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Title: Identification, recombinant protein production, and functional analysis of a M60-like metallopeptidase, secreted by the liver fluke Opisthorchis viverrini
Authors: 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
Faculty of Medicine, Khon Kaen University
Occidental College
James Cook University, Australia
Leiden University Medical Center - LUMC
Mahidol University
Faculty of Medicine, Siriraj Hospital, Mahidol University
Keywords: Immunology and Microbiology;Medicine
Issue Date: 1-Apr-2020
Citation: Parasitology International. Vol.75, (2020)
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.
ISSN: 18730329
Appears in Collections:Scopus 2020

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