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Acta tropica v.167, 2017년, pp.99 - 107   SCI SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

A cysteine protease from Spirometra erinaceieuropaei plerocercoid is a critical factor for host tissue invasion and migration

Tsubokawa, Daigo (Department of Molecular and Cellular Parasitology, Kitasato University Graduate School of Medical Sciences, 1-15-1 Kitasato, Minami, Sagamihara, Kanagawa 252-0373, Japan ); Hatta, Takeshi (Department of Molecular and Cellular Parasitology, Kitasato University Graduate School of Medical Sciences, 1-15-1 Kitasato, Minami, Sagamihara, Kanagawa 252-0373, Japan ); Maeda, Hiroki (Department of Parasitology, Kitasato University School of Medicine, 1-15-1 Kitasato, Minami, Sagamihara, Kanagawa 252-0374, Japan ); Mikami, Fusako (Department of Parasitology, Kitasato University School of Medicine, 1-15-1 Kitasato, Minami, Sagamihara, Kanagawa 252-0374, Japan ); Goso, Yukinobu (Department of Biochemistry, Kitasato University School of Medicine, 1-15-1 Kitasato, Minami, Sagamihara, Kanagawa 252-0374, Japan ); Nakamura, Takeshi (Department of Parasitology, Kitasato University School of Medicine, 1-15-1 Kitasato, Minami, Sagamihara, Kanagawa 252-0374, Japan ); Alim, M. Abdul (Department of Parasitology, Faculty of Veterinary Science, Bangladesh Agricultural University, Mymensingh 2202, Bangladesh ); Tsuji, Naotoshi (Dep );
  • 초록  

    Abstract Sparganosis in humans caused by the plerocercoid larvae of Spirometra erinaceieuropaei is found worldwide, especially in Eastern Asia and the Far East. Previous studies have suggested that dissolution of plerocercoid body, plerocercoid invasion of host tissue, and migration are important processes for sparganosis progression. However, the mechanisms underlying these processes have yet to be determined. Here, we demonstrated the enzymatic property and involvement of a native 23kDa cysteine protease (Se23kCP), purified from plerocercoids, in sparganosis pathogenesis. Se23kCP is mature protease consisting of 216 amino acids and has a high sequence similarity with cathepsin L in various organisms. Se23kCP conjugated with N -glycans, which have a core fucose residue. Both cysteine and serine protease-specific activities were determined in Se23kCP and their optimal pHs were found to be different, indicating that Se23kCP has a wide range of substrate specificity. Se23kCP was secreted from tegumental vacuoles of the plerocercoid to host subcutaneous tissues and degraded human structural proteins, such as collagen and fibronectin. In addition, the plerocercoid body was lysed by Se23kCP, which facilitated larval invasion of host tissue. Our findings suggest that Se23kCP induces host tissue invasion and migration, and might be an essential molecule for sparganosis onset and progression. Highlights A cysteine protease (Se23kCP) is purified from S. erinaceieuropaei plerocercoids. Se23kCP has both cysteine and serine protease-specific activities. Se23kCP is secreted from tegumental vacuoles and degrades host structural proteins. The body region of plerocercoid is lysed by Se23kCP, allowing host tissue invasion. Se23kCP acts for host tissue invasion and migration of plerocercoid. Graphical abstract [DISPLAY OMISSION]


  • 주제어

    Spirometra erinaceieuropaei .   Plerocercoid .   Cysteine protease .   Body dissolution .   Invasion .   Migration.  

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