The StcE protease contributes to intimate adherence of enterohemorrhagic Escherichia coli O157:H7 to host cells

Thomas Grys, Matthew B. Siegel, Wyndham W. Lathem, Rodney A. Welch

Research output: Contribution to journalArticle

81 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)1295-1303
Number of pages9
JournalInfection and Immunity
Volume73
Issue number3
DOIs
StatePublished - Mar 1 2005
Externally publishedYes

Fingerprint

Enterohemorrhagic Escherichia coli
Escherichia coli O157
Peptide Hydrolases
Actins
Coloring Agents
Complement C1 Inhibitor Protein
Membrane Glycoproteins
Gene Deletion
Metalloproteases
Mucins
Saliva
Viscosity
Virulence
Zinc
Glycoproteins
Plasmids
Epithelial Cells
Inflammation
Bacteria
Gene Expression

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

Cite this

The StcE protease contributes to intimate adherence of enterohemorrhagic Escherichia coli O157:H7 to host cells. / Grys, Thomas; Siegel, Matthew B.; Lathem, Wyndham W.; Welch, Rodney A.

In: Infection and Immunity, Vol. 73, No. 3, 01.03.2005, p. 1295-1303.

Research output: Contribution to journalArticle

Grys, Thomas ; Siegel, Matthew B. ; Lathem, Wyndham W. ; Welch, Rodney A. / The StcE protease contributes to intimate adherence of enterohemorrhagic Escherichia coli O157:H7 to host cells. In: Infection and Immunity. 2005 ; Vol. 73, No. 3. pp. 1295-1303.
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