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Bacterial FIC Proteins AMP Up Infection
Craig R Roy1, Shaeri Mukherjee
1Yale University, New Haven, CT 06536, USA. craig.roy@yale.edu
Science Signaling
|March 19, 2009
Summary
Bacterial FIC domain proteins use AMPylation to modify host proteins, disrupting cellular functions. This posttranslational modification is exploited by pathogens to manipulate host cells during infection.
Area of Science:
- Molecular biology
- Microbiology
- Cell biology
Background:
- FIC domain proteins are conserved in prokaryotes and eukaryotes, but their functions are largely unknown.
- Bacterial FIC proteins are secreted into host cells, where they interfere with eukaryotic cellular processes.
- Examples include Vibrio parahaemolyticus VopS and Legionella pneumophila AnkX.
Purpose of the Study:
- To elucidate the function of FIC domain proteins.
- To understand the mechanism by which bacterial FIC proteins disrupt host cell processes.
- To investigate the role of FIC domain-mediated AMPylation in posttranslational regulation.
Main Methods:
- Biochemical analysis of the VopS protein.
- Characterization of protein-protein interactions.
- In vitro assays to study enzyme activity.
Main Results:
- FIC domains catalyze the transfer of adenosine 5'-monophosphate (AMP) to target proteins.
- VopS protein was shown to covalently modify Rac, a Rho GTPase, at a threonine residue.
- This modification, termed AMPylation, alters the function of the target protein.
Conclusions:
- FIC domain-mediated AMPylation is a novel mechanism for posttranslational regulation of protein function.
- Bacterial pathogens have evolved to utilize FIC domain AMPylation to manipulate host cell functions during infection.
- This finding opens new avenues for understanding host-pathogen interactions and developing therapeutic strategies.
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