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

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 Opisthorchi...

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Main Authors: Wendo, Woro Danur, Tangkawattana, Sirikachorn, Saichua, Prasert, Ta, Binh T. T., Candra, Agatha R. K., Tangkawattana, Prasarn, Suttiprapa, Sutas
Format: Article PeerReviewed
Language:English
Published: Cambridge University Press 2022
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Online Access:https://repository.ugm.ac.id/278778/1/Wendo_KH.pdf
https://repository.ugm.ac.id/278778/
https://www.cambridge.org/par
https://doi.org/10.1017/S0031182022000403
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spelling id-ugm-repo.2787782023-11-02T00:32:12Z https://repository.ugm.ac.id/278778/ Immunolocalization and functional analysis of Opisthorchis viverrini-M60-like-1 metallopeptidase in animal models Wendo, Woro Danur Tangkawattana, Sirikachorn Saichua, Prasert Ta, Binh T. T. Candra, Agatha R. K. Tangkawattana, Prasarn Suttiprapa, Sutas Veterinary Sciences 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. Cambridge University Press 2022-04-21 Article PeerReviewed application/pdf en https://repository.ugm.ac.id/278778/1/Wendo_KH.pdf Wendo, Woro Danur and Tangkawattana, Sirikachorn and Saichua, Prasert and Ta, Binh T. T. and Candra, Agatha R. K. and Tangkawattana, Prasarn and Suttiprapa, Sutas (2022) Immunolocalization and functional analysis of Opisthorchis viverrini-M60-like-1 metallopeptidase in animal models. Parasitology, 149 (10). pp. 1356-1363. ISSN 1469-8161 https://www.cambridge.org/par https://doi.org/10.1017/S0031182022000403
institution Universitas Gadjah Mada
building UGM Library
continent Asia
country Indonesia
Indonesia
content_provider UGM Library
collection Repository Civitas UGM
language English
topic Veterinary Sciences
spellingShingle Veterinary Sciences
Wendo, Woro Danur
Tangkawattana, Sirikachorn
Saichua, Prasert
Ta, Binh T. T.
Candra, Agatha R. K.
Tangkawattana, Prasarn
Suttiprapa, Sutas
Immunolocalization and functional analysis of Opisthorchis viverrini-M60-like-1 metallopeptidase in animal models
description 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.
format Article
PeerReviewed
author Wendo, Woro Danur
Tangkawattana, Sirikachorn
Saichua, Prasert
Ta, Binh T. T.
Candra, Agatha R. K.
Tangkawattana, Prasarn
Suttiprapa, Sutas
author_facet Wendo, Woro Danur
Tangkawattana, Sirikachorn
Saichua, Prasert
Ta, Binh T. T.
Candra, Agatha R. K.
Tangkawattana, Prasarn
Suttiprapa, Sutas
author_sort Wendo, Woro Danur
title Immunolocalization and functional analysis of Opisthorchis viverrini-M60-like-1 metallopeptidase in animal models
title_short Immunolocalization and functional analysis of Opisthorchis viverrini-M60-like-1 metallopeptidase in animal models
title_full Immunolocalization and functional analysis of Opisthorchis viverrini-M60-like-1 metallopeptidase in animal models
title_fullStr Immunolocalization and functional analysis of Opisthorchis viverrini-M60-like-1 metallopeptidase in animal models
title_full_unstemmed Immunolocalization and functional analysis of Opisthorchis viverrini-M60-like-1 metallopeptidase in animal models
title_sort immunolocalization and functional analysis of opisthorchis viverrini-m60-like-1 metallopeptidase in animal models
publisher Cambridge University Press
publishDate 2022
url https://repository.ugm.ac.id/278778/1/Wendo_KH.pdf
https://repository.ugm.ac.id/278778/
https://www.cambridge.org/par
https://doi.org/10.1017/S0031182022000403
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