Literature DB >> 9596778

Formation of ring-shaped structures on erythrocyte membranes after treatment with botulinolysin, a thiol-activated hemolysin from Clostridium botulinum.

K Sekiya1, H Danbara, Y Futaesaku, A Haque, N Sugimoto, M Matsuda.   

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.

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Year:  1998        PMID: 9596778      PMCID: PMC108300          DOI: 10.1128/IAI.66.6.2987-2990.1998

Source DB:  PubMed          Journal:  Infect Immun        ISSN: 0019-9567            Impact factor:   3.441


  31 in total

1.  Ring formation of perfringolysin O as revealed by negative stain electron microscopy.

Authors:  K Mitsui; T Sekiya; S Okamura; Y Nozawa; J Hase
Journal:  Biochim Biophys Acta       Date:  1979-12-12

2.  Alteration of human erythrocyte plasma membranes by perfringolysin O as revealed by freeze-fracture electron microscopy. Studies on Clostridium perfringens exotoxins V.

Authors:  K Mitsui; T Sekiya; Y Nozawa; J Hase
Journal:  Biochim Biophys Acta       Date:  1979-06-13

3.  Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form.

Authors:  J Rossjohn; S C Feil; W J McKinstry; R K Tweten; M W Parker
Journal:  Cell       Date:  1997-05-30       Impact factor: 41.582

4.  Alteration by cereolysin of the structure of cholesterol-containing membranes.

Authors:  J L Cowell; K S Kim; A W Bernheimer
Journal:  Biochim Biophys Acta       Date:  1978-02-21

5.  Isolation and identification of two hemolytic forms of streptolysin-O.

Authors:  S Bhakdi; M Roth; A Sziegoleit; J Tranum-Jensen
Journal:  Infect Immun       Date:  1984-11       Impact factor: 3.441

Review 6.  Streptococcal toxins (streptolysin O, streptolysin S, erythrogenic toxin).

Authors:  J E Alouf
Journal:  Pharmacol Ther       Date:  1980       Impact factor: 12.310

7.  Evidence for membrane cholesterol as the common binding site for cereolysin, streptolysin O and saponin.

Authors:  S Shany; A W Bernheimer; P S Grushoff; K S Kim
Journal:  Mol Cell Biochem       Date:  1974-05-30       Impact factor: 3.396

8.  Binding of cholesterol by sulfhydryl-activated cytolysins.

Authors:  M K Johnson; C Geoffroy; J E Alouf
Journal:  Infect Immun       Date:  1980-01       Impact factor: 3.441

9.  Botulinolysin, a thiol-activated hemolysin produced by Clostridium botulinum, inhibits endothelium-dependent relaxation of rat aortic ring.

Authors:  N Sugimoto; A Haque; Y Horiguchi; M Matsuda
Journal:  Toxicon       Date:  1997-07       Impact factor: 3.033

10.  Effect of streptolysin O on erythrocyte membranes, liposomes, and lipid dispersions. A protein-cholesterol interaction.

Authors:  J L Duncan; R Schlegel
Journal:  J Cell Biol       Date:  1975-10       Impact factor: 10.539

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  2 in total

Review 1.  Role of pore-forming toxins in bacterial infectious diseases.

Authors:  Ferdinand C O Los; Tara M Randis; Raffi V Aroian; Adam J Ratner
Journal:  Microbiol Mol Biol Rev       Date:  2013-06       Impact factor: 11.056

Review 2.  Botulinum toxins--cause of botulism and systemic diseases?

Authors:  H Böhnel; F Gessler
Journal:  Vet Res Commun       Date:  2005-05       Impact factor: 2.459

  2 in total

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