| 词条 | Clostridium enterotoxin |
| 释义 |
| Symbol = Clenterotox | Name = Clostridium enterotoxin | image = 2QUO.pdb.jpg | width = | caption = Crystal Structure of C terminal fragment of Clostridium perfringens enterotoxin[1] | Pfam= PF03505 | InterPro= IPR003897 | SMART= | Prosite = | SCOP = | TCDB = 1.C.59 | OPM family= | OPM protein= | PDB= }}Clostridium enterotoxins are toxins produced by Clostridium species.[2] Clostridial species are one of the major causes of food poisoning/gastrointestinal illnesses. They are anaerobic,[1] gram-positive, spore-forming rods that occur naturally in the soil.[3] Among the family are: Clostridium botulinum, which produces one of the most potent toxins in existence; Clostridium tetani, causative agent of tetanus; and Clostridium perfringens, commonly found in wound infections and diarrhea cases. The use of toxins to damage the host is a method deployed by many bacterial pathogens. The major virulence factor of C. perfringens is the CPE enterotoxin, which is secreted upon invasion of the host gut, and contributes to food poisoning and other gastrointestinal illnesses.[3] It has a molecular weight of 35.3kDa, and is responsible for the disintegration of tight junctions between epithelial cells in the gut.[4] This mechanism is mediated by host claudin-3 and claudin-4 receptors, situated at the tight junctions.[5] Clostridium enterotoxin is a nine-stranded beta sheet sandwich in shape. It has been determined that it is very similar to other spore-forming bacteria.[1] The PFAM ID is a clenterotox.[6] The binding site is between beta sheets eight and nine. This allows the human claudin-3,4,6,7,8 and 14 to bind but not 1,2,5, and 10. The way the protein work is it destroys the cell membrane structure of animals by binding to claudin family proteins. These are components of tight junctions of the epithelial cell membrane.[1] References1. ^1 2 3 {{cite journal |vauthors=Van Itallie CM, Betts L, Smedley JG, McClane BA, Anderson JM |title=Structure of the claudin-binding domain of Clostridium perfringens enterotoxin |journal=J. Biol. Chem. |volume=283 |issue=1 |pages=268–74 |date=January 2008 |pmid=17977833 |doi=10.1074/jbc.M708066200 |url=}} {{Toxins}}{{InterPro content|IPR003897}}2. ^{{cite journal |vauthors=Katahira J, Sugiyama H, Inoue N, Horiguchi Y, Matsuda M, Sugimoto N |title=Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo |journal=The Journal of Biological Chemistry |volume=272 |issue=42 |pages=26652–8 |date=October 1997 |pmid=9334247 |doi= 10.1074/jbc.272.42.26652|url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=9334247}} 3. ^1 {{cite journal |vauthors=Czeczulin JR, Hanna PC, Mcclane BA |title=Cloning, nucleotide sequencing, and expression of the Clostridium perfringens enterotoxin gene in Escherichia coli |journal=Infect. Immun. |volume=61 |issue=8 |pages=3429–3439 |year=1993 |pmid=8335373 |pmc=281020}} 4. ^{{cite journal |vauthors=Katahira J, Inoue N, Horiguchi Y, Matsuda M, Sugimoto N |title=Molecular cloning and functional characterization of the receptor for Clostridium perfringens enterotoxin |journal=J. Cell Biol. |volume=136 |issue=6 |pages=1239–1247 |year=1997 |pmid=9087440 |doi=10.1083/jcb.136.6.1239 |pmc=2132509}} 5. ^{{cite journal |vauthors=Long H, Crean CD, Lee WH, Cummings OW, Gabig TG |title=Expression of Clostridium perfringens enterotoxin receptors claudin-3 and claudin-4 in prostate cancer epithelium |journal=Cancer Research |volume=61 |issue=21 |pages=7878–81 |date=November 2001 |pmid=11691807 |doi= |url=http://cancerres.aacrjournals.org/cgi/pmidlookup?view=long&pmid=11691807}} 6. ^{{cite web |url=http://pfam.sanger.ac.uk/family?acc=PF03505 |title=Pfam: Family: Clenterotox (PF03505) |format= |work= |accessdate=}} 2 : Bacterial toxins|Gas gangrene |
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