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Related Experiment Video

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Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

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The pathogen protein EspF(U) hijacks actin polymerization using mimicry and multivalency.

Nathan A Sallee¹, Gonzalo M Rivera, John E Dueber

¹Graduate Program in Chemistry and Chemical Biology, University of California, San Francisco, 600 16th Street, San Francisco, California 94158, USA.

|July 25, 2008

Summary

Enterohaemorrhagic Escherichia coli uses EspF(U) protein to trigger actin pedestal formation in host cells. This protein uniquely mimics an internal N-WASP element, not CDC42, to activate actin polymerization for bacterial attachment.

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Area of Science:

Microbiology
Cell Biology
Biochemistry

Background:

Enterohaemorrhagic Escherichia coli (EHEC) utilizes actin pedestals for intestinal attachment.
Bacterial protein EspF(U) (TccP) injection into host cells induces actin pedestal formation.
EspF(U) activates Wiskott-Aldrich syndrome protein (WASP) family actin nucleators, typically regulated by CDC42.

Purpose of the Study:

To elucidate the mechanism by which EspF(U) activates N-WASP.
To identify the specific EspF(U) motif responsible for N-WASP interaction.
To understand how EspF(U) exploits host cell machinery for bacterial adhesion.

Main Methods:

Structural analysis of EspF(U) repeats.
Identification of the N-WASP binding motif within EspF(U).
Biochemical assays to measure actin polymerization and N-WASP activation.

Main Results:

A 17-amino acid motif within EspF(U) repeats is sufficient for N-WASP binding.
EspF(U) mimics an autoinhibitory element of N-WASP, not the natural activator CDC42.
Multiple EspF(U) repeats enhance actin polymerization potency by coordinating N-WASP activation.

Conclusions:

EHEC EspF(U) activates N-WASP by disrupting its autoinhibited state, offering a novel mechanism of pathogen-host interaction.
The pathogen has engineered a potent actin polymerization machine using simple, repeated autoinhibitory fragments.
This mechanism allows for selective activation of specific cellular processes, facilitating bacterial colonization.