Clever Cooperation: Interactions Between EspF and Host Proteins.

Ying Hua,Chengsong Wan,Kaina Yan

doi:10.3389/fmicb.2018.02831

Abstract

EspF is a central effector protein of enterohemorrhagic Escherichia coli (EHEC), enteropathogenic E. coli (EPEC), and Citrobacter rodentium (CR) that is secreted through the type III secretion system to host cells. The interaction between EspF and host proteins plays an important role in bacterial pathogenesis. EspF protein binds to host SNX9 and N-WASP proteins to promote the colonization of pathogenic bacteria in intestinal epithelial cells; combines with cytokeratin 18, actin, 14-3-3ζ, Arp2/3, profilin, and ZO-1 proteins to intervene in the redistribution of intermediate filaments, the rearrangement of actin, and the disruption of tight junctions; acts together with Abcf2 to boost host cell intrinsic apoptosis; and collaborates with Anxa6 protein to inhibit phagocytosis. The interaction between EspF and host proteins is key to the pathogenic mechanism of EHEC and EPEC. Here, we review how EspF protein functions through interactions with these 10 host proteins and contributes to the pathogenicity of EHEC/EPEC.

Highlights

Over the last decade, the advancing field of cellular microbiology has provided a glimpse of the complex interactions between many bacteria and eukaryotic cells (Hartland and Richardson, 2016)
Dean and Kenny have found that Enteropathogenic Escherichia coli (EPEC) EspF can induce multinucleation and cell-cell internalization of intestinal epithelial cells accompanied by cell fusion events, which depend on its C-terminal proline repeat sequence (Dean and Kenny, 2013)
Many pathogens are equipped with highly evolved infectious strategies, for example secreting “smart” effectors like EspF, which can inject into the host cell, and interact with some host proteins and take advantage of their function to mediate virulence, promote bacterial survival, and destroy host cells

Summary

INTRODUCTION

The advancing field of cellular microbiology has provided a glimpse of the complex interactions between many bacteria and eukaryotic cells (Hartland and Richardson, 2016). Dean and Kenny have found that EPEC EspF can induce multinucleation and cell-cell internalization of intestinal epithelial cells accompanied by cell fusion events, which depend on its C-terminal proline repeat sequence (Dean and Kenny, 2013) This result reveals a new function of the C-terminal domain of the EspF protein. Through its mitochondrial targeting domain, and accelerates the targeting through the mitochondrial membrane protein Tom, which it may interact with (Muto et al, 2001; Nagai et al., 2005) This results in the destruction of mitochondrial membrane potential (MMP), the release of cytochrome c into the cytoplasm, the cleavage of caspases 9 and 3, and the initiation of the TABLE 1 | EspF host binding partners and their biological functions

Is found in two main states

Cadherin binding involved in cell-cell adhesion

Findings

CONCLUSIONS