Parasites, Hosts and Diseases

The Korea Society for Parasitology and Tropical Medicine (대한기생충학·열대의학회)
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Identification of Protein Arginine Methyltransferase 5 as a Regulator for Encystation of Acanthamoeba

  • Moon, Eun-Kyung (Department of Medical Zoology, Kyung Hee University School of Medicine) ;
  • Hong, Yeonchul (Department of Parasitology and Tropical Medicine, Kyungpook National University School of Medicine) ;
  • Chung, Dong-Il (Department of Parasitology and Tropical Medicine, Kyungpook National University School of Medicine) ;
  • Goo, Youn-Kyoung (Department of Parasitology and Tropical Medicine, Kyungpook National University School of Medicine) ;
  • Kong, Hyun-Hee (Department of Parasitology, Dong-A University College of Medicine)
  • Received : 2015.09.14
  • Accepted : 2015.12.29
  • Published : 2016.04.30
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Abstract

Encystation is an essential process for Acanthamoeba survival under nutrient-limiting conditions and exposure to drugs. The expression of several genes has been observed to increase or decrease during encystation. Epigenetic processes involved in regulation of gene expression have been shown to play a role in several pathogenic parasites. In the present study, we identified the protein arginine methyltransferase 5 (PRMT5), a known epigenetic regulator, in Acanthamoeba castellanii. PRMT5 of A. castellanii (AcPRMT5) contained domains found in S-adenosylmethionine-dependent methyltransferases and in PRMT5 arginine-N-methyltransferase. Expression levels of AcPRMT5 were increased during encystation of A. castellanii. The EGFP-PRMT5 fusion protein was mainly localized in the nucleus of trophozoites. A. castellanii transfected with siRNA designed against AcPRMT5 failed to form mature cysts. The findings of this study lead to a better understanding of epigenetic mechanisms behind the regulation of encystation in cyst-forming pathogenic protozoa.

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References

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