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Original Article

Molecular and Biochemical Properties of a Cysteine Protease of Acanthamoeba castellanii

Yeonchul Hong1,*, Jung-Mi Kang2,3, So-Young Joo1, Su-Min Song1, Hương Giang Lê2,3, Thị Lam Thái2,3, Jinyoung Lee2, Youn-Kyoung Goo1, Dong-Il Chung1, Woon-Mok Sohn2, Byoung-Kuk Na2,3,*
The Korean Journal of Parasitology 2018;56(5):409-418.
Published online: October 31, 2018

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*Corresponding authors (ychong@knu.ac.kr; bkna@gnu.ac.kr)
• Received: September 10, 2018   • Revised: September 10, 2018   • Accepted: September 27, 2018

Copyright © 2018 by The Korean Society for Parasitology and Tropical Medicine

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Molecular and Biochemical Properties of a Cysteine Protease of Acanthamoeba castellanii
Korean J Parasitol. 2018;56(5):409-418.   Published online October 31, 2018
DOI: https://doi.org/10.3347/kjp.2018.56.5.409
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Molecular and Biochemical Properties of a Cysteine Protease of Acanthamoeba castellanii
Korean J Parasitol. 2018;56(5):409-418.   Published online October 31, 2018
DOI: https://doi.org/10.3347/kjp.2018.56.5.409
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Molecular and Biochemical Properties of a Cysteine Protease of Acanthamoeba castellanii
Image Image Image Image Image
Fig. 1 Sequence alignment and phylogenetic analysis. (A) Multiple sequence alignment of AcCP (EF053509) with the cysteine proteases of other protozoan parasites and human including Acanthamoeba healyi (AF462309), Entamoeba histolytica (X87214), Toxoplasma gondii (XP_002371694), Plasmodium falciparum (XP_001347836) and human (M20498). The dashes represent gaps introduced to maximize alignment. The ERFNIN motif, which is well conserved in the cathepsin L-like subgroup, was marked with closed blue circles. The GNFD motif was shown as red triangles. The predicted signal peptide region was shown with a black line. Red asterisks indicate the conserved active site residues. (B) Genomic DNA structure. AcCP gene was interrupted by an intron with the size of 131 bp in genomic DNA sequence. (C) Phylogenetic analysis. The tree was built with the neighbor-joining method using the MEGA4 program. Numbers on the branches indicate bootstrap proportions (1,000 replicates). Full-length amino acid sequences for each gene were analyzed.
Fig. 2 Production and refolding of rAcCP. (A) Expression and production of rAcCP. Proteins were analyzed by SDS-PAGE and stained with Coomassie blue. Lane 1, Escherichia coli lysate control (30 μg); lane 2, isopropyl-1-thio-β-D-galactopyranoside-induced E. coli lysate (30 μg); lane 3, rAcCP purified by Ni–NTA affinity chromatography (5 μg). Lane M, molecular size marker proteins. (B) Autocatalytic processing of refolded rAcCP. The purified rAcCP was refolded and incubated at different pHs. Aliquots were collected at indicated times and were analyzed by 12% SDS-PAGE with Coomassie staining. (C) Enzyme activity assay. The refolded rAcCP was incubated in different pH buffers and enzyme activity was assayed with Z-FR-MCA as a substrate.
Fig. 3 Characterization of biochemical properties of rAcCP. Biochemical properties of fully activated rAcCP were analyzed. (A) Optimal pH. Enzyme activity was assayed in various pH buffers ranging from pH 3.5–7.5. Maximal activity was shown as 100%. (B) Enzyme stability. rAcCP was incubated in various pH buffers at 37°C for the indicated time and residual enzyme activity was assayed. All the assays were performed with Z-LR-MCA as a substrate. pH 4.0 (▲), pH 5.0 (■), pH 6.0 (□), pH 7.0 (●), and pH 8.0 (○). (C) Degradation of human proteins by rAcCP. Each macromolecular protein substrate was incubated with rAcCP (100 nM) in 50 mM sodium acetate (pH 4.0) or 50 mM sodium phosphate (pH 7.0) in the presence of 1 mM GSH for 3 hr at 37°C and analyzed by SDS-PAGE. Lane C, protein without rAcCP; lanes 4 and 7, incubated with rAcCP at pH 4.0 and pH 7.0, respectively.
Fig. 4 Cellular localization of AcCP. Trophozoites of A. castellanii were transfected with pGAPDH-AcCP-EGFP to analyze locations of AcCP-EGFP expression in the amoeba. The transfected A. castellanii trophozoites (A–D) were transferred into encystation medium, incubated for 24 hr (E–H), 48 hr (I–L), and 72 hr (M–P), and then examined under a fluorescence microscope (green). Lysosomes and autophagolysosomes were visualized by counter-staining with LysoTracker Red (red), and the resulting images were merged (yellow). BF denotes bright-field images. Scale bars indicate 5 μm.
Fig. 5 Expression profiles of AcCP. (A) Expression profile of AcCP in different developmental stages of A. castellanii. A. castellanii trophozoites were encysted in encystation medium for 24, 48, or 72 hr. Lysates of A. castellanii trophozoites and cysts collected at each time point were separated by SDS-PAGE, transferred to PVDF membrane and probed with anti-AcCP and anti-actin. (B) Secretion of AcCP. The trophozoites were incubated in PYG medium at 25°C for 24, 48, or 72 hr and the cultured medium were collected at indicated time, respectively. Western blot analysis for cultured medium was performed with anti-AcCP. T, lysates of A. castellanii trophozoites.

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Fig. 5

Molecular and Biochemical Properties of a Cysteine Protease of Acanthamoeba castellanii

Kinetic parameters for AcCP

Substrate kcat/Km (M−1s−1)
Z-FR-MCA 6.2×103
Z-LR-MCA 2.1×104
Z-RR-MCA NH

NH, no hydrolysis.

Table 1 Kinetic parameters for AcCP

NH, no hydrolysis.

Table 1

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