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Updated: Jul 18, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
EspC, an autotransporter protein secreted by enteropathogenic Escherichia coli (EPEC), displays protease activity on
Maria Elisa Drago-Serrano1, Sandra Gavilanes Parra, H Angel Manjarrez-Hernández
1Departmento de Sistemas Biológicos, UAM-Xochimilco, México D.F., Mexico.
Abstract:
Some enteropathogenic Escherichia coli (EPEC) strains, which are an important cause of diarrhea among infants, secrete a serine protease autotransporter protein called EspC. The pathogenic role of EspC upon EPEC infection is unknown. In this study, we demonstrated that purified EspC protein, obtained from supernatants of EPEC cultures, interacted with hemoglobin and degraded it. Moreover, we have shown that EspC is a hemin-binding protein. We hypothesized that hemoglobin proteolysis by EspC may contribute to the utilization of heme and hemoglobin iron for bacterial growth.
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