This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Moon, E.-K.
Right arrow Articles by Kong, H.-H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moon, E.-K.
Right arrow Articles by Kong, H.-H.

 Previous Article  |  Next Article 

Eukaryotic Cell, September 2008, p. 1513-1517, Vol. 7, No. 9
1535-9778/08/$08.00+0     doi:10.1128/EC.00068-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Characterization of a Serine Proteinase Mediating Encystation of Acanthamoeba{triangledown}

Eun-Kyung Moon, Dong-Il Chung, Yeon-Chul Hong, and Hyun-Hee Kong*

Department of Parasitology, Kyungpook National University School of Medicine, Taegu, South Korea

Received 20 February 2008/ Accepted 21 July 2008

Members of the genus Acanthamoeba, amphizoic protozoan parasites, are causative agents of granulomatous amoebic encephalitis and amoebic keratitis. Proteinases play a role in various biologic actions in Acanthamoeba, including host tissue destruction, pathogenesis, and digestion of phagocytosed food. Interestingly, we found that encystation of Acanthamoeba was inhibited by the serine proteinase inhibitor phenylmethanesulfonyl fluoride. In this study, we characterize a serine proteinase that is involved in mediating the encystation of Acanthamoeba. This encystation-mediating serine proteinase (EMSP) is shown to be highly expressed during encystation by real-time PCR and Western blot analysis. Chemically synthesized small interfering RNA against EMSP inhibited the expression of EMSP mRNA and significantly reduced the encystation efficiency of Acanthamoeba. An EMSP-enhanced green fluorescent protein fusion protein localized to vesicle-like structures within the amoeba. Using LysoTracker analysis, these vesicular structures were confirmed to be lysosomes. After incubation of the transfected amoeba in encystment media, small fluorescent vesicle-like structures gathered and formed ball-like structures, which were identified as colocalizing with the autophagosome. Taken together, these results indicate that EMSP plays an important role in the differentiation of Acanthamoeba by promoting autolysis.

* Corresponding author. Mailing address: Department of Parasitology, Kyungpook National University School of Medicine, 101 Dongin-dong, Joong-gu, Taegu 700-422, South Korea. Phone: 82 53 420 4882. Fax: 82 53 422 9330. E-mail: hhkong{at}mail.knu.ac.kr

{triangledown} Published ahead of print on 1 August 2008.

Eukaryotic Cell, September 2008, p. 1513-1517, Vol. 7, No. 9
1535-9778/08/$08.00+0     doi:10.1128/EC.00068-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • El-Etr, S. H., Margolis, J. J., Monack, D., Robison, R. A., Cohen, M., Moore, E., Rasley, A. (2009). Francisella tularensis Type A Strains Cause the Rapid Encystment of Acanthamoeba castellanii and Survive in Amoebal Cysts for Three Weeks Postinfection. Appl. Environ. Microbiol. 75: 7488-7500 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»