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The StcE Protease Contributes to Intimate Adherence of Enterohemorrhagic Escherichia coli O157:H7 to Host Cells
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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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“StcE and SslE, metalloproteases from diarrheagenic E. coli strains, also cleave mucin glycoproteins, which may help the pathogen to reach the epithelium.74–76”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [75]
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“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”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [75]
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Monteiro, R., Chafsey, I., Ageorges, V., Léroy, S., Chambon, C., Hébraud, M., Livrelli, V., Pizza, M., Pezzicoli, A., & Desvaux, M. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2020.104025 · Cited by 14
Korotkov, K. V., & Hol, W. G. J. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.02.013 · Cited by 14
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Proteomes of pathogenicEscherichia coli/Shigellagroup surveyed in their host environments
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Jaroentomeechai, T., Veloz, B., Soares, C. O., Goerdeler, F., Grosso, A. S., Büll, C., Miller, R. L., Furukawa, S., Ginés‐Alcober, I., Taleb, V., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63756-w · Cited by 12
Bai, J., McAteer, S. P., Paxton, E. A., Mahajan, A., Gally, D. L., & Tree, J. J. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00168 · Cited by 12
Enteropathogens: Tuning Their Gene Expression for Hassle-Free Survival
Chatterjee, R., Shreenivas, M. M., Sunil, R., & Chakravortty, D. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.03303 · Cited by 11
Hayashi, N., Matsukawa, M., Horinishi, Y., Nakai, K., Shoji, A., Yoneko, Y., Yoshida, N., Minagawa, S., & Gotoh, N. (2013) · Journal of Infection and Chemotherapy · doi:10.1007/s10156-013-0554-4 · Cited by 12
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Steck, N., Mueller, K., Schemann, M., & Haller, D. (2012) · Postgraduate Medical Journal · doi:10.1136/postgradmedj-2011-300775rep · Cited by 11
Enterohemorrhagic and other Shigatoxin-producing Escherichia coli
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Phosphotyrosine-Mediated Regulation of Enterohemorrhagic Escherichia coli Virulence
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Furniss, R. C. D., Low, W. W., Mavridou, D. A. I., Dagley, L. F., Webb, A. I., Tate, E. W., & Clements, A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005114 · Cited by 11
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Metadata
- Authors
- Grys, T. E., Siegel, M. B., Lathem, W. W., & Welch, R. A.
- Affiliations
- University of Wisconsin–Madison (US)
- 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
- 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
- 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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