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Screening for host proteins interacting with Escherichia coli O157:H7 EspF using bimolecular fluorescence
Ying Hua1,2, Jingwei Ju3,4, Xiangyu Wang1,2
1Biosafety Level 3 Laboratory, School of Public Health, Southern Medical University, Guangzhou 510515, China.
Future Microbiology
|December 12, 2017
Summary
Enterohemorrhagic Escherichia coli O157:H7 EspF protein interacts with host proteins, including ANXA6. This interaction may influence phagocytosis and highlights EspF's role in E. coli infections.
Area of Science:
- Microbiology
- Molecular Biology
- Host-Pathogen Interactions
Background:
- Enterohemorrhagic Escherichia coli (EHEC) O157:H7 is a significant human pathogen.
- The EHEC secreted protein F (EspF) is crucial for virulence.
- Understanding host-pathogen protein interactions is key to deciphering E. coli pathogenesis.
Purpose of the Study:
- To identify host proteins that interact with the EHEC O157:H7 EspF protein.
- To elucidate the functional roles of these interacting proteins in the context of E. coli infection.
Main Methods:
- Host protein interaction screening using flow cytometry and high-throughput sequencing.
- Bioinformatic analysis of protein functions and pathways using DAVID online tool.
- Validation of specific protein interactions via glutathione S-transferase pull-down and dot blotting assays.
Main Results:
- Identification of 293 host proteins associating with EspF.
- Enrichment analysis revealed significant associations with RNA splicing and ribosome structure.
- Confirmation of interactions between EspF and SNX9, and notably ANXA6.
Conclusions:
- EspF directly interacts with the host protein ANXA6.
- The EspF-ANXA6 complex likely plays a role in manipulating host cell phagocytosis.
- EspF contributes significantly to the pathogenic mechanisms of enterohemorrhagic E. coli infections.
