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AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence

Authors :
Deyan Luo
Zhan Li
Fanghong Chen
Nianzhi Ning
Jianxin Wang
Zhili He
Tao Li
Hui Wang
Source :
Frontiers in Microbiology, Vol 12 (2021), Frontiers in Microbiology
Publication Year :
2021
Publisher :
Frontiers Media SA, 2021.

Abstract

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.

Details

Language :
English
ISSN :
1664302X
Volume :
12
Database :
OpenAIRE
Journal :
Frontiers in Microbiology
Accession number :
edsair.doi.dedup.....5a15c470b6deab897a6f88d94c17daf0
Full Text :
https://doi.org/10.3389/fmicb.2021.627141