Related Experiment Video
Updated: May 5, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
The enteropathogenic E. coli effector EspF targets and disrupts the nucleolus by a process regulated by mitochondrial
Paul Dean1, Jon A Scott, Andrew A Knox
1Institute for Cell and Molecular Biosciences, Medical School, University of Newcastle, Newcastle upon Tyne, United Kingdom. p.dean@ncl.ac.uk
Abstract:
The nucleolus is a multifunctional structure within the nucleus of eukaryotic cells and is the primary site of ribosome biogenesis. Almost all viruses target and disrupt the nucleolus--a feature exclusive to this pathogen group. Here, using a combination of bio-imaging, genetic and biochemical analyses, we demonstrate that the enteropathogenic E. coli (EPEC) effector protein EspF specifically targets the nucleolus and disrupts a subset of nucleolar factors. Driven by a defined N-terminal nucleolar targeting domain, EspF causes the complete loss from the nucleolus of nucleolin, the most abundant nucleolar protein. We also show that other bacterial species disrupt the nucleolus, dependent on their ability to deliver effector proteins into the host cell. Moreover, we uncover a novel regulatory mechanism whereby nucleolar targeting by EspF is strictly controlled by EPEC's manipulation of host mitochondria. Collectively, this work reveals that the nucleolus may be a common feature of bacterial pathogenesis and demonstrates that a bacterial pathogen has evolved a highly sophisticated mechanism to enable spatio-temporal control over its virulence proteins.
Insights
Enteropathogenic E. coli (EPEC) uses the effector protein EspF to target the nucleolus, disrupting key factors like nucleolin. This reveals a sophisticated bacterial strategy for controlling virulence during infection.
Area of Science:
- Cell Biology
- Microbiology
- Virology
Background:
- The nucleolus is a vital nuclear structure responsible for ribosome biogenesis in eukaryotic cells.
- Nucleolar disruption is a characteristic feature observed in infections by most viruses.
- The role of nucleolar disruption in bacterial pathogenesis is less understood.
Purpose of the Study:
- To investigate the specific mechanisms by which the enteropathogenic E. coli (EPEC) effector protein EspF targets and disrupts the nucleolus.
- To elucidate the role of nucleolar disruption in bacterial pathogenesis.
- To uncover novel regulatory mechanisms controlling bacterial effector protein targeting.
Main Methods:
- Bio-imaging techniques to visualize protein localization and cellular structures.
- Genetic analyses to study the function of specific bacterial proteins and pathways.
- Biochemical assays to analyze protein interactions and cellular processes.
Main Results:
- The EPEC effector protein EspF specifically targets the nucleolus, driven by its N-terminal domain.
- EspF causes the loss of nucleolin, the most abundant nucleolar protein, from the nucleolus.
- Bacterial species can disrupt the nucleolus, contingent on their ability to deliver effector proteins.
- EspF's nucleolar targeting is regulated by EPEC's manipulation of host mitochondria.
Conclusions:
- The nucleolus is a potential common target in bacterial pathogenesis.
- Bacterial pathogens have evolved sophisticated mechanisms for spatio-temporal control of virulence proteins.
- EspF-mediated nucleolar disruption represents a novel virulence strategy for EPEC.
Related Concept Videos
Nuclear Export
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
Regulation of Nuclear Protein Sorting
The Unfolded Protein Response
Regulation of the Unfolded Protein Response
Stringent Response in E. coli
Bacterial Gastroenteritis

