Screening for host proteins interacting with Escherichia coli O157:H7 EspF using bimolecular fluorescence complementation
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Updated: Feb 17, 2026
Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
Published on: January 6, 2015
Ying Hua1,2, Jingwei Ju3,4, Xiangyu Wang1,2
1Biosafety Level 3 Laboratory, School of Public Health, Southern Medical University, Guangzhou 510515, China.
Aim:
To screen host proteins that interact with enterohemorrhagic Escherichia coli O157:H7 EspF.
Materials & Methods:
Flow cytometry and high-throughput sequencing were used to screen interacting proteins. Molecular function, biological processes and Kyoto Encyclopedia of Genes and Genomes pathways were studied using the DAVID online tool. Glutathione S-transferase pull down and dot blotting were used to verify the interactions.
Results:
293 host proteins were identified to associate with EspF. They were mainly enriched in RNA splicing (p = 0.005), ribosome structure (p = 0.012), and involved in 109 types of signaling pathways. SNX9 and ANXA6 were confirmed to interact with EspF.
Conclusion:
EspF interacts with ANXA6; they may form a complex to manipulate the process of phagocytosis; EspF plays a highlighted pathogenic role in enterohemorrhagic E. coli infection process.
