Protein Acetylation Is Involved inSalmonella entericaSerovar Typhimurium Virulence

Abstract

Salmonella causes a range of diseases in different hosts, including enterocolitis and systemic infection. Lysine acetylation regulates many eukaryotic cellular processes, but its function in bacteria is largely unexplored. The acetyltransferase Pat and NAD(+)-dependent deacetylase CobB are involved in the reversible protein acetylation in Salmonella Typhimurium. Here, we used cell and animal models to evaluate the virulence of pat and cobB deletion mutants in S. Typhimurium and found that pat is critical for bacterial intestinal colonization and systemic infection. Next, to understand the underlying mechanism, genome-wide transcriptome was analyzed. RNA sequencing data showed that the expression of Salmonella pathogenicity island 1 (SPI-1) is partially dependent on pat In addition, we found that HilD, a key transcriptional regulator of SPI-1, is a substrate of Pat. The acetylation of HilD by Pat maintained HilD stability and was essential for the transcriptional activation of HilA. Taