The family of thiol-activated, cholesterol-binding cytolysins

Toxicon

Volumn 39, Issue 11, 2001, Pages 1681-1689

  Palmer, M ^a  

^a TEXAS A M COLLEGE OF MEDICINE   (United States)

Author keywords

Cholesterol binding; Membrane permeabilization; Pore formation; Pore forming toxins

Indexed keywords

CELL SURFACE RECEPTOR; CHOLESTEROL; CYTOLYSIN; LISTERIOLYSIN; PERFRINGOLYSIN; PNEUMOLYSIN; POLYSACCHARIDE; STREPTOLYSIN O; THIOL DERIVATIVE; UNCLASSIFIED DRUG; VACCINE;

AMINO ACID SEQUENCE; ARCANOBACTERIUM; BACILLUS; BIODIVERSITY; CHANNEL GATING; CLOSTRIDIUM; CRYSTAL STRUCTURE; CYTOLOGY; HOST CELL; LISTERIA MONOCYTOGENES; LYSOSOME; MACROMOLECULE; MEMBRANE DAMAGE; MEMBRANE PERMEABILITY; NONHUMAN; OLIGOMERIZATION; PATHOGENICITY; PHAGOSOME; PRIORITY JOURNAL; PROTEIN BINDING; REVIEW; SEQUENCE HOMOLOGY; STREPTOCOCCUS; STRUCTURE ACTIVITY RELATION; VACCINATION;

ANIMALIA; BACTERIA (MICROORGANISMS); CLOSTRIDIUM; LISTERIA MONOCYTOGENES; STREPTOCOCCUS;

EID: 0034877296     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(01)00155-6     Document Type: Article

References (87)

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4. Permeabilization of the erythrocyte membrane with streptolysin O allows access to the vacuolar membrane of Plasmodium falciparum and a molecular analysis of membrane topology
5. pH-dependent perforation of macrophage phagosomes by listeriolysin O from Listeria monocytogenes
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10. On the cause and nature of C9-related heterogeneity of terminal complement complexes generated on target erythrocytes through the action of whole serum
11. Mechanism of membrane damage by streptolysin-O
12. The Arcanobacterium (Actinomyces) pyogenes hemolysin, pyolysin, is a novel member of the thiol-activated cytolysin family
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16. The potential to use PspA and other pneumococcal proteins to elicit protection against pneumococcal infection
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31. Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae
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33. The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane
34. Cholesterol-Streptolysin O-interaction: An EM study of wild-type and mutant Streptolysin O
35. Mechanism of membrane insertion of a multimeric beta-barrel protein. Perfringolysin O creates a pore using ordered and coupled conformational changes
36. Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane β-sheet from a prepore intermediate
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38. Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens
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42. Structure and molecular mechanism of a functional form of pneumolysin: A cholesterol-dependent cytolysin from Streptococcus pneumoniae
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45. A genetic approach to demonstrate the role of listeriolysin O in the virulence of Listeria monocytogenes
46. Attenuated mutants of the intracellular bacterium Listeria monocytogenes obtained by single amino acid substitutions in listeriolysin O
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48. A synthetic peptide administered with IL-12 elicits immunity to Listeria monocytogenes
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50. Subunit organisation and symmetry of pore-forming, oligomeric pneumolysin
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52. Distribution of the intermedilysin gene among the anginosus group streptococci and correlation between intermedilysin production and deep-seated infection with Streptococcus intermedius
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54. Immunization of mice with combinations of pneumococcal virulence proteins elicits enhanced protection against challenge with Streptococcus pneumoniae
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56. Protease-nicked theta-toxin of Clostridium perfringens, a new membrane probe with no cytolytic effect, reveals two classes of cholesterol as toxin-binding sites on sheep erythrocytes
57. A cytolysin, theta-toxin, preferentially binds to membrane cholesterol surrounded by phospholipids with 18-carbon hydrocarbon chains in cholesterol-rich region
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71. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
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73. The mechanism of pore assembly for a cholesterol-dependent cytolysin: Formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins
74. C-terminal amino acid residues are required for the folding and cholesterol binding property of perfringolysin O, a pore-forming cytolysin
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76. Ultrastructure of the membrane attack complex of complement. Heterogeneity of the complex caused by different degree of C9 polymerization
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78. Transmembrane beta-barrel of staphylococcal alpha-toxin forms in sensitive but not in resistant cells
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82. Pore-forming toxins trigger shedding of receptors for interleukin 6 and lipopolysaccharide
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87. Coupling of cholesterol and cone-shaped lipids in bilayers augments membrane permeabilization by the cholesterol-specific toxins Streptolysin O and Vibrio cholerae cytolysin