We purified and characterized a serine proteinase secreted by Acanthamoeba healyi to evaluate it as a possible virulence factor in the pathogenesis of granulomatous amoebic encephalitis (GAE). Ammonium sulfate precipitated culture supernatant of A. healyi OC-3A strain was purified by chromatography on CM-Sepharose, Sephacryl-S200, and Q-2 anion-exchange columns. The purified 33-kDa enzyme had a pH optimum of 8.0 and a temperature optimum of 40 C. Phenylmethylsulfonylfluoride and diisopropyl fluorophosphate, serine proteinase inhibitors, diminished activity of the enzyme to near zero. In addition to types I and IV collagen and fibronectin, the main components of the extracellular matrix, other proteins such as fibrinogen, IgG, IgA, albumin, and hemoglobin were also degraded by the enzyme. The broad substrate specificity of this secreted serine proteinase suggests that it may play an important role in pathogenesis of GAE by A. healyi.
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February 2000
Research Article|
February 01 2000
PURIFICATION AND CHARACTERIZATION OF A SECRETORY SERINE PROTEINASE OF ACANTHAMOEBA HEALYI ISOLATED FROM GAE
Hyun-Hee Kong;
Hyun-Hee Kong
Department of Parasitology, Kyungpook National University, School of Medicine, Taegu 700-422, Korea
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Tae-Ho Kim;
Tae-Ho Kim
Department of Parasitology, Kyungpook National University, School of Medicine, Taegu 700-422, Korea
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Dong-Il Chung
Dong-Il Chung
Department of Parasitology, Kyungpook National University, School of Medicine, Taegu 700-422, Korea
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J Parasitol (2000) 86 (1): 12–17.
Citation
Hyun-Hee Kong, Tae-Ho Kim, Dong-Il Chung; PURIFICATION AND CHARACTERIZATION OF A SECRETORY SERINE PROTEINASE OF ACANTHAMOEBA HEALYI ISOLATED FROM GAE. J Parasitol 1 February 2000; 86 (1): 12–17. doi: https://doi.org/10.1645/0022-3395(2000)086[0012:PACOAS]2.0.CO;2
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