Extracellular Protease Activity of Enteropathogenic Escherechia coli on Mucin Substrate

Enteropathogenic Escherichia coli (EPEC) causes gastrointestinal infections in human. EPEC invasion was initiated by attachment and aggressive colonization on intestinal surface. Attachment of EPEC alter the intestine mucosal cells. Despite this, the pathogenic mechanism of EPEC infectior has not be...

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Main Authors: SRI BUDIARTI, NISA RACHMANIA MUBARIK
Format: Article
Language:English
Published: Bogor Agricultural University 2007-03-01
Series:Hayati Journal of Biosciences
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S1978301916302972
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spelling doaj-9411fa010d7d4f6bb4e318a40acdca0e2020-11-24T21:40:44ZengBogor Agricultural UniversityHayati Journal of Biosciences1978-30192007-03-01141363810.4308/hjb.14.1.36Extracellular Protease Activity of Enteropathogenic Escherechia coli on Mucin SubstrateSRI BUDIARTINISA RACHMANIA MUBARIKEnteropathogenic Escherichia coli (EPEC) causes gastrointestinal infections in human. EPEC invasion was initiated by attachment and aggressive colonization on intestinal surface. Attachment of EPEC alter the intestine mucosal cells. Despite this, the pathogenic mechanism of EPEC infectior has not been fully understood. This research hypothesizes that extracellular proteolytic enzymes is necessary for EPEC colonization. The enzyme is secreted into gastrointestinal milieu and presumably destroy mucus layer cover the gastrointestinal tract. The objective of this study was to assay EPEC extracellular protease enzyme by using mucin substrate. The activity of EPEC extracellular proteolytic enzyme on 1% mucin substrate was investigated. Non-pathogenic E. coli was used as a negative control. Positive and tentative controls were Yersinia enterocolitica and Salmonella. Ten EPEC strains were assayed, seven of them were able to degrade mucin, and the highest activity was produced by K1.1 strain. Both positive and tentative controls also showed the ability to digest 0.20% mucin.http://www.sciencedirect.com/science/article/pii/S1978301916302972EPECproteasemucindiarrhea
collection DOAJ
language English
format Article
sources DOAJ
author SRI BUDIARTI
NISA RACHMANIA MUBARIK
spellingShingle SRI BUDIARTI
NISA RACHMANIA MUBARIK
Extracellular Protease Activity of Enteropathogenic Escherechia coli on Mucin Substrate
Hayati Journal of Biosciences
EPEC
protease
mucin
diarrhea
author_facet SRI BUDIARTI
NISA RACHMANIA MUBARIK
author_sort SRI BUDIARTI
title Extracellular Protease Activity of Enteropathogenic Escherechia coli on Mucin Substrate
title_short Extracellular Protease Activity of Enteropathogenic Escherechia coli on Mucin Substrate
title_full Extracellular Protease Activity of Enteropathogenic Escherechia coli on Mucin Substrate
title_fullStr Extracellular Protease Activity of Enteropathogenic Escherechia coli on Mucin Substrate
title_full_unstemmed Extracellular Protease Activity of Enteropathogenic Escherechia coli on Mucin Substrate
title_sort extracellular protease activity of enteropathogenic escherechia coli on mucin substrate
publisher Bogor Agricultural University
series Hayati Journal of Biosciences
issn 1978-3019
publishDate 2007-03-01
description Enteropathogenic Escherichia coli (EPEC) causes gastrointestinal infections in human. EPEC invasion was initiated by attachment and aggressive colonization on intestinal surface. Attachment of EPEC alter the intestine mucosal cells. Despite this, the pathogenic mechanism of EPEC infectior has not been fully understood. This research hypothesizes that extracellular proteolytic enzymes is necessary for EPEC colonization. The enzyme is secreted into gastrointestinal milieu and presumably destroy mucus layer cover the gastrointestinal tract. The objective of this study was to assay EPEC extracellular protease enzyme by using mucin substrate. The activity of EPEC extracellular proteolytic enzyme on 1% mucin substrate was investigated. Non-pathogenic E. coli was used as a negative control. Positive and tentative controls were Yersinia enterocolitica and Salmonella. Ten EPEC strains were assayed, seven of them were able to degrade mucin, and the highest activity was produced by K1.1 strain. Both positive and tentative controls also showed the ability to digest 0.20% mucin.
topic EPEC
protease
mucin
diarrhea
url http://www.sciencedirect.com/science/article/pii/S1978301916302972
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