EspF

Sequence

Protein Sequence

MLNGISNAASTLGRQLVGIASRVSSAGGTGFSVAPQAVRLTPVRVHSPFSPGSSNVNARTIFNVSSQVTS
FTPSRPAPPPPTSGQASGASRPLPPIAQALKDHLAAYELSKASETVNFKPTRPAPPPPTSGQASGASRPL
PPIAQALKDHLAAYELSKASETVSFKPTRQAPPPPTSGQASGPGGLPPLAQALKDHLAAYEQSKKG

Gene Sequence

ATGCTTAATGGAATTAGTAACGCTGCTTCTACACTAGGGCGGCAGCTTGTAGGTATCGCAAGTCGAGTGA
GCTCTGCGGGGGGAACTGGATTTTCTGTAGCCCCTCAGGCTGTTCGTCTTACTCCGGTGAGAGTTCATTC
CCCCTTTTCTCCAGGTTCGTCGAATGTTAATGCGAGGACGATTTTTAATGTGAGCAGCCAGGTGACTTCA
TTTACTCCCTCTCGTCCGGCACCGCCGCCACCGACAAGTGGACAGGCATCCGGGGCATCCCGACCTTTAC
CGCCCATTGCACAGGCATTAAAAGATCATTTAGCTGCCTATGAACTATCGAAAGCGTCTGAGACTGTAAA
CTTTAAGCCAACCCGTCCGGCACCGCCGCCACCGACAAGTGGACAGGCATCCGGGGCATCCCGACCTTTA
CCGCCCATTGCACAGGCATTAAAAGATCATTTAGCTGCCTATGAACTATCGAAAGCGTCTGAGACTGTAA
GCTTTAAGCCAACCCGTCAGGCACCACCGCCACCGACAAGTGGACAGGCATCCGGGCCTGGTGGACTACC
GCCCCTTGCACAGGCACTAAAAGATCATTTAGCTGCCTATGAGCAATCGAAGAAAGGGTAA 

Domains & Motifs

• Three proline-rich repeats (target host actin regulators)
• Mitochondrial targeting sequence
• Apoptosis-inducing motifs
• Nucleolar targeting motif
• SH3-binding (RxAPxxP)
• N-WASP-binding motif
• Mitochondrial targeting sequence (MTS)

Functional Summary

EspF subverts multiple host processes, including tight junction integrity, mitochondrial function, and actin cytoskeleton rearrangement.

Effector References

• Ansari et al. (2024). The C-terminal proline-rich repeats of Enteropathogenic E. coli effector EspF are sufficient for the depletion of tight junction membrane proteins and interactions with early and recycling endosomes. PMID:38972985
• Tahoun et al. (2021). Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) Interacts with Escherichia coli Effector Protein EspF. PMID:34575120
• Hua et al. (2020). Enterohemorrhagic Escherichia coli Effector Protein EspF Interacts With Host Protein ANXA6 and Triggers Myosin Light Chain Kinase (MLCK)-Dependent Tight Junction Dysregulation. PMID: 33425920.
• Karjalainen et al. (2021). 1H,13C, and15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain. PMID:33475933
• Ugalde-Silva et al. (2019). Coordinated transient interaction of ZO-1 and afadin is required for pedestal maturation induced by EspF from enteropathogenic Escherichia coli. PMID:31568664
• Xia et al. (2019). EspF is crucial for Citrobacter rodentium-induced tight junction disruption and lethality in immunocompromised animals. PMID:31251784
• Kassa et al. (2019). Enteropathogenic Escherichia coli remodels host endosomes to promote endocytic turnover and breakdown of surface polarity. PMID:31242273
• Hua et al. (2018). Clever Cooperation: Interactions Between EspF and Host Proteins. PMID:30524410
• Singh et al. (2018). Enteropathogenic E. coli effectors EspF and Map independently disrupt tight junctions through distinct mechanisms involving transcriptional and post-transcriptional regulation. PMID:29487356
• Tapia et al. (2017). EPEC effector EspF promotes Crumbs3 endocytosis and disrupts epithelial cell polarity. PMID:28618099
• Blasche et al. (2014). The EHEC-host interactome reveals novel targets for the translocated intimin receptor. PMID: 25519916.
• Dean et al. (2013). A bacterial encoded protein induces extreme multinucleation and cell-cell internalization in intestinal cells. PMID:24665371
• Holmes et al. (2010). The EspF effector, a bacterial pathogen's Swiss army knife. PMID:20679436
• Dean et al. (2010). The enteropathogenic E. coli effector EspF targets and disrupts the nucleolus by a process regulated by mitochondrial dysfunction. PMID:20585567
• Weflen et al. (2010). E. coli secreted protein F promotes EPEC invasion of intestinal epithelial cells via an SNX9-dependent mechanism. PMID:20088948
• Peralta-Ramírez et al. (2008). EspF Interacts with nucleation-promoting factors to recruit junctional proteins into pedestals for pedestal maturation and disruption of paracellular permeability. PMID:18559425
• Hodges et al. (2008). The enteropathogenic Escherichia coli effector protein EspF decreases sodium hydrogen exchanger 3 activity. PMID:18433466
• Alto et al. (2007). The type III effector EspF coordinates membrane trafficking by the spatiotemporal activation of two eukaryotic signaling pathways. PMID:17893247
• Nougayrède et al. (2007). Enteropathogenic Escherichia coli effector EspF interacts with host protein Abcf2. PMID:17064289
• Campellone et al. (2006). Enterohaemorrhagic Escherichia coli Tir requires a C-terminal 12-residue peptide to initiate EspF-mediated actin assembly and harbours N-terminal sequences that influence pedestal length. PMID:16922867
• Quitard et al. (2006). The enteropathogenic Escherichia coli EspF effector molecule inhibits PI-3 kinase-mediated uptake independently of mitochondrial targeting. PMID:16681838
• Marchès et al. (2006). EspF of enteropathogenic Escherichia coli binds sorting nexin 9. PMID:16585770
• Dean et al. (2006). Potent diarrheagenic mechanism mediated by the cooperative action of three enteropathogenic Escherichia coli-injected effector proteins. PMID:16446436
• Nagai et al. (2005). Targeting of enteropathogenic Escherichia coli EspF to host mitochondria is essential for bacterial pathogenesis: critical role of the 16th leucine residue in EspF. PMID:15533930
• Dean et al. (2004). Intestinal barrier dysfunction by enteropathogenic Escherichia coli is mediated by two effector molecules and a bacterial surface protein. PMID:15491358
• Nougayrède et al. (2004). Enteropathogenic Escherichia coli EspF is targeted to mitochondria and is required to initiate the mitochondrial death pathway. PMID:15469437
• Viswanathan et al. (2004). Cytokeratin 18 interacts with the enteropathogenic Escherichia coli secreted protein F (EspF) and is redistributed after infection. PMID:15339273
• Elliott et al. (2002). A gene from the locus of enterocyte effacement that is required for enteropathogenic Escherichia coli to increase tight-junction permeability encodes a chaperone for EspF. PMID:11953359
• Crane et al. (2001). Role of EspF in host cell death induced by enteropathogenic Escherichia coli. PMID:11298644
• McNamara et al. (2001). Translocated EspF protein from enteropathogenic Escherichia coli disrupts host intestinal barrier function. PMID:11238563
• McNamara et al. (1998). A novel proline-rich protein, EspF, is secreted from enteropathogenic Escherichia coli via the type III export pathway. PMID:9741085