Mechanism of membrane insertion of a multimeric β-barrel protein: Perfringolysin O creates a pore using ordered and coupled conformational changes

Molecular Cell

Volumn 6, Issue 5, 2000, Pages 1233-1242

  Heuck, Alejandro P ^a   Hotze, Eileen M ^b   Tweten, Rodney K ^b   Johnson, Arthur E ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

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

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; CLOSTRIDIUM PERFRINGENS TOXIN; UNCLASSIFIED DRUG;

ARTICLE; BILAYER MEMBRANE; BINDING KINETICS; CHANNEL GATING; CLOSTRIDIUM PERFRINGENS; CYTOLYSIS; MEMBRANE BINDING; NONHUMAN; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN INTERACTION;

EID: 0033636662     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)00119-2     Document Type: Article

References (33)

1. Extension of the parallax analysis of membrane penetration depth to the polar region of model membranes: Use of fluorescence quenching by a spin-label attached to the phospholipid polar headgroup
2. Introduction to the family of the structurally related cholesterol-binding cytolysins ('sulfhydryl-activated' toxins)
3. The family of the antigenically-related cholesterol-binding ('sulphydryl-activated') cytolytic toxins
4. Cholesterol-dependent tetanolysin damage to liposomes
5. Interactions between membranes and cytolytic bacterial toxins
6. Proteinaceous bacterial toxins and pathogenesis of sepsis syndrome and septic shock: The unknown connection
7. Mechanism of membrane damage by streptolysin-O
8. Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
9. Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β-barrel
10. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
11. Streptolysin O: Inhibition of the conformational change during membrane binding of the monomor prevents oligomerization and pore formation
12. Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae
13. Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae
14. The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane
15. Fluoresceinthiocarbamylinsulin: A potential analytical tool for the assay of disulfide bond reduction
16. Effect of isolated C-terminal fragment of θ-toxin (perfringolysin O) on toxin assembly and membrane lysis
17. Listeriolysin O: Cholesterol inhibits cytolysis but not binding to cellular membranes
18. Structure and mechanism of carbonic anhydrase
19. Pneumolysin: Structure, function and role in disease
20. Interaction of θ-toxin (Perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: Change in the aromatic side chains upon binding and insertion
21. Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
22. Kinetics of streptolysin O self-assembly
23. Crystal structure of the anthrax toxin protective antigen
24. Interaction of streptolysin O with sterols
25. Effect of streptolysin O and digitonin on egg lecithin/cholesterol vesicles
26. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
27. Perfringolysin O
28. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
29. 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
30. The mechanism of pore assembly for a cholesterol-dependent cytolysin: Formation of a large prepore complex precedes the insertion of the transmembrane β-hairpins
31. Nucleotide sequence of the gene for perfringolysin O (theta-toxin) from Clostridium perfringens: Significant homology with the genes for streptolysin O and pneumolysin
32. Pore-forming toxins of gram-positive bacteria
33. Isolation of a tryptic fragment from Clostridium perfringens θ-toxin that contains sites for membrane binding and self-aggregation