Cited by 51Escherichia coli research studiesComplement system in diseasesProtease and Inhibitor Mechanisms

Characterization of the StcE Protease Activity of Escherichia coli O157:H7

Grys, Thomas E., Walters, Laura L., Welch, Rodney A.·2006·Journal of Bacteriology

Abstract

The StcE zinc metalloprotease is secreted by enterohemorrhagic Escherichia coli (EHEC) O157:H7 and contributes to intimate adherence of this bacterium to host cells, a process essential for mammalian colonization. StcE has also been shown to localize the inflammatory regulator C1 esterase inhibitor (C1-INH) to cell membranes. We tried to more fully characterize StcE activity to better understand its role in EHEC pathogenesis. StcE was active at pH 6.1 to 9.0, in the presence of NaCl concentrations ranging from 0 to 600 mM, and at 4°C to 55°C. Interestingly, antisera against StcE or C1-INH did not eliminate StcE cleavage of C1-INH. Treatment of StcE with the proteases trypsin, chymotrypsin, human neutrophil elastase, and Pseudomonas aeruginosa elastase did not eliminate StcE activity against C1-INH. After StcE was kept at 23°C for 65 days, it exhibited full proteolytic activity, and it retained 30% of its original activity after incubation for 8 days at 37°C. Together, these results show the StcE protease is a stable enzyme that is probably active in the environment of the colon. Additionally, k cat / K m data showed that StcE proteolytic activity was 2.5-fold more efficient with the secreted mucin MUC7 than with the complement regulator C1-INH. This evidence supports a model which includes two roles for StcE during infection, in which StcE acts first as a mucinase and then as an anti-inflammatory agent by localizing C1-INH to cell membranes.

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Crossref · 10.1128/jb.01806-05

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  • The zinc metalloproteases StcE and SslE secreted by E. coli EHEC and EPEC/ETEC respectively contribute to intimate adherence of these bacteria to host cells, a process essential for colonization.

    “Finally, the zinc metalloproteases StcE and SslE secreted by E. coli EHEC and EPEC/ETEC respectively, contribute to intimate adherence of these bacteria to host cells, a process that is essential for colonization.73–78”

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Authors
Grys, T. E., Walters, L. L., & Welch, R. A.
Affiliations
University of Wisconsin–Madison (US)
Corresponding author
Welch, Rodney A.
Venue
Journal of Bacteriology
Published
2006-07
Volume
188
Issue
13
Pages
4646-4653
ISSN
  • 0021-9193 (ISSN-L)
  • 1098-5530
OpenAlex
W2139233841
Cited by
51
References
29
Citations by year
2026: 2 · 2025: 4 · 2024: 3 · 2023: 3 · 2022: 6 · 2021: 2 · 2020: 3 · 2019: 2 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 3 · 2014: 2 · 2013: 1 · 2012: 5
FWCI
0.79
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Bacteriology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health
  • National Institute of General Medical Sciences (5T32GM08349, T32GM008349, T32GM008692)
  • National Institute of Allergy and Infectious Diseases (R01AI051735)
  • National Institute of Diabetes and Digestive and Kidney Diseases (R01DK063250)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
  • Life Sciences › Immunology and Microbiology › Immunology › Complement system in diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Keywords
zinc metalloprotease, Escherichia coli O157:H7, enterohemorrhagic Escherichia coli, C1 inhibitor, mucinase, MUC7, anti-inflammatory activity, enzyme stability, proteolytic activity, complement regulation, bacterial pathogenesis
MeSH terms
Antibodies, Bacterial, Chymotrypsin, Escherichia coli Infections, Humans, Hydrogen-Ion Concentration, Metalloendopeptidases, Mucins, Pancreatic Elastase, Pseudomonas aeruginosa, Salivary Proteins and Peptides, Temperature, Time Factors, Trypsin, Leukocyte Elastase, Escherichia coli O157, Escherichia coli Proteins, Complement C1 Inhibitor Protein

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