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The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components.

Memorias do Instituto Oswaldo Cruz (2011-05-04)
Caroline A Magalhães, Sarita S Rossato, Angela S Barbosa, Thiago O dos Santos, Waldir P Elias, Marcelo P Sircili, Roxane M F Piazza
RÉSUMÉ

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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Carboxypeptidase Y from baker′s yeast (S. cerevisiae), lyophilized powder, ≥50 units/mg protein