WordNet

a form of staphylococcal enterotoxin that has been used as an incapacitating agent in biological warfare (同)SEB
of or relating to the staphylococcus bacteria; "a staphylococcal infection"
a cytotoxin specific for the cells of the intestinal mucosa

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/10/20 23:41:25」(JST)

wiki en

An enterotoxin is a protein exotoxin released by a microorganism that targets the intestines. Its target site is indicated within its name.^[1] ^{[clarification needed]}

Enterotoxins are chromosomally encoded exotoxins that are produced and secreted from several bacterial organisms. They are often heat-stable, and are of low molecular weight and water-soluble. Enterotoxins are frequently cytotoxic and kill cells by altering the apical membrane permeability of the mucosal (epithelial) cells of the intestinal wall. They are mostly pore-forming toxins (mostly chloride pores), secreted by bacteria, that assemble to form pores in cell membranes. This causes the cells to die.

Clinical significance

Enterotoxins have a particularly marked effect upon the gastrointestinal tract, causing vomiting, diarrhea, and abdominal pain. The action of enterotoxins leads to increased chloride ion permeability of the apical membrane of intestinal mucosal cells. These membrane pores are activated either by increased cAMP or by increased calcium ion concentration intracellularly. The pore formation has a direct effect on the osmolarity of the luminal contents of the intestines. Increased chloride permeability leads to leakage into the lumen followed by sodium and water movement. This leads to a secretory diarrhea within a few hours of ingesting enterotoxin. Several microbial organisms contain the necessary enterotoxin to create such an effect, such as Staphylococcus aureus and E. coli.

Classification and 3D structures of enterotoxins

Bacterial

Staphylococcal enterotoxins and streptococcal pyrogenic exotoxins constitute a family of biologically and structurally related toxins produced by Staphylococcus aureus and Streptococcus pyogenes.^[2]^[3] These toxins share the ability to bind to the major histocompatibility complex proteins of their hosts. A more distant relative of the family is the S. aureus toxic shock syndrome toxin, which shares only a low level of sequence similarity with this group.

All of these toxins share a similar two-domain fold (N and C-terminal domains) with a long alpha-helix in the middle of the molecule, a characteristic beta-barrel known as the "oligosaccharide/oligonucleotide fold" at the N-terminal domain and a beta-grasp motif at the C-terminal domain. Examples include enterotoxin type B. Each superantigen possesses slightly different binding mode(s) when it interacts with MHC class II molecules or the T-cell receptor.^[4]

The beta-grasp domain has some structural similarities to the beta-grasp motif present in immunoglobulin-binding domains, ubiquitin, 2Fe-2 S ferredoxin and translation initiation factor 3 as identified by the SCOP database.

Clostridium difficile
Clostridium perfringens (Clostridium perfringens enterotoxin)^[5]
Vibrio cholerae (Cholera toxin)^[6]
Staphylococcus aureus (Staphylococcal Enterotoxin B)^[7]
Yersinia enterocolitica
Shigella dysenteriae (Shiga toxin)^[6]

Viral

Rotavirus (NSP4)

References

^ "enterotoxin" at Dorland's Medical Dictionary
^ Iandolo JJ (1989). "Genetic analysis of extracellular toxins of Staphylococcus aureus". Annu. Rev. Microbiol. 43: 375–402. doi:10.1146/annurev.mi.43.100189.002111. PMID 2679358.
^ Marrack P, Kappler J (May 1990). "The staphylococcal enterotoxins and their relatives". Science 248 (4956): 705–11. doi:10.1126/science.2185544. PMID 2185544.
^ Papageorgiou AC, Tranter HS, Acharya KR (March 1998). "Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors". J. Mol. Biol. 277 (1): 61–79. doi:10.1006/jmbi.1997.1577. PMID 9514739.
^ Katahira J, Sugiyama H, Inoue N, Horiguchi Y, Matsuda M, Sugimoto N (October 1997). "Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo". The Journal of Biological Chemistry 272 (42): 26652–8. doi:10.1074/jbc.272.42.26652. PMID 9334247.
^ ^a ^b Enterotoxins at the US National Library of Medicine Medical Subject Headings (MeSH)
^ "eMedicine - CBRNE - Staphylococcal Enterotoxin B : Article by Danielle M Pesce". Retrieved 2008-11-08.

External links

Alfonse T. Masi, Rafael A. Timothee, Rolando Armijo, Darwin Alonso, and Luis E. Mainardi (Mar 1959). "Two poisoning outbreaks in Puerto Rico from salt preserved codfish". Public Health Rep 74 (3): 265–270. doi:10.2307/4590423. PMC 1929208.

