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Original Article

Comparison of specific activity and cytopathic effects of purified 33 kDa serine proteinase from Acanthamoeba strains with different degree of virulence

Won-Tae Kim1, Hyun-Hee Kong1, Young-Ran Ha1, Yeon-Chul Hong1, Hae Jin Jeong2, Hak Sun Yu2, Dong-Il Chung1
The Korean Journal of Parasitology 2006;44(4):321-330.
Published online: December 20, 2006

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Corresponding author (dichung@knu.ac.kr)
• Received: June 20, 2006   • Accepted: November 13, 2006

Copyright © 2006 by The Korean Society for Parasitology

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Comparison of specific activity and cytopathic effects of purified 33 kDa serine proteinase from Acanthamoeba strains with different degree of virulence
Korean J Parasitol. 2006;44(4):321-330.   Published online December 20, 2006
DOI: https://doi.org/10.3347/kjp.2006.44.4.321
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Comparison of specific activity and cytopathic effects of purified 33 kDa serine proteinase from Acanthamoeba strains with different degree of virulence
Korean J Parasitol. 2006;44(4):321-330.   Published online December 20, 2006
DOI: https://doi.org/10.3347/kjp.2006.44.4.321
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Comparison of specific activity and cytopathic effects of purified 33 kDa serine proteinase from Acanthamoeba strains with different degree of virulence
Image Image Image Image Image Image Image Image Image
Fig. 1 A. Light microscopic pictures of Giemsa stained human corneal cells after coculture with trophozoites of the 3 strains of Acanthamoeba, OC-3A, KA/E2 and Neff, with or without serine proteinase inhibitor, PMSF. B. Bar graph showing calculated cytopathic effects of the 3 strains.
Fig. 2 Anion exchange column chromatograms of proteinase purification from the culture supernatant of Acanthamoeba strains, OC-3A, KA/E2 and Neff.
Fig. 3 SDS-PAGE of the purified enzyme of the 3 strains, OC-3A, KA/E2 and Neff in a 4-20% gradient acrylamide gel. A single protein band stained with Coomassie blue is observed with a size of approximately 33 kDa in 3 strains. Lane: M, standard size marker; 1, OC-3A; 2, KA/E2; 3, Neff strain.
Fig. 4 Proteolytic activity of the purified 33 kDa serine proteinase of Acanthamoeba strains, OC-3A, KA/E2 and Neff against extracellular matrix proteins. M, standard size marker; C, reaction mixture without enzyme; Reaction mixtures for each strain were incubated for 30'', 10', 30'.
Fig. 5 Proteolytic activity of the purified 33 kDa serine proteinase of Acanthamoeba strains, OC-3A, KA/E2 and Neff against host serum proteins. M, standard marker; C, reaction mixture without enzyme; Reaction mixtures for each strain were incubated for 30'', 10', 30'.
Fig. 6 Proteolytic activity of the purified 33 kDa serine proteinase of Acanthamoeba strains, OC-3A, KA/E2 and Neff against immunoglobulins. M, standard marker; C, reaction mixture without enzyme; Reaction mixtures for each strain were incubated for 30'', 10', 30'.
Fig. 7 Gelatin zymogram of the purified enzyme of Acanthamoeba strains, OC-3A, KA/E2 and Neff. Acrylamide gel copolymerized with gelatin was stained with Commassie blue after incubation with the purified serine proteinase loaded in the hole of the gel.
Fig. 8 Cytopathic effects of the purified 33 kDa enzymes of Acanthamoeba strains, OC-3A, KA/E2 and Neff on HCE cell. Cytopathy was determined by staining the culture plate with Giemsa after incubation with the purified enzyme.
Fig. 9 Gelatin zymogram of culture supernatant of Acanthamoeba strains, OC-3A, KA/E2 and Neff. Acrylamide gel copolymerized with gelatin was stained with Commassie blue after incubation with anti-serum against purified 33 kDa serine proteinase or without anti-serum.

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Fig. 8

Fig. 9

Comparison of specific activity and cytopathic effects of purified 33 kDa serine proteinase from Acanthamoeba strains with different degree of virulence
Step Total protein (mg)
 Total activity (nmol/min)
 Specific activity (nmol/min/mg)
 Purification (fold)
 Yield (%)
OC-3A KA/E2 Neff OC-3A KA/E2 Neff OC-3A KA/E2 Neff OC-3A KA/E2 Neff OC-3A KA/E2 Neff
Culture supernatant 135.0 156.3 246.1 1836.3 813.0 516.7 13.6 5.2 2.1 1.0 1.0 1.0 100.0 100.0 100.0
Amonium sulfate percipitation 25.3 28.0 30.0 1120.7 770 426.0 44.3 27.5 14.2 3.3 5.3 6.8 61.0 94.7 82.4
CM-Sepharose 8.0 3.7 6.5 763.0 243.1 226.9 95.5 66.6 34.9 7.0 12.8 16.8 41.6 29.9 43.9
Sephacryl S-200 0.4 0.3 0.4 364.5 142.6 120.6 1041.4 570.3 335.0 76.6 109.7 159.5 19.8 17.5 23.3
Q-anion exchange 0.04 0.03 0.02 45.8 26.1 10.6 1145.0 814.4 704.6 84.2 156.6 335.5 2.5 3.2 2.0
Inhibitor/Activitor Final concentration Activity as percentage of control
OC-3A KA/E2 Neff
Control (none) 100.0 100.0 100.0
Serine Class
 PMSF 1.0 mM 6.1 6.9 7.3
 DFP 1.0 mM 15.3 15.9 16.7
Cystein Class
 E-64 10.0 μg/ml 115.8 96.7 93.3
 DTT 1.0 mM 111.9 85.8 102.0
Aspartic Class
 Pepstatin A 1.0 μg/ml 107.9 97.4 96.7
Metallo Class
 EDTA 1.0 mM 102.6 108.3 90.3
 1,10-Phenanthroline 1.0 mM 91.8 107.2 93.3
Table 1. Purification steps of 33 kDa serine proteinase from culture supernatant of 3 strains of Acanthamoeba, OC-3A, KA-E2 and Neff
Table 2. Effects of proteinase inhibitors and activators on the activity of the purified enzymes of 3 strains of Acanthamoeba

Table 1.

Table 2.

PHD : Parasites, Hosts and Diseases

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