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The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components
Magalhães, Caroline A; Rossato, Sarita S; Barbosa, Ângela S; Santos, Thiago O dos; Elias, Waldir P; Sircili, Marcelo P; Piazza, Roxane MF.
  • Magalhães, Caroline A; Instituto Butantan. Laboratório de Bacteriologia. São Paulo. BR
  • Rossato, Sarita S; Instituto Butantan. Laboratório de Bacteriologia. São Paulo. BR
  • Barbosa, Ângela S; Instituto Butantan. Laboratório de Bacteriologia. São Paulo. BR
  • Santos, Thiago O dos; Instituto Butantan. Laboratório de Bacteriologia. São Paulo. BR
  • Elias, Waldir P; Instituto Butantan. Laboratório de Bacteriologia. São Paulo. BR
  • Sircili, Marcelo P; Instituto Butantan. Laboratório de Bacteriologia. São Paulo. BR
  • Piazza, Roxane MF; Instituto Butantan. Laboratório de Bacteriologia. São Paulo. BR
Mem. Inst. Oswaldo Cruz ; 106(2): 146-152, Mar. 2011. ilus, graf, tab
Article in English | LILACS, SES-SP | ID: lil-583937
ABSTRACT
Typical and atypical enteropathogenic Escherichia coli (EPEC) are considered important bacterial causes of diarrhoea. Considering the repertoire of virulence genes, atypical EPEC (aEPEC) is a heterogeneous group, harbouring genes that are found in other diarrheagenic E. coli pathotypes, such as those encoding haemolysins. Haemolysins are cytolytic toxins that lyse host cells disrupting the function of the plasma membrane. In addition, these cytolysins mediate a connection to vascular tissue and/or blood components, such as plasma and cellular fibronectin. Therefore, we investigated the haemolytic activity of 72 aEPEC isolates and determined the correlation of this phenotype with the presence of genes encoding enterohaemolysins (Ehly) and cytolysin A (ClyA). In addition, the correlation between the expression of haemolysins and the ability of these secreted proteins to adhere to extracellular matrix (ECM) components was also assessed in this study. Our findings demonstrate that a subset of aEPEC presents haemolytic activity due to the expression of Ehlys and/or ClyA and that this activity is closely related to the ability of these isolates to bind to ECM components.
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Full text: Available Index: LILACS (Americas) Main subject: Escherichia coli Proteins / Extracellular Matrix / Enteropathogenic Escherichia coli Limits: Animals / Humans Language: English Journal: Mem. Inst. Oswaldo Cruz Year: 2011 Type: Article / Project document Institution/Affiliation country: Instituto Butantan/BR

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Full text: Available Index: LILACS (Americas) Main subject: Escherichia coli Proteins / Extracellular Matrix / Enteropathogenic Escherichia coli Limits: Animals / Humans Language: English Journal: Mem. Inst. Oswaldo Cruz Year: 2011 Type: Article / Project document Institution/Affiliation country: Instituto Butantan/BR