This article incorporates text from the public domain Pfam and InterPro IPR006123

UpToDate Contents

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1. 微生物による食中毒疾患の鑑別診断 differential diagnosis of microbial foodborne disease
2. ブドウ球菌性毒素性ショック症候群 staphylococcal toxic shock syndrome
3. メチシリン耐性黄色ブドウ球菌の微生物学 microbiology of methicillin resistant staphylococcus aureus
4. 成人における黄色ブドウ球菌菌血症の疫学 epidemiology of staphylococcus aureus bacteremia in adults
5. 市中感染型メチシリン耐性黄色ブドウ球菌の病原性決定基 virulence determinants of community acquired methicillin resistant staphylococcus aureus

English Journal

Molecular characterization of foodborne-associated Staphylococcus aureus strains isolated in Shijiazhuang, China, from 2010 to 2012.

Lv G1, Xu B2, Wei P2, Song J2, Zhang H2, Zhao C2, Qin L3, Zhao B4.Author information 1College of Life Science, Hebei Normal University, Shijiazhuang 050000, China; Shijiazhuang Center for Disease Control and Prevention, Shijiazhuang 050000, China.2Shijiazhuang Center for Disease Control and Prevention, Shijiazhuang 050000, China.3Shijiazhuang Center for Disease Control and Prevention, Shijiazhuang 050000, China. Electronic address: qinliyun-2007@163.com.4College of Life Science, Hebei Normal University, Shijiazhuang 050000, China. Electronic address: Zhaobaohua@hebtu.edu.cn.AbstractStaphylococcus aureus is an opportunistic pathogen commonly identified from food poisoning-associated foodstuffs. From 1996 to the present, S. aureus isolates have been found to exhibit increasing resistance to antimicrobial drugs. The aim of this study was to assess the molecular epidemiology properties of various S. aureus isolates through molecular typing and to investigate their characterization based on their production of enterotoxins and hemolysins and their resistance to antibiotics. A total of 78 coagulase-positive staphylococcal strains isolated from food or clinical samples were analyzed. Eight VNTR loci were used to genotype the 78 isolates, and this analysis resulted in 39 different multilocus variable number tandem repeat analysis (MLVA) profiles. The isolates recovered from a single outbreak exhibited the same MLVA profile. According to CLSI, 97.4% of the isolates were resistant to penicillin, whereas only 3.8% were methicillin-resistant Staphylococcus aureus strains. Through multiplex PCR, 87.2% of the isolates were shown to be enterotoxigenic (SEs), and the most common genes present were sea, sem, seg, seu, and sek. In conclusion, this study demonstrates the prevalence of staphylococcal enterotoxins, the contents of virulent factors, and the characteristics of β-lactam antibiotic resistance in 78 S. aureus isolates. These findings emphasize the need to prevent the presence of S. aureus strains and SE production in foods. Our results also demonstrate that MLVA is a useful and powerful method for epidemiological studies of S. aureus. In contrast to multilocus sequence typing, the MLVA method is a simpler and more rapid method for epidemiological typing with a higher discriminatory power.
Diagnostic microbiology and infectious disease.Diagn Microbiol Infect Dis.2014 Apr;78(4):462-8. doi: 10.1016/j.diagmicrobio.2013.12.006. Epub 2013 Dec 14.
Staphylococcus aureus is an opportunistic pathogen commonly identified from food poisoning-associated foodstuffs. From 1996 to the present, S. aureus isolates have been found to exhibit increasing resistance to antimicrobial drugs. The aim of this study was to assess the molecular epidemiology prope
PMID 24582576

Staphylococcus aureus genomic pattern and atopic dermatitis: may factors other than superantigens be involved?

Rojo A1, Aguinaga A, Monecke S, Yuste JR, Gastaminza G, España A.Author information 1Department of Clinical Microbiology, Clínica Universidad de Navarra, Avenida. Pio XII nº36, 31008, Pamplona, Spain, andrea.rojo.asin@gmail.com.AbstractThe purpose of this investigation was to compare the genotypic profiles of Staphylococcus aureus isolated from atopic dermatitis (AD) patients and from control subjects, and to study the relationship between clinical severity, immune response, and genomic pattern of S. aureus isolated from AD patients. We selected 32 patients with AD and S. aureus skin colonization and 31 atopic controls with no history of AD who where asymptomatic carriers of S. aureus. Microarray-based genotyping was performed on S. aureus isolates. In AD patients, clinical severity was assessed using the Scoring Atopic Dermatitis index and total IgE levels and staphylococcal superantigen-specific IgE levels (SEA, SEB, SEC, TSST1) were determined. The genes lukE, lukD, splA, splB, ssl8, and sasG were more frequent in isolates from AD patients. CC30 was more common in isolates from atopic controls than in AD patients. There was a correlation between total IgE and clinical severity, but an association between clinical severity, immune response, and the presence of S. aureus superantigen genes, including enterotoxin genes, could not be demonstrated. Finally, a correlation was found between AD severity and other S. aureus genes, such as sasG and scn. S. aureus factors besides superantigens could be related to the worsening and onset of AD.
European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology.Eur J Clin Microbiol Infect Dis.2014 Apr;33(4):651-8. doi: 10.1007/s10096-013-2000-z. Epub 2013 Oct 27.
The purpose of this investigation was to compare the genotypic profiles of Staphylococcus aureus isolated from atopic dermatitis (AD) patients and from control subjects, and to study the relationship between clinical severity, immune response, and genomic pattern of S. aureus isolated from AD patien
PMID 24162256

Oral tungstate (Na2WO4) exposure reduces adaptive immune responses in mice after challenge.

Osterburg AR1, Robinson CT, Mokashi V, Stockelman M, Schwemberger SJ, Chapman G, Babcock GF.Author information 1Department of Surgery, University of Cincinnati, Cincinnati , OH , USA .AbstractAbstract Tungstate ([Formula: see text]) has been identified as a ground water contaminant at military firing ranges and can be absorbed by ingestion. In this study, C57BL6 mice were exposed to sodium tungstate (Na2WO4·2H2O) (0, 2, 62.5, 125, and 200 mg/kg/day) in their drinking water for an initial 28-day screen and in a one-generation (one-gen) model. Twenty-four hours prior to euthanasia, mice were intraperitoneally injected with Staphylococcal enterotoxin B (SEB) (20 μg/mouse) or saline as controls. After euthanasia, splenocytes and blood were collected and stained with lymphocyte and/or myeloid immunophenotyping panels and analyzed by flow cytometry. In the 28-day and one-gen exposure, statistically significant reductions were observed in the quantities of activated cytotoxic T-cells (TCTL; CD3(+)CD8(+)CD71(+)) and helper T-cells (TH; CD3(+)CD4(+)CD71(+)) from spleens of SEB-treated mice. In the 28-day exposures, CD71(+) TCTL cells were 12.87 ± 2.05% (SE) in the 0 tungstate (control) group compared to 4.44 ± 1.42% in the 200 mg/kg/day (p < 0.001) group. TH cells were 4.85 ± 1.23% in controls and 2.76 ± 0.51% in the 200 mg/kg/day (p < 0.003) group. In the one-gen exposures, TCTL cells were 7.98 ± 0.49% and 6.33 ± 0.49% for P and F1 mice after 0 mg/kg/day tungstate vs 1.58 ± 0.23% and 2.52 ± 0.25% after 200 mg/kg/day of tungstate (p < 0.001). Similarly, TH cells were reduced to 6.21 ± 0.39% and 7.20 ± 0.76%, respectively, for the 0 mg/kg/day P and F1 mice, and 2.28 ± 0.41% and 2.85 ± 0.53%, respectively, for the 200 mg/kg/day tungstate P and F1 groups (p < 0.001). In delayed-type hypersensitivity Type IV experiments, tungstate exposure prior to primary and secondary antigen challenge significantly reduced footpad swelling at 20 and 200 mg/kg/day. These data indicate that exposure to tungstate can result in immune suppression that may, in turn, reduce host defense against pathogens.
Journal of immunotoxicology.J Immunotoxicol.2014 Apr;11(2):148-59. doi: 10.3109/1547691X.2013.816394. Epub 2013 Jul 29.
Abstract Tungstate ([Formula: see text]) has been identified as a ground water contaminant at military firing ranges and can be absorbed by ingestion. In this study, C57BL6 mice were exposed to sodium tungstate (Na2WO4·2H2O) (0, 2, 62.5, 125, and 200 mg/kg/day) in their drinking water for a
PMID 23895378

Japanese Journal

Public Health : Detection of the staphylococcal enterotoxin D-like gene from staphylococcal food poisoning isolates over the last two decades in Tokyo

The journal of veterinary medical science 77(8), 905-911, 2015-08
NAID 40020571212

ブドウ球菌エンテロトキシンに関する最新の知見—特に分子多様性と生物学的多機能性について—

日本食品微生物学会雑誌 32(2), 87-94, 2015
NAID 130005097977

Detection of the staphylococcal enterotoxin D-like gene from staphylococcal food poisoning isolates over the last two decades in Tokyo

Journal of Veterinary Medical Science 77(8), 905-911, 2015
NAID 130005094680

Related Pictures

Staphylococcal enterotoxin C2 molecule - Stock Image - F009/6242 - Science Photo Library Staphylococcal enterotoxin gene location and emetic activity. Adapted | Download Enterotoxins Crystal structure of staphylococcal enterotoxin N (SEN). The structure | Download

★リンクテーブル★

リンク元	「ブドウ球菌エンテロトキシン」
関連記事	「staphylococcal」「enterotoxins」「enterotoxin」

「ブドウ球菌エンテロトキシン」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Stap_Strp_tox_C
	identification of a secondary zinc-binding site in staphylococcal enterotoxin c2: implications for superantigen recognition
Identifiers
Symbol	Stap_Strp_tox_C
Pfam	PF02876
Pfam clan	CL0386
InterPro	IPR006123
PROSITE	PDOC00250
SCOP	1se3
SUPERFAMILY	1se3
OPM superfamily	429
OPM protein	1dyq
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary