Cited by 138Escherichia coli research studiesBacterial Genetics and BiotechnologyClostridium difficile and Clostridium perfringens research

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The StcE Protease Contributes to Intimate Adherence of Enterohemorrhagic Escherichia coli O157:H7 to Host Cells

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Grys, Thomas E., Siegel, Matthew B., Lathem, Wyndham W., Welch, Rodney A.·2005·Infection and Immunity

DOI 10.1128/iai.73.3.1295-1303.2005PMC PMC1064933

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Abstract

Enterohemorrhagic Escherichia coli(EHEC) O157:H7 is a diarrheal pathogen that causes attaching and effacing (A/E) lesions on intestinal epithelial cells. Strains of the O157 serogroup carry the large virulence plasmid pO157, which encodes the etp type II secretion system that secretes the genetically linked zinc metalloprotease StcE. The Ler regulator controls expression of many genes involved in A/E lesion formation, as well as StcE, suggesting StcE may be important at a similar time during colonization. Our laboratory has previously demonstrated that StcE cleaves C1-esterase inhibitor, a regulator of multiple inflammation pathways. Here we report two new substrates for StcE, mucin 7 and glycoprotein 340, and that purified StcE reduces the viscosity of human saliva. We tested the hypothesis that StcE contributes to intimate adherence of EHEC to host cells by cleavage of glycoproteins from the cell surface. The fluorescent actin stain (FAS) test was used to observe the intimate adherence represented by fluorescently stained bacteria colocalized with regions of bundled actin formed on HEp-2 cells. An E. coli O157:H7 strain with a stcE gene deletion was not affected in its ability to generally adhere to HEp-2 cells, but it did score threefold lower on the FAS test than wild-type or complemented strains. Addition of exogenous recombinant StcE increased intimate adherence of the mutant to wild-type levels. Thus, StcE may help block host clearance of E. coli O157:H7 by destruction of some classes of glycoproteins, and it contributes to intimate adherence of E. coli O157:H7 to the HEp-2 cell surface.

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Research works printed but not linked: 1

Lathem, W. W., T. Bergsbaken, S. E. Witowski, N. T. Perna, and R. A. Welch. 2002. Acquisition of StcE, a C1 esterase inhibitor-specific metalloprotease, by Escherichia coli O157:H7. J. Infect. Dis.187:1907-1914.

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Authors: Grys, T. E., Siegel, M. B., Lathem, W. W., & Welch, R. A.
Affiliations: University of Wisconsin–Madison (US)
ORCID: Grys, Thomas E.
Lathem, Wyndham W.
Welch, Rodney A.
Venue: Infection and Immunity
Publisher: American Society for Microbiology
Published: 2005-03
Volume: 73
Issue: 3
Pages: 1295-1303
ISSN: 0019-9567 (ISSN-L)
1098-5522
DOI: 10.1128/iai.73.3.1295-1303.2005
PMC: PMC1064933
OpenAlex: W2097638901
Cited by: 138
References: 72
Citations by year: 2026: 8 · 2025: 7 · 2024: 2 · 2023: 3 · 2022: 12 · 2021: 7 · 2020: 6 · 2019: 5 · 2018: 6 · 2017: 5 · 2016: 6 · 2015: 4 · 2014: 6 · 2013: 9 · 2012: 7
FWCI: 4.02
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Infection and Immunity (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (5T32GM08349, T32GM008349)
National Institute of Allergy and Infectious Diseases (R01AI051735)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK063250)
Topics: Life Sciences › Immunology and Microbiology › Microbiology › Escherichia coli research studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Infectious Diseases › Clostridium difficile and Clostridium perfringens research
Keywords: Escherichia coli O157:H7, zinc metalloprotease, type II secretion system, C1 inhibitor, actin cytoskeleton, HEp-2 cells, saliva viscosity, attaching and effacing lesions
MeSH terms: Bacterial Adhesion, Cell Line, Humans, Metalloendopeptidases, Molecular Sequence Data, Mucins, Receptors, Immunologic, Saliva, Salivary Proteins and Peptides, Virulence, Sequence Analysis, DNA, Escherichia coli O157, Escherichia coli Proteins

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The StcE Protease Contributes to Intimate Adherence of Enterohemorrhagic Escherichia coli O157:H7 to Host Cells

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