The N-Terminal Domain of EspF Induces Host Cell Apoptosis after Infection with Enterohaemorrhagic Escherichia coli O157:H7Reportar como inadecuado




The N-Terminal Domain of EspF Induces Host Cell Apoptosis after Infection with Enterohaemorrhagic Escherichia coli O157:H7 - Descarga este documento en PDF. Documentación en PDF para descargar gratis. Disponible también para leer online.

Enterohemorrhagic Escherichia coli EHEC employs a type III secretion system TTSS to export the translocator and effector proteins required for mucosal colonization. As an important bacterial effector protein in locus of enterocyte effacement four, the EspF protein causes F-actin filament aggregations to form attaching and effacing A-E lesions, and induces the destruction of brush-border microvilli and cytoskeletal rearrangements to form pedestals. However, the molecular pathogenesis of A-E lesions due to EHEC O157:H7 infection is unclear. In this study, we constructed an espF-deficient mutant ΔespF with a 162-bp deletion in the N-terminal domain by using overlap extension PCR. The results showed that EHEC EspF translocated into intestinal epithelial cells, targeted mitochondria and induced apoptosis. The ΔespF mutant, compared to EHEC prototype Guangzhou strain, had lower cell attachment and effacement abilities, lower caspase-9-3 and lactate dehydrogenase levels, lower bacterial adhesion, weaker mitochondria apoptosis, and a higher mouse survival rate. Our results demonstrate the probable function of the EspF N-terminal domain, which targets mitochondria and binds mitochondria heat shock protein 70 to induce cell apoptosis via A-E lesions. These findings may be invaluable in clarifying the molecular pathogenesis of EspF of EHEC O157:H7.



Autor: Suhui Zhao , Ying Zhou , Chunhui Wang , Yu Yang, Xianbo Wu, Yao Wei, Li Zhu, Wei Zhao, Qiwei Zhang , Chengsong Wan

Fuente: http://plos.srce.hr/



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