{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["12"],"submitter":["He Z"],"funding":["Beijing Nova Program","National Key Research and Development Program of China"],"pubmed_abstract":["A novel type II toxin of toxin-antitoxin systems (TAs), Gcn5-related <i>N</i>-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 <i>Escherichia coli</i> (EHEC) can significantly enhance strain pathogenicity. First, we detected the virulence of Δ<i>ataT</i> and Δ<i>ataR</i> in cell and animal models. In the absence of <i>ataT</i>, 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 <i>E. coli</i> po"],"journal":["Frontiers in microbiology"],"pagination":["627141"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7957018"],"repository":["biostudies-literature"],"pubmed_title":["AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence."],"pmcid":["PMC7957018"],"pubmed_authors":["Li Z","He Z","Li T","Ning N","Chen F","Wang H","Wang J","Luo D"],"additional_accession":[]},"is_claimable":false,"name":"AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence.","description":"A novel type II toxin of toxin-antitoxin systems (TAs), Gcn5-related <i>N</i>-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 <i>Escherichia coli</i> (EHEC) can significantly enhance strain pathogenicity. First, we detected the virulence of Δ<i>ataT</i> and Δ<i>ataR</i> in cell and animal models. In the absence of <i>ataT</i>, 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 <i>E. coli</i> po","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021","modification":"2025-04-20T02:25:31.634Z","creation":"2025-04-20T02:25:31.634Z"},"accession":"S-EPMC7957018","cross_references":{"pubmed":["33732222"],"doi":["10.3389/fmicb.2021.627141"]}}