สถาบันวิจัยวิทยาศาสตร์สาธารณสุข

National Institute of Health of Thailand

Authors : Supathra Tiewcharoen1, Watchara Phurttikul1,2, Jundee Rabablert3, Prasert Auewarakul2, Sittiruk Roytrakul4, Pruksawan Chetanachan5, Thassanant Atithep6 and Virach Junnu1

 

Affiliations : 

1 Department of Parasitology,
2 Department of Microbiology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
3 Department of Biology, Faculty of Science, Silpakorn University, Nakhon Pathom;
4 Genome Institute, National Center for Genetic Engineering and Biotechnology, Pathum Thani;
5 National Institute of Health, Department of Medical Sciences, Nonthaburi;
6 Center of Nanoimaging, Faculty of Science, Mahidol University, Bangkok, Thailand

 

Source :

Southeast Asian J Trop Med Public Health Vol.45, No.3, May 2014 Page 537-546.

 

Language :

English

 

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 µg/ml) caused apoptosis  of N. fowleri trophozoites  (2x105 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 µg/ml was not toxic against SK-N-MC cells. Our findings suggest tritrpticin has activity against the surface membrane and nfa1and Mp2CL5 of N. fowleri trophozoites and could be developed as a potential therapeutic agent.

 

Link :

Mahidol : http://www.tm.mahidol.ac.th/seameo/2014-45-3-full/03-6034-14.pdf

NCBI : https://www.ncbi.nlm.nih.gov/pubmed/24974637