Publication: Identification, recombinant protein production, and functional analysis of a M60-like metallopeptidase, secreted by the liver fluke Opisthorchis viverrini
Issued Date
2020-04-01
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ISSN
18730329
13835769
13835769
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2-s2.0-85077460220
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Mahidol University
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SCOPUS
Bibliographic Citation
Parasitology International. Vol.75, (2020)
Suggested Citation
Binh T.T. Ta, D. Linh Nguyen, Isabelle Jala, Rieofarng Dontumprai, Sirikanya Plumworasawat, Omorose Aighewi, Emily Ong, Audrey Shawley, Jeremy Potriquet, Prasert Saichua, Angela van Diepen, Banchob Sripa, Cornelis H. Hokke, Sutas Suttiprapa Identification, recombinant protein production, and functional analysis of a M60-like metallopeptidase, secreted by the liver fluke Opisthorchis viverrini. Parasitology International. Vol.75, (2020). doi:10.1016/j.parint.2019.102050 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/49614
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Title
Identification, recombinant protein production, and functional analysis of a M60-like metallopeptidase, secreted by the liver fluke Opisthorchis viverrini
Abstract
© 2020 Elsevier B.V. The carcinogenic liver fluke Opisthorchis viverrini (O. viverrini) is endemic in Thailand and neighboring countries including Laos PDR, Vietnam and Cambodia. Infections with O. viverrini lead to hepatobiliary abnormalities including bile duct cancer–cholangiocarcinoma (CCA). Despite decades of extensive studies, the underlying mechanisms of how this parasite survives in the bile duct and causes disease are still unclear. Therefore, this study aims to identify and characterize the most abundant protein secreted by the parasite. Proteomics and bioinformatics analysis revealed that the most abundant secretory protein is a metallopeptidase, named Ov-M60-like-1. This protein contains an N-terminal carbohydrate-binding domain and a C-terminal M60-like domain with a zinc metallopeptidase HEXXH motif. Further analysis by mass spectrometry revealed that Ov-M60-like-1 is N-glycosylated. Recombinant Ov-M60-like-1 (rOv-M60-like-1) expressed in Escherichia coli (E. coli) was able to digest bovine submaxillary mucin (BSM). The mucinase activity was inhibited by the ion chelating agent EDTA, confirming its metallopeptidase identity. The enzyme was active at temperatures ranging 25–37 °C in a broad pH range (pH 2–10). The identification of Ov-M60-like-1 mucinase as the major secretory protein of O. viverrini worms warrants further research into the role of this glycoprotein in the pathology induced by this carcinogenic worm.