The cholesterol-dependent cytolysins

Current Topics in Microbiology and Immunology

Volumn 257, Issue , 2000, Pages 15-33

  Tweten, R K ^a   Parker, M W ^b   Johnson, A E ^c  

^a UNIVERSITY OF OKLAHOMA COLLEGE OF MEDICINE   (United States)

^b ST VINCENT'S INSTITUTE OF MEDICAL RESEARCH   (Australia)

^c TEXAS A AND M UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; CYTOLYSIN;

CHANNEL GATING; CRYSTAL STRUCTURE; CYTOLYSIS; NOMENCLATURE; NONHUMAN; PRIORITY JOURNAL; RECEPTOR BINDING; REVIEW; STRUCTURE ANALYSIS; TOXIN ANALYSIS; TOXIN STRUCTURE;

AMINO ACID SEQUENCE; BACTERIAL TOXINS; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CHOLESTEROL; CLOSTRIDIUM PERFRINGENS; CYTOTOXINS; HEMOLYSIN PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN FOLDING; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS);

EID: 0034468770     PISSN: 0070217X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (63)

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9. The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
10. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
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13. Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to listeriolysin-O, perfringolysin-O, pneumolysin, and streptolysin-O and contains a single cysteine
14. Purification and characterization of streptolysin O secreted by Streptococcus equisimilis (group C)
15. Studies on the structure and mechanism of a bacterial protein toxin by analytical ultracentrifugation and small-angle neutron scattering
16. Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae
17. Clostridium septicum alpha toxin uses GPI-anchored proteins receptors
18. Listeriolysin genes: Complete sequence of ILO from Listeria ivanovii and of ISO from Listeria seeligeri
19. The aqueous pore through the translocon has a diameter of 40-60Å during cotranslational protein translocation at the ER membrane
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26. The conserved undecapeptide shared by thiol-activated cytolysins is involved in membrane binding
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29. Intermedilysin, a novel cytotoxin specific for human cells secreted by Streptococcus intermedius UNS46 isolated from a human liver abscess
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32. Cold-labile hemolysin produced by limited proteolysis of theta-toxin from Clostridium perfringens
33. Protease nicked q-toxin of Clostridium perfringens, a new membrane probe with no cytolytic effect, reveals two classes of cholesterol as toxin-binding sites on sheep erythrocytes
34. A modified q-toxin produced by limited proteolysis and methylation: A probe for the functional study of membrane cholesterol
35. A cytolysin, theta-toxin, preferentially binds to membrane cholesterol surrounded by phospholipids with 18-carbon hydrocarbon chains in cholesterol-rich region
36. The projection structure of perfringolysin-O (Clostridium Perfringens theta-toxin)
37. Crystal structure of Staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
38. A role in cell-binding for the C-terminus of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae
39. Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis
40. Assembly mechanism of the oligomeric streptolysin O pore: The early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization
41. Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis
42. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
43. The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins
44. Crystal structure of the anthrax toxin protective antigen
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46. Interaction of streptolysin O with sterols
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48. Structural characteristics of tetanolysin and its binding to lipid vesicles
49. Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require a thiol group for in vitro activity
50. Contribution of individual tryptophan residues to the structure and activity of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin
51. A ring-shaped structure with a crown formed by streptolysin-O on the erythrocyte membrane
52. Electron microscopic evaluation of a two-step theory of pore formation by streptolysin O
53. Generation of a membrane-bound, oligomerized prepore complex is necessary for pore formation by Clostridium septicum alpha toxin
54. The mechanism of membrane insertion for a cholesterol dependent cytolysin: A novel paradigm for pore-forming toxins
55. Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: An α-helical to β-sheet transition identified by fluorescence spectroscopy
56. The mechanism of assembly and insertion of the membrane complex of the cholesterol-dependent cytolysin perfringolysin O: Formation of a large prepore complex
57. C-terminal amino acid residues are required for the folding and cholesterol binding property of perfringolysin O, a pore-forming cytolysin
58. Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
59. Nucleotide sequence of the gene for perfringolysin O (theta-toxin) from Clostridium perfringens: Significant homology with the genes for streptolysin O and pneumolysin
60. Isolation of a tryptic fragment from Clostridium perfringens q-toxin that contains sites for membrane binding and self-aggregation
61. Oligomerization of the channel-forming toxin aerolysin precedes insertion into lipid bilayers
62. Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumoniae
63. Sterol structural requirements for inhibition of streptolysin O activity