| 词条 | Bacillus haemolytic enterotoxin |
| 释义 |
| Symbol = Bacillus_HBL | Name = Bacillus_HBL | image = | width = | caption = crystal structure of hemolysin binding component from bacillus cereus | Pfam = PF05791 | Pfam_clan = | InterPro = IPR008414 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = 1.C.41 | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, the Bacillus haemolytic enterotoxin family of proteins consists of several Bacillus haemolytic enterotoxins (HblC, HblD, HblA, NheA, and NheB), which can cause food poisoning in humans.[1] Haemolysin BL (encoded by HBL) and non-haemolytic enterotoxin (encoded by NHE), represent the major enterotoxins produced by Bacillus cereus. Most of the cytotoxic activity of B. cereus isolates has been attributed to the level of Nhe, which may indicate a highly diarrheic potential.[2] The exact mechanism by which B. cereus causes diarrhoea is unknown. Hbl, cytotoxin K (CytK) and Nhe are all putative causes. Both Hbl and Nhe are three-component cytotoxins composed of a binding component, B, and two lytic components, L1 and L2. All three subunits act synergically to cause hemolysis. Maximal cytotoxicity of Nhe against epithelia is dependent on all three components. Nhe has haemolytic activity against erythrocytes from a variety of species. It is possible that the common structural and functional properties of these toxins indicate that the Hbl/Nhe and ClyA families of toxins constitute a superfamily of pore-forming cytotoxins.[3] Haemolysin BL and non-haemolytic enterotoxin production are both influenced by pH and micro.[4] References1. ^{{cite journal |vauthors=Phelps RJ, McKillip JL | title = Enterotoxin production in natural isolates of Bacillaceae outside the Bacillus cereus group | journal = Appl. Environ. Microbiol. | volume = 68 | issue = 6 | pages = 3147–51 |date=June 2002 | pmid = 12039781 | pmc = 123918 | doi = 10.1128/aem.68.6.3147-3151.2002| url = }} {{InterPro content|IPR008414}}2. ^{{cite journal |vauthors=Moravek M, Dietrich R, Buerk C, Broussolle V, Guinebretiere MH, Granum PE, Nguyen-The C, Martlbauer E | title = Determination of the toxic potential of Bacillus cereus isolates by quantitative enterotoxin analyses | journal = FEMS Microbiol. Lett. | volume = 257 | issue = 2 | pages = 293–8 |date=April 2006 | pmid = 16553866 | doi = 10.1111/j.1574-6968.2006.00185.x | url = }} 3. ^{{cite journal |vauthors=Fagerlund A, Lindback T, Storset AK, Granum PE, Hardy SP | title = Bacillus cereus Nhe is a pore-forming toxin with structural and functional properties similar to the ClyA (HlyE, SheA) family of haemolysins, able to induce osmotic lysis in epithelia | journal = Microbiology | volume = 154 | issue = Pt 3 | pages = 693–704 |date=March 2008 | pmid = 18310016 | doi = 10.1099/mic.0.2007/014134-0 | url = }} 4. ^{{cite journal |vauthors=Thomassin S, Jobin MP, Schmitt P | title = The acid tolerance response of Bacillus cereus ATCC14579 is dependent on culture pH, growth rate and intracellular pH | journal = Arch. Microbiol. | volume = 186 | issue = 3 | pages = 229–39 |date=September 2006 | pmid = 16906407 | doi = 10.1007/s00203-006-0137-1 | url = }} 1 : Protein families |
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