Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/195574
Type: Artigo de periódico
Title: Thiol-independent Activity Of A Cholesterol-binding Enterohemolysin Produced By Enteropathogenic Escherichia Coli.
Author: Figueirêdo, P M S
Catani, C F
Yano, T
Abstract: Enterohemolysin produced by Escherichia coli associated with infant diarrhea showed characteristics similar to those of thiol-activated hemolysins produced by Gram-positive bacteria, including inactivation by cholesterol, lytic activity towards eukaryotic cells and thermoinstability. However, enterohemolysin activity was not inactivated by oxidation or by SH group-blocking agents (1 mM HgCl2, 1 mM iodoacetic acid) and the hemolysin (100 microg/ml) was not lethal to mice, in contrast to the lethality of the thiol-activated hemolysin family to animals. Earlier reports showed that intravenous injection of partially purified streptolysin O preparations (0.2 microg) was rapidly lethal to mice. These results suggest that E. coli enterohemolysin is not a thiol-activated hemolysin, despite its ability to bind cholesterol, probably due to the absence of free thiol-group(s) that characterize the active form of the thiol-activated hemolysin molecule.
Subject: Animals
Bacterial Toxins
Cell Membrane
Cholesterol
Electrophoresis, Polyacrylamide Gel
Erythrocytes
Escherichia Coli
Escherichia Coli Proteins
Eukaryotic Cells
Hemolysin Proteins
Hemolysis
Male
Mice
Protein Binding
Rights: aberto
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/14576905
Date Issue: 2003
Appears in Collections:Unicamp - Artigos e Outros Documentos

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