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Immunolocalization and functional analysis of Opisthorchis viverrini-M60-like-1 metallopeptidase in animal models

Published online by Cambridge University Press:  21 April 2022

Woro D. Wendo
Affiliation:
Faculty of Veterinary Medicine, Khon Kaen University, Khon Kaen 40002, Thailand Graduate School, Khon Kaen University, Khon Kaen 40002, Thailand Department of Anatomy, Faculty of Veterinary Medicine, Universitas Gadjah Mada, Yogyakarta, Indonesia
Sirikachorn Tangkawattana*
Affiliation:
Faculty of Veterinary Medicine, Khon Kaen University, Khon Kaen 40002, Thailand Tropical Disease Research Center, WHO Collaborating Centre for Research and Control of Opisthorchiasis, Khon Kaen University, Khon Kaen 40002, Thailand
Prasert Saichua
Affiliation:
Tropical Disease Research Center, WHO Collaborating Centre for Research and Control of Opisthorchiasis, Khon Kaen University, Khon Kaen 40002, Thailand Tropical Medicine Graduate Program, Academic Affairs, Faculty of Medicine, Khon Kaen University, Khon Kaen 40002, Thailand
Binh T. T. Ta*
Affiliation:
Tropical Medicine Graduate Program, Academic Affairs, Faculty of Medicine, Khon Kaen University, Khon Kaen 40002, Thailand
Agatha R. K. Candra
Affiliation:
Department of Biomedicine, School of Life Sciences, Indonesia International Institute for Life Sciences, Jakarta, Indonesia
Prasarn Tangkawattana
Affiliation:
Faculty of Veterinary Medicine, Khon Kaen University, Khon Kaen 40002, Thailand
Sutas Suttiprapa*
Affiliation:
Tropical Disease Research Center, WHO Collaborating Centre for Research and Control of Opisthorchiasis, Khon Kaen University, Khon Kaen 40002, Thailand Tropical Medicine Graduate Program, Academic Affairs, Faculty of Medicine, Khon Kaen University, Khon Kaen 40002, Thailand
*
Authors for correspondence: Sirikachorn Tangkawattana, E-mail: [email protected]; Sutas Suttiprapa, E-mail: [email protected]
Authors for correspondence: Sirikachorn Tangkawattana, E-mail: [email protected]; Sutas Suttiprapa, E-mail: [email protected]
Authors for correspondence: Sirikachorn Tangkawattana, E-mail: [email protected]; Sutas Suttiprapa, E-mail: [email protected]

Abstract

Host mucins have crucial physical roles in preventing the parasitic establishment and maturation, and also in expelling the invading parasites. However, some parasites utilize mucinase enzymes to facilitate the infection. Recently, we have identified a mucinase enzyme of the liver fluke Opisthorchis viverrini, Ov-M60-like-1, which exhibits metallopeptidase activity against bovine submaxillary mucin substrate. Here, we aimed to study the localization of this enzyme in O. viverrini and the bile duct of hamsters using immunohistochemistry and functional analysis by mucin digestion in hamsters and mice tissues. The results showed that Ov-M60-like-1 was detected strongly in the tegument, tegumental cells, vitelline glands and mature eggs with miracidium. Expression in the gut, ovary and testis of the parasite was moderate while parenchyma showed slight colour intensity. In addition, the mucinase was also detected in the host biliary epithelial cells and goblet cells surrounding the worm. The mucinase assay revealed that the Ov-M60-like-1 could digest neutral mucin in the parenchyma, testis and seminal receptacle, but not the mucin in the tegument, tegumental cells and vitelline glands of the worm. The enzyme can also digest mucin in the cholangiocytes and modified the mixture type in the bile duct goblet cells of the infected hamsters, a susceptible host. In contrast, the enzyme was unable to digest neutral, acid and mixture mucin in the bile duct of the mice, a non-susceptible host. These findings indicate that Ov-M60-like-1 may have functions in both housekeeping tasks and host–parasite interactions, especially in modification of host susceptibility.

Type
Research Article
Copyright
Copyright © The Author(s), 2022. Published by Cambridge University Press

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