» Articles » PMID: 8955326

Electron Microscopic Evaluation of a Two-step Theory of Pore Formation by Streptolysin O

Overview
Journal J Bacteriol
Specialty Microbiology
Date 1996 Dec 1
PMID 8955326
Citations 5
Authors
Affiliations
Soon will be listed here.
Abstract

The formation of pores by streptolysin O (SLO) was analyzed in erythrocyte membranes and liposomes by immunoelectron microscopy and electron spectroscopic imaging. The binding of SLO molecules to membranes was temperature independent, while the polymerization of SLO molecules was temperature dependent. Our results also suggest that proteins in erythrocyte membranes are not involved in the formation of SLO rings.

Citing Articles

PNC-27, a Chimeric p53-Penetratin Peptide Binds to HDM-2 in a p53 Peptide-like Structure, Induces Selective Membrane-Pore Formation and Leads to Cancer Cell Lysis.

Sarafraz-Yazdi E, Mumin S, Cheung D, Fridman D, Lin B, Wong L Biomedicines. 2022; 10(5).

PMID: 35625682 PMC: 9138867. DOI: 10.3390/biomedicines10050945.


Crystal structure of Clostridium perfringens enterotoxin displays features of beta-pore-forming toxins.

Kitadokoro K, Nishimura K, Kamitani S, Fukui-Miyazaki A, Toshima H, Abe H J Biol Chem. 2011; 286(22):19549-55.

PMID: 21489981 PMC: 3103334. DOI: 10.1074/jbc.M111.228478.


Molecular features of the cytolytic pore-forming bacterial protein toxins.

ALOUF J Folia Microbiol (Praha). 2003; 48(1):5-16.

PMID: 12744072 DOI: 10.1007/BF02931271.


Sizing the holin lesion with an endolysin-beta-galactosidase fusion.

Wang I, Deaton J, Young R J Bacteriol. 2003; 185(3):779-87.

PMID: 12533453 PMC: 142811. DOI: 10.1128/JB.185.3.779-787.2003.


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

Sekiya K, Danbara H, Futaesaku Y, Haque A, Sugimoto N, Matsuda M Infect Immun. 1998; 66(6):2987-90.

PMID: 9596778 PMC: 108300. DOI: 10.1128/IAI.66.6.2987-2990.1998.

References
1.
Duncan J, Schlegel R . Effect of streptolysin O on erythrocyte membranes, liposomes, and lipid dispersions. A protein-cholesterol interaction. J Cell Biol. 1975; 67(1):160-74. PMC: 2109585. DOI: 10.1083/jcb.67.1.160. View

2.
Prigent D, ALOUF J . Interaction of steptolysin O with sterols. Biochim Biophys Acta. 1976; 443(2):288-300. DOI: 10.1016/0005-2736(76)90511-3. View

3.
Cowell J, Kim K, BERNHEIMER A . Alteration by cereolysin of the structure of cholesterol-containing membranes. Biochim Biophys Acta. 1978; 507(2):230-41. DOI: 10.1016/0005-2736(78)90419-4. View

4.
Johnson M, Geoffroy C, ALOUF J . Binding of cholesterol by sulfhydryl-activated cytolysins. Infect Immun. 1980; 27(1):97-101. PMC: 550729. DOI: 10.1128/iai.27.1.97-101.1980. View

5.
Wannamaker L . Streptococcal toxins. Rev Infect Dis. 1983; 5 Suppl 4:S723-32. DOI: 10.1093/clinids/5.supplement_4.s723. View