infection.
- Limited therapeutic options exist for Naegleria fowleri infections, necessitating the search for novel treatment strategies.
Purpose of the Study:
- To evaluate the in vitro efficacy of tritrpticin against Naegleria fowleri trophozoites.
- To compare tritrpticin's activity with other peptides and amphotericin B.
- To investigate the mechanism of action of tritrpticin on N. fowleri.
Main Methods:
- In vitro testing of tritrpticin, lactoferrin, killer decapeptide, and scrambled peptide against N. fowleri trophozoites.
- Assessment of parasite viability, apoptosis induction, and morphological changes using Gormori trichrome staining.
- Ultrastructural analysis of trophozoite surface membrane and food cup formation.
- Evaluation of tritrpticin's toxicity against human SK-N-MC cells.
Main Results:
- Tritrpticin (100 microg/ml) induced apoptosis in N. fowleri trophozoites, unlike other tested peptides.
- Tritrpticin affected trophozoite surface membrane elasticity and reduced nuclear size.
- Complete inhibition of N. fowleri trophozoite surface membrane ultrastructure and food cup formation was observed.
- Tritrpticin demonstrated no toxicity against human SK-N-MC cells at the tested concentration.
- Results suggest inhibition of nfa1 and Mp2CL5 genes involved in food cup formation.
Conclusions:
- Tritrpticin exhibits significant in vitro activity against Naegleria fowleri trophozoites.
- Tritrpticin targets the parasite's surface membrane and key genes involved in its function.
- Tritrpticin presents a promising candidate for developing new therapeutic agents against N. fowleri infections.
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