AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence
A novel type II toxin of toxin–antitoxin systems (TAs), Gcn5-related N-acetyltransferase (GNAT) family, was reported recently. GNAT toxins are mainly present in pathogenic species, but studies of their involvement in pathogenicity are rare. This study discovered that the GANT toxin AtaT in enterohem...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2021-03-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2021.627141/full |
| _version_ | 1819295021731414016 |
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| author | Zhili He Tao Li Jianxin Wang Deyan Luo Nianzhi Ning Zhan Li Fanghong Chen Hui Wang |
| author_facet | Zhili He Tao Li Jianxin Wang Deyan Luo Nianzhi Ning Zhan Li Fanghong Chen Hui Wang |
| author_sort | Zhili He |
| collection | DOAJ |
| description | A novel type II toxin of toxin–antitoxin systems (TAs), Gcn5-related N-acetyltransferase (GNAT) family, was reported recently. GNAT toxins are mainly present in pathogenic species, but studies of their involvement in pathogenicity are rare. This study discovered that the GANT toxin AtaT in enterohemorrhagic Escherichia coli (EHEC) can significantly enhance strain pathogenicity. First, we detected the virulence of ΔataT and ΔataR in cell and animal models. In the absence of ataT, strains showed a lower adhesion number, and host cells presented weaker attaching and effacing lesions, inflammatory response, and pathological injury. Next, we screened the acetylation substrate of AtaT to understand the underlying mechanism. Results showed that E. coli pore-forming protein EspB, which acts as a translocon in type III secretion system (T3SS) in strains, can be acetylated specifically by AtaT. The acetylation of K206 in EspB increases protein stability and maintains the efficiency of effectors translocating into host cells to cause close adhesion and tissue damage. |
| first_indexed | 2024-12-24T04:35:36Z |
| format | Article |
| id | doaj.art-369e5cc33cc04656b514d70794cd1068 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-24T04:35:36Z |
| publishDate | 2021-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-369e5cc33cc04656b514d70794cd10682022-12-21T17:15:12ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2021-03-011210.3389/fmicb.2021.627141627141AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain VirulenceZhili HeTao LiJianxin WangDeyan LuoNianzhi NingZhan LiFanghong ChenHui WangA novel type II toxin of toxin–antitoxin systems (TAs), Gcn5-related N-acetyltransferase (GNAT) family, was reported recently. GNAT toxins are mainly present in pathogenic species, but studies of their involvement in pathogenicity are rare. This study discovered that the GANT toxin AtaT in enterohemorrhagic Escherichia coli (EHEC) can significantly enhance strain pathogenicity. First, we detected the virulence of ΔataT and ΔataR in cell and animal models. In the absence of ataT, strains showed a lower adhesion number, and host cells presented weaker attaching and effacing lesions, inflammatory response, and pathological injury. Next, we screened the acetylation substrate of AtaT to understand the underlying mechanism. Results showed that E. coli pore-forming protein EspB, which acts as a translocon in type III secretion system (T3SS) in strains, can be acetylated specifically by AtaT. The acetylation of K206 in EspB increases protein stability and maintains the efficiency of effectors translocating into host cells to cause close adhesion and tissue damage.https://www.frontiersin.org/articles/10.3389/fmicb.2021.627141/fullGcn5-related N-acetyltransferaseAtaTenterohemorrhagic Escherichia coliEspBvirulence |
| spellingShingle | Zhili He Tao Li Jianxin Wang Deyan Luo Nianzhi Ning Zhan Li Fanghong Chen Hui Wang AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence Frontiers in Microbiology Gcn5-related N-acetyltransferase AtaT enterohemorrhagic Escherichia coli EspB virulence |
| title | AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence |
| title_full | AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence |
| title_fullStr | AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence |
| title_full_unstemmed | AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence |
| title_short | AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence |
| title_sort | atat improves the stability of pore forming protein espb by acetylating lysine 206 to enhance strain virulence |
| topic | Gcn5-related N-acetyltransferase AtaT enterohemorrhagic Escherichia coli EspB virulence |
| url | https://www.frontiersin.org/articles/10.3389/fmicb.2021.627141/full |
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