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A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2

Akkermansia muciniphila can produce various mucin-degrading proteins. However, the functional characteristics of these proteins and their role in mucin degradation are unclear. Of the predicted protein-coding genes, Amuc_1434, which encodes for a hypothetical protein, is the focus in this study. A r...

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Autores principales: Meng, Xin, Wang, Wencheng, Lan, Tianqi, Yang, Wanxin, Yu, Dahai, Fang, Xuexun, Wu, Hao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6982040/
https://www.ncbi.nlm.nih.gov/pubmed/31861919
http://dx.doi.org/10.3390/ijms21010072
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author Meng, Xin
Wang, Wencheng
Lan, Tianqi
Yang, Wanxin
Yu, Dahai
Fang, Xuexun
Wu, Hao
author_facet Meng, Xin
Wang, Wencheng
Lan, Tianqi
Yang, Wanxin
Yu, Dahai
Fang, Xuexun
Wu, Hao
author_sort Meng, Xin
collection PubMed
description Akkermansia muciniphila can produce various mucin-degrading proteins. However, the functional characteristics of these proteins and their role in mucin degradation are unclear. Of the predicted protein-coding genes, Amuc_1434, which encodes for a hypothetical protein, is the focus in this study. A recombinant enzyme Amuc_1434 containing the 6× His-tag produced in Escherichia coli (hereinafter termed Amuc_1434*) was isolated to homogeneity and biochemically characterised. Results showed that the enzyme can hydrolyse hemoglobin with an activity of 17.21 U/μg. The optimal pH and temperature for hemoglobin hydrolysis of Amuc_1434* were found to be around 8.0 and 40 °C, respectively. Amuc_1434* is identified as a member of the aspartic protease family through the action of inhibitor pepstatin A. Amuc_1434* promotes the adhesion of colon cancer cell line LS174T, which can highly express Muc2. Significantly Amuc_1434* can degrade Muc2 of colon cancer cells. Amuc_1434 is mainly located in the colon of BALB/c mice. These results suggest that the presence of Amuc_1434 from Akkermansia muciniphila may be correlated with the restoration of gut barrier function by decreasing mucus layer thickness.
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spelling pubmed-69820402020-02-07 A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2 Meng, Xin Wang, Wencheng Lan, Tianqi Yang, Wanxin Yu, Dahai Fang, Xuexun Wu, Hao Int J Mol Sci Article Akkermansia muciniphila can produce various mucin-degrading proteins. However, the functional characteristics of these proteins and their role in mucin degradation are unclear. Of the predicted protein-coding genes, Amuc_1434, which encodes for a hypothetical protein, is the focus in this study. A recombinant enzyme Amuc_1434 containing the 6× His-tag produced in Escherichia coli (hereinafter termed Amuc_1434*) was isolated to homogeneity and biochemically characterised. Results showed that the enzyme can hydrolyse hemoglobin with an activity of 17.21 U/μg. The optimal pH and temperature for hemoglobin hydrolysis of Amuc_1434* were found to be around 8.0 and 40 °C, respectively. Amuc_1434* is identified as a member of the aspartic protease family through the action of inhibitor pepstatin A. Amuc_1434* promotes the adhesion of colon cancer cell line LS174T, which can highly express Muc2. Significantly Amuc_1434* can degrade Muc2 of colon cancer cells. Amuc_1434 is mainly located in the colon of BALB/c mice. These results suggest that the presence of Amuc_1434 from Akkermansia muciniphila may be correlated with the restoration of gut barrier function by decreasing mucus layer thickness. MDPI 2019-12-20 /pmc/articles/PMC6982040/ /pubmed/31861919 http://dx.doi.org/10.3390/ijms21010072 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Meng, Xin
Wang, Wencheng
Lan, Tianqi
Yang, Wanxin
Yu, Dahai
Fang, Xuexun
Wu, Hao
A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2
title A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2
title_full A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2
title_fullStr A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2
title_full_unstemmed A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2
title_short A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2
title_sort purified aspartic protease from akkermansia muciniphila plays an important role in degrading muc2
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6982040/
https://www.ncbi.nlm.nih.gov/pubmed/31861919
http://dx.doi.org/10.3390/ijms21010072
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