title: Formation of ring-shaped structures on erythrocyte membranes after treatment with botulinolysin, a thiol-activated hemolysin from Clostridium botulinum.
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 degrees C, but subsequent treatment with glutaraldehyde prevented ring formation during further incubation at 37 degrees C. Zn2+ ions inhibited ring formation but not binding of BLY to membranes.
authors.affiliation: Department of Microbiology, School of Pharmaceutical Sciences, Kitasato University, Minato-ku, Tokyo 108-8641, Japan. sekiyak@platinum.pharm.kitasato-u.jp
authors.forename: K
authors.initials: K
authors.lastname: Sekiya
authors.forename: H
authors.initials: H
authors.lastname: Danbara
authors.forename: Y
authors.initials: Y
authors.lastname: Futaesaku
authors.forename: A
authors.initials: A
authors.lastname: Haque
authors.forename: N
authors.initials: N
authors.lastname: Sugimoto
authors.forename: M
authors.initials: M
authors.lastname: Matsuda
mesh_terms: D001427:Bacterial Toxins / Q000494:pharmacology*; D003014:Clostridium botulinum; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000473:pathology; D006460:Hemolysin Proteins / Q000378:metabolism / Q000494:pharmacology*; D009930:Organic Chemicals; D011485:Protein Binding; D013696:Temperature; D015032:Zinc / Q000494:pharmacology
chemical_list: D001427:Bacterial Toxins; D006460:Hemolysin Proteins; D009930:Organic Chemicals; C112565:botulinolysin; D015032:Zinc