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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

44 Perfringolysin O, a bacterial cytolytic toxin, forms unu

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

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

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

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

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

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

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

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

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

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

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