ライフサイエンスコーパス: perfringolysin

1 Clostridium perfringens perfringolysin O (PFO or theta-toxin) is a cytolytic tox

2 X) although most type B strains also produce perfringolysin O (PFO) and beta2 toxin (CPB2).

3 holesterol-binding bacterial toxin proteins, perfringolysin O (PFO) and domain 4 of anthrolysin O (AL

4 has four domains and is globally similar to perfringolysin O (PFO) and intermedilysin (ILY), yet the

5 Two cholesterol-binding CDCs, perfringolysin O (PFO) and streptolysin O (SLO), were fo

6 The cholesterol-dependent cytolysin Perfringolysin O (PFO) constitutes a powerful tool to de

7 ridium perfringens phospholipase C (PLC) and perfringolysin O (PFO) differentially induced human umbi

8 embrane interactive structures at the tip of perfringolysin O (PFO) domain 4 reveals that a threonine

9 mum) beta toxin (CPB), alpha toxin (CPA) and perfringolysin O (PFO) during log-phase growth.

10 odel built on the basis of its homology with perfringolysin O (PFO) for which there is an atomic stru

11 Upon interaction with cholesterol, perfringolysin O (PFO) inserts into membranes and forms

12 Perfringolysin O (PFO) is a member of the cholesterol-de

13 Perfringolysin O (PFO) is a prototype of the large famil

14 Perfringolysin O (PFO) is a sterol-dependent, pore-formi

15 Perfringolysin O (PFO) is a toxic protein that binds to

16 The cholesterol-dependent cytolysin perfringolysin O (PFO) is secreted by Clostridium perfri

17 Perfringolysin O (PFO) is the prototype for the choleste

18 The sterol-binding protein perfringolysin O (PFO) was used to test this hypothesis.

19 generate an (125)I-labeled mutant version of Perfringolysin O (PFO), a cholesterol-binding protein, a

20 Perfringolysin O (PFO), a cholesterol-dependent cytolysi

21 Perfringolysin O (PFO), a member of the cholesterol-depe

22 dered lipid domains (rafts) was tested using perfringolysin O (PFO), a pore-forming cholesterol-depen

23 e translocation process, we examined whether perfringolysin O (PFO), a pore-forming protein related t

24 Perfringolysin O (PFO), a water-soluble monomeric cytoly

25 in SLO to that of the well-characterized CDC perfringolysin O (PFO), although the sequences in this r

26 erobic C. perfringens, alpha-toxin (PLC) and perfringolysin O (PFO), are thought to be important in t

27 g agent composed of the pore-forming protein Perfringolysin O (PFO), potent silencing was achieved in

28 In contrast, perfringolysin O (PFO), secreted by Clostridium perfring

29 r residues from a pH-insensitive orthologue, perfringolysin O (PFO), we identified leucine 461 as uni

30 protein toxins, particularly alpha-toxin and perfringolysin O (PFO).

31 pathogen which secretes a related cytolysin, perfringolysin O (PFO).

32 ore-forming, cholesterol-dependent cytolysin perfringolysin O (PFO).

33 nding by a modified version of the cytolysin perfringolysin O (PFO*), whereas another pool is sequest

34 ns, contain the genes for alpha toxin (plc), perfringolysin O (pfoA), beta toxin (cpb), and sometimes

35 aponin (SAP), digitonin (DIG) or recombinant perfringolysin O (rPFO) (XF-plasma membrane permeabilize

36 eveals that only large pores are produced by perfringolysin O and streptolysin O during insertion (an

37 he sterol-specific toxins streptolysin O and perfringolysin O and subsequent cytotoxicity.

38 ion of chromosomally encoded alpha-toxin and perfringolysin O by C. perfringens, as well as sporulati

39 showed reduced production of alpha-toxin and perfringolysin O during vegetative growth.

40 during the prepore-to-pore transition of the perfringolysin O oligomer.

41 vation of the genes encoding alpha toxin and perfringolysin O only slightly decreased the lethality o

42 l chemical activity and its accessibility to perfringolysin O or membrane sensors like Scap.

43 Our results demonstrate that perfringolysin O perforation is a valuable tool for stru

44 sistant to pneumolysin and the related toxin perfringolysin O relative to healthy red blood cells.

45 The structure of the monomeric form of perfringolysin O solved by X-ray crystallography has bee

46 n study native capsid structure, we used the perfringolysin O to perforate the membrane of HIV-1 part

47 Transfer of the sequence to perfringolysin O transformed this toxic cytolysin into a

48 relation between ETX (but not alpha-toxin or perfringolysin O) levels in late-log-phase genotype D su

49 Perfringolysin O, a bacterial cytolytic toxin, forms unu

50 cells permeabilized at high cell density by perfringolysin O, a pore-forming cytolysin.

51 determine the domain-specific topography of perfringolysin O, a pore-forming toxin, on a membrane su

52 as a prepore mechanism has been proposed for perfringolysin O, a very different mechanism has been pr

53 which the levels of alpha toxin, beta toxin, perfringolysin O, and beta2 toxin production were compar

54 lethal toxins, alpha toxin, beta toxin, and perfringolysin O, and several isolates also produced bet

55 CDC) family, which includes listeriolysin O, perfringolysin O, and streptolysin O.

56 ndent repair responses to streptolysin O and perfringolysin O, but only 50% of repair to intermedilys

57 re-forming toxins, such as streptolysin O or perfringolysin O, during septic cardiomyopathy or necrot

58 We found that the gene encoding toxin perfringolysin O, pfoA, was largely deficient in a human

59 utation was identified in the archetype CDC, perfringolysin O, that blocks detectable D3 structural c

60 that preserve the cholesterol specificity of perfringolysin O, the prototypical cholesterol-dependent

61 ecific membrane binding domain (D4) of toxin perfringolysin O, we demonstrated that ketamine induced

62 soluble cholesterol-binding bacterial toxin, perfringolysin O, we show that cholesterol accessibility

63 Using the archetype betaPFT perfringolysin O, we show that E183 of each monomer with

64 o bind 125I-PFO*, a mutant form of bacterial Perfringolysin O, which binds cholesterol in membranes;

65 duced cytotoxicity and that ceramide reduced perfringolysin O- but not streptolysin O-mediated cytoto

66 (ETX), enterotoxin, beta2-toxin (CPB2), and perfringolysin O.

67 cific activity exceeds that of the wild-type perfringolysin O.