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PMID:23397569
Citation |
Lee, JY, Song, SM, Moon, EK, Lee, YR, Jha, BK, Danne, DB, Cha, HJ, Yu, HS, Kong, HH, Chung, DI and Hong, Y (2013) Cysteine Protease Inhibitor (AcStefin) Is Required for Complete Cyst Formation of Acanthamoeba. Eukaryotic Cell 12:567-74 |
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Abstract |
The encystation of Acanthamoeba leads to the formation of resilient cysts from vegetative trophozoites. This process is essential for parasite survival under unfavorable conditions, such as those associated with starvation, low temperatures, and biocides. Furthermore, cysteine proteases have been implicated in the massive turnover of intracellular components required for encystation. Thus, strict modulation of the activities of cysteine proteases is required to protect Acanthamoeba from intracellular damage. However, mechanisms underlying the control of protease activity during encystation have not been established in Acanthamoeba. In the present study, we identified and characterized Acanthamoeba cysteine protease inhibitor (AcStefin), which was found to be highly expressed during encystation and to be associated with lysosomes by fluorescence microscopy. Recombinant AcStefin inhibited various cysteine proteases, including human cathepsin B, human cathepsin L, and papain. Transfection with small interfering RNA against AcStefin increased cysteine protease activity during encystation and resulted in incomplete cyst formation, reduced excystation efficiency, and a significant reduction in cytoplasmic area. Taken together, these results indicate that AcStefin is involved in the modulation of cysteine proteases and that it plays an essential role during the encystation of Acanthamoeba. |
Links |
PubMed Online version:10.1128/EC.00308-12 |
Keywords |
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Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|
GO:0030414: peptidase inhibitor activity |
ECO:0000314: |
F |
Figure 1B and 1C show that the cysteine protease inhibitor inhibited human cathepsin L, human cathepsin B, and papain enzymes. All of these enzymes are part of the C1 family of cysteine proteinases, therefore showing that the cysteine protease inhibitor inhibits protease, or peptidase, activity. |
complete | ||||
GO:0005764: lysosome |
ECO:0000314: |
C |
Figure two shows that the cysteine protease inhibitor, originally located in the cytoplasm, localizes to the lysosome during cyst formation. |
complete | ||||
enables |
GO:0030414: peptidase inhibitor activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005764: lysosome |
ECO:0000314: direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
See also
References
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