Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) Interacts with <i>Escherichia coli</i> Effector Protein EspF
<i>Enteropathogenic</i> (EPEC) and <i>Enterohemorrhagic</i> (EHEC) <i>Escherichia coli</i> are considered emerging zoonotic pathogens of worldwide distribution. The pathogenicity of the bacteria is conferred by multiple virulence determinants, including the locus...
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MDPI AG
2021-09-01
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| author | Amin Tahoun Hanem El-Sharkawy Samar M. Moustafa Lina Jamil M. Abdel-Hafez Ashraf Albrakati Manfred Koegl Juergen Haas Arvind Mahajan David L. Gally Ehab Kotb Elmahallawy |
| author_facet | Amin Tahoun Hanem El-Sharkawy Samar M. Moustafa Lina Jamil M. Abdel-Hafez Ashraf Albrakati Manfred Koegl Juergen Haas Arvind Mahajan David L. Gally Ehab Kotb Elmahallawy |
| author_sort | Amin Tahoun |
| collection | DOAJ |
| description | <i>Enteropathogenic</i> (EPEC) and <i>Enterohemorrhagic</i> (EHEC) <i>Escherichia coli</i> are considered emerging zoonotic pathogens of worldwide distribution. The pathogenicity of the bacteria is conferred by multiple virulence determinants, including the locus of enterocyte effacement (LEE) pathogenicity island, which encodes a type III secretion system (T3SS) and effector proteins, including the multifunctional secreted effector protein (EspF). EspF sequences differ between EPEC and EHEC serotypes in terms of the number and residues of SH3-binding polyproline-rich repeats and N-terminal localization sequence. The aim of this study was to discover additional cellular interactions of EspF that may play important roles in <i>E. coli</i> colonization using the Yeast two-hybrid screening system (Y2H). Y2H screening identified the anaphase-promoting complex inhibitor Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) as a host protein that interacts with EspF. Using LUMIER assays, MAD2L2 was shown to interact with EspF variants from EHEC O157:H7 and O26:H11 as well as EPEC O127:H6. MAD2L2 is targeted by the non-homologous <i>Shigella</i> effector protein invasion plasmid antigen B (IpaB) to halt the cell cycle and limit epithelial cell turnover. Therefore, we postulate that interactions between EspF and MAD2L2 serve a similar function in promoting EPEC and EHEC colonization, since cellular turnover is a key method for bacteria removal from the epithelium. Future work should investigate the biological importance of this interaction that could promote the colonization of EPEC and EHEC <i>E. coli</i> in the host. |
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| institution | Directory Open Access Journal |
| issn | 2075-1729 |
| language | English |
| last_indexed | 2024-03-10T07:30:09Z |
| publishDate | 2021-09-01 |
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| spelling | doaj.art-9ad67e5681744122acbfc8e7b3d85e182023-11-22T13:56:40ZengMDPI AGLife2075-17292021-09-0111997110.3390/life11090971Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) Interacts with <i>Escherichia coli</i> Effector Protein EspFAmin Tahoun0Hanem El-Sharkawy1Samar M. Moustafa2Lina Jamil M. Abdel-Hafez3Ashraf Albrakati4Manfred Koegl5Juergen Haas6Arvind Mahajan7David L. Gally8Ehab Kotb Elmahallawy9Division of Immunity and Infection, The Roslin Institute and R(D)SVS, The University of Edinburgh, Easter Bush, Midlothian EH25 9RG, UKDepartment of Poultry and Rabbit Diseases, Faculty of Veterinary Medicine, Kafrelsheikh University, Kafrelsheikh 33511, EgyptDepartment of Zoonoses, Faculty of Veterinary Medicine, Benha University, Benha 13511, EgyptDepartment of Microbiology and Immunology, Faculty of Pharmacy, October 6 University, October 6 City 12566, Giza, EgyptDepartment of Human Anatomy, College of Medicine, Taif University, P.O. Box 11099, Taif 21944, Saudi ArabiaPreclinical Target Development and Genomics and Proteomics Core Facilities, German Cancer Research Center, 69120 Heidelberg, GermanyDivision of Pathway Medicine and Centre for Infectious Diseases, University of Edinburgh, Edinburgh EH16 4SB, UKDivision of Immunity and Infection, The Roslin Institute and R(D)SVS, The University of Edinburgh, Easter Bush, Midlothian EH25 9RG, UKDivision of Immunity and Infection, The Roslin Institute and R(D)SVS, The University of Edinburgh, Easter Bush, Midlothian EH25 9RG, UKDepartment of Zoonoses, Faculty of Veterinary Medicine, Sohag University, Sohag 82524, Egypt<i>Enteropathogenic</i> (EPEC) and <i>Enterohemorrhagic</i> (EHEC) <i>Escherichia coli</i> are considered emerging zoonotic pathogens of worldwide distribution. The pathogenicity of the bacteria is conferred by multiple virulence determinants, including the locus of enterocyte effacement (LEE) pathogenicity island, which encodes a type III secretion system (T3SS) and effector proteins, including the multifunctional secreted effector protein (EspF). EspF sequences differ between EPEC and EHEC serotypes in terms of the number and residues of SH3-binding polyproline-rich repeats and N-terminal localization sequence. The aim of this study was to discover additional cellular interactions of EspF that may play important roles in <i>E. coli</i> colonization using the Yeast two-hybrid screening system (Y2H). Y2H screening identified the anaphase-promoting complex inhibitor Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) as a host protein that interacts with EspF. Using LUMIER assays, MAD2L2 was shown to interact with EspF variants from EHEC O157:H7 and O26:H11 as well as EPEC O127:H6. MAD2L2 is targeted by the non-homologous <i>Shigella</i> effector protein invasion plasmid antigen B (IpaB) to halt the cell cycle and limit epithelial cell turnover. Therefore, we postulate that interactions between EspF and MAD2L2 serve a similar function in promoting EPEC and EHEC colonization, since cellular turnover is a key method for bacteria removal from the epithelium. Future work should investigate the biological importance of this interaction that could promote the colonization of EPEC and EHEC <i>E. coli</i> in the host.https://www.mdpi.com/2075-1729/11/9/971MAD2L2interactioneffector proteinsEspF<i>Escherichia coli</i>pathogenesis |
| spellingShingle | Amin Tahoun Hanem El-Sharkawy Samar M. Moustafa Lina Jamil M. Abdel-Hafez Ashraf Albrakati Manfred Koegl Juergen Haas Arvind Mahajan David L. Gally Ehab Kotb Elmahallawy Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) Interacts with <i>Escherichia coli</i> Effector Protein EspF Life MAD2L2 interaction effector proteins EspF <i>Escherichia coli</i> pathogenesis |
| title | Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) Interacts with <i>Escherichia coli</i> Effector Protein EspF |
| title_full | Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) Interacts with <i>Escherichia coli</i> Effector Protein EspF |
| title_fullStr | Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) Interacts with <i>Escherichia coli</i> Effector Protein EspF |
| title_full_unstemmed | Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) Interacts with <i>Escherichia coli</i> Effector Protein EspF |
| title_short | Mitotic Arrest-Deficient 2 Like 2 (MAD2L2) Interacts with <i>Escherichia coli</i> Effector Protein EspF |
| title_sort | mitotic arrest deficient 2 like 2 mad2l2 interacts with i escherichia coli i effector protein espf |
| topic | MAD2L2 interaction effector proteins EspF <i>Escherichia coli</i> pathogenesis |
| url | https://www.mdpi.com/2075-1729/11/9/971 |
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