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Original Article

Phospholipase Activities in Clinical and Environmental Isolates of Acanthamoeba

Abdul Matin1, Suk-Yul Jung2
The Korean Journal of Parasitology 2011;49(1):1-8.
Published online: March 18, 2011

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Corresponding author (syjung@nsu.ac.kr)
• Received: September 29, 2010   • Revised: November 30, 2010   • Accepted: December 16, 2010

© 2011, Korean Society for Parasitology

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Phospholipase Activities in Clinical and Environmental Isolates of Acanthamoeba
Korean J Parasitol. 2011;49(1):1-8.   Published online March 18, 2011
DOI: https://doi.org/10.3347/kjp.2011.49.1.1
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Phospholipase Activities in Clinical and Environmental Isolates of Acanthamoeba
Korean J Parasitol. 2011;49(1):1-8.   Published online March 18, 2011
DOI: https://doi.org/10.3347/kjp.2011.49.1.1
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Phospholipase Activities in Clinical and Environmental Isolates of Acanthamoeba
Image Image Image Image Image Image
Fig. 1 Acanthamoeba exhibiting PLA2 activities. Both the encephalitis (A) and the environmental (C) isolates exhibited optimal, while the keratitis isolate (B) exhibited the least PLA2 activities. Results are representative of 3 independent experiments performed in triplicate. Bars represent standard errors.
Fig. 2 Clinical and environmental Acanthamoeba isolates exhibiting PLD activities. As for PLA2, both the encephalitis (A) and the environmental (C) isolates exhibited optimal, while the keratitis isolate (B) exhibited the least PLD activities. Results are representative of 3 independent experiments performed in triplicate. Bars represent standard errors.
Fig. 3 Acanthamoeba exhibiting optimal phospholipase activities at 37℃. To determine optimal temperatures of Acanthamoeba phospholipases, assays were performed at various temperatures using Acanthamoeba lysates (5×106 amoebae). Note that all Acanthamoeba isolates tested exhibit optimal PLA2 (A) and PLD (B) activities at 37℃ indicating their physiological relevance. Results are representative of 3 independent experiments performed in triplicate. Bars represent standard errors.
Fig. 4 Acanthamoeba exhibiting optimal phospholipase activities at neutral pH. To determine optimal pH of Acanthamoeba phospholipases, assays were performed at various pH using Acanthamoeba lysates (5×106 amoebae). Note that all Acanthamoeba isolates tested exhibit optimal PLA2 (A) and PLD (B) activities at neutral pH indicating their physiological relevance. Results are representative of 3 independent experiments performed in triplicate. Bars represent standard errors.
Fig. 5 Phospholipase inhibitors blocking the environmental isolate-mediated binding to HBMEC but not the clinical isolates-mediated binding. The results revealed that both phospholipase inhibitors restricted environmental isolate (C)-mediated binding to HBMEC. However, neither inhibitors had any effects on the clinical isolates (A, T1; B, T4). Results are representative of 3 independent experiments performed in duplicates. Bars represent standard errors.
Fig. 6 Compound 48/80 partially inhibiting encephalitis isolate-mediated HBMEC cytotoxicity. The results revealed that cytidine 5'-diphosphocholine had no significant effect on Acanthamoeba-mediated HBMEC cytotoxicity. Similarly, compound 48/80 had no effect on Acanthamoeba keratitis isolate (B) but partially inhibited encephalitis isolate (A)-mediated HBMEC cytotoxicity. C is a environmental isolate of T7. Results are representative of 3 independent experiments performed in duplicates. Bars represent standard errors.

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Phospholipase Activities in Clinical and Environmental Isolates of Acanthamoeba
PHD : Parasites, Hosts and Diseases

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