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논문 기본 정보

자료유형
학술저널
저자정보
Yeonchul Hong (Kyungpook National University School of Medicine) Jung-Mi Kang (Gyeongsang National University College of Medicine) So-Young Joo (Kyungpook National University School of Medicine) Su-Min Song (Kyungpook National University School of Medicine) Hương Giang Lê (Gyeongsang National University College of Medicine) Thị Lam Thái (Gyeongsang National University College of Medicine) Jinyoung Lee (Gyeongsang National University College of Medicine) Youn-Kyoung Goo (Kyungpook National University School of Medicine) Dong-Il Chung (Kyungpook National University School of Medicine) Woon-Mok Sohn (Gyeongsang National University College of Medicine) Byoung-Kuk Na (Gyeongsang National University College of Medicine)
저널정보
대한기생충학열대의학회 Parasites, Hosts and Diseases The Korean Journal of Parasitology Vol.56 No.5
발행연도
2018.10
수록면
409 - 418 (10page)

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Acanthamoeba spp. are free-living protozoa that are opportunistic pathogens for humans. Cysteine proteases of Acanthamoeba have been partially characterized, but their biochemical and functional properties are not clearly understood yet. In this study, we isolated a gene encoding cysteine protease of A. castellanii (AcCP) and its biochemical and functional properties were analyzed. Sequence analysis of AcCP suggests that this enzyme is a typical cathepsin L family cysteine protease, which shares similar structural characteristics with other cathepsin L-like enzymes. The recombinant AcCP showed enzymatic activity in acidic conditions with an optimum at pH 4.0. The recombinant enzyme effectively hydrolyzed human proteins including hemoglobin, albumin, immunoglobuins A and G, and fibronectin at acidic pH. AcCP mainly localized in lysosomal compartment and its expression was observed in both trophozoites and cysts. AcCP was also identified in cultured medium of A. castellanii. Considering to lysosomal localization, secretion or release by trophozoites and continuous expression in trophozoites and cysts, the enzyme could be a multifunctional enzyme that plays important biological functions for nutrition, development and pathogenicity of A. castellanii. These results also imply that AcCP can be a promising target for development of chemotherapeutic drug for Acanthamoeba infections.

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Abstract
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES

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