Host response to the subtilase cytotoxin produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli.
Animals
Apoptosis
/ physiology
Endoplasmic Reticulum
/ physiology
Endoplasmic Reticulum Chaperone BiP
Endoplasmic Reticulum Stress
/ physiology
Escherichia coli Proteins
/ genetics
Foodborne Diseases
/ microbiology
Humans
Mice
Shiga Toxin 1
/ metabolism
Shiga Toxin 2
/ metabolism
Shiga-Toxigenic Escherichia coli
/ genetics
Subtilisins
/ genetics
Virulence Factors
/ genetics
Shiga-toxigenic Escherichia coli
apoptosis
endoplasmic reticulum stress
receptor
subtilase cytotoxin
Journal
Microbiology and immunology
ISSN: 1348-0421
Titre abrégé: Microbiol Immunol
Pays: Australia
ID NLM: 7703966
Informations de publication
Date de publication:
Oct 2020
Oct 2020
Historique:
received:
18
06
2020
revised:
05
08
2020
accepted:
07
09
2020
pubmed:
10
9
2020
medline:
9
6
2021
entrez:
9
9
2020
Statut:
ppublish
Résumé
Shiga-toxigenic Escherichia coli (STEC) is a major bacterium responsible for disease resulting from foodborne infection, including bloody diarrhea and hemolytic uremic syndrome. STEC produces important virulence factors such as Shiga toxin (Stx) 1 and/or 2. In the STEC family, some locus of enterocyte effacement-negative STEC produce two different types of cytotoxins, namely, Stx2 and subtilase cytotoxin (SubAB). The Stx2 and SubAB cytotoxins are structurally similar and composed of one A subunit and pentamer of B subunits. The catalytically active A subunit of SubAB is a subtilase-like serine protease and specifically cleaves an endoplasmic reticulum (ER) chaperone 78-kDa glucose-regulated protein (GRP78/BiP), a monomeric ATPase that is crucial in protein folding and quality control. The B subunit binds to cell surface receptors. SubAB recognizes sialic carbohydrate-modified cell surface proteins as a receptor. After translocation into cells, SubAB is delivered to the ER, where it cleaves GRP78/BiP. SubAB-catalyzed BiP cleavage induces ER stress, which causes various cell events including inhibition of protein synthesis, suppression of nuclear factor-kappa B activation, apoptotic cell death, and stress granules formation. In this review, we describe SubAB, the SubAB receptor, and the mechanism of cell response to the toxin.
Identifiants
pubmed: 32902863
doi: 10.1111/1348-0421.12841
doi:
Substances chimiques
Endoplasmic Reticulum Chaperone BiP
0
Escherichia coli Proteins
0
HSPA5 protein, human
0
Hspa5 protein, mouse
0
Shiga Toxin 1
0
Shiga Toxin 2
0
Virulence Factors
0
Subtilisins
EC 3.4.21.-
subtilase cytotoxin, E coli
EC 3.4.21.-
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
657-665Subventions
Organisme : Research Program on Emerging and Re-emerging Infectious Diseases from Japan Agency for Medical Research and Development, AMED
Organisme : Japan Society for Promotion of Science (JSPS) KAKENHI; Takeda Science Foundation
Informations de copyright
© 2020 The Societies and John Wiley & Sons Australia, Ltd.
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