Formation of Ring-Shaped Structures on Erythrocyte Membranes after Treatment with Botulinolysin, a Thiol-Activated Hemolysin from Clostridium botulinum

@article{Sekiya1998FormationOR,
  title={Formation of Ring-Shaped Structures on Erythrocyte Membranes after Treatment with Botulinolysin, a Thiol-Activated Hemolysin from Clostridium botulinum},
  author={Kachiko Sekiya and Hirofumi Danbara and Yutaka Futaesaku and Abdul Haque and Nakaba Sugimoto and Morihiro Matsuda},
  journal={Infection and Immunity},
  year={1998},
  volume={66},
  pages={2987 - 2990}
}
ABSTRACT Damage to erythrocyte membranes by botulinolysin (BLY) was studied by electron microscopy, which revealed ring-shaped structures with inner diameters and widths of approximately 32 and 6.7 nm, respectively. BLY bound to membranes at 0°C, but subsequent treatment with glutaraldehyde prevented ring formation during further incubation at 37°C. Zn2+ ions inhibited ring formation but not binding of BLY to membranes. 
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This study investigates the molecular mechanism of cooperation between hemolysin and phospholipases and proposes a model involving interactions between proteins that increase the affinity of cytolysins for the membrane as well direct enzymatic enhancement of lysis.
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The cholesterol-dependent cytolyslns (CDCs) are a group of toxins produced by several genera of Gram-positive bacteria, that bind to and form large oligomeric pores in target cell membranes that contain cholesterol, and are being used in a diverse array of applications that utilise their pore-forming and toxic properties.
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This study investigates the molecular mechanism of cooperation between hemolysin and phospholipases and proposes a model involving interactions between proteins that increase the affinity of cytolysins for the membrane as well direct enzymatic enhancement of lysis.
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In vivo actions of different botulinum toxins after their entry into the organism may contribute to the onset of different diseases of hitherto cryptogenic origin.
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Common functions of PFTs include disruption of epithelial barrier function and evasion of host immune responses, which contribute to bacterial growth and spreading, make this group of toxins an attractive target for the development of new virulence-targeted therapies that may have broad activity against human pathogens.
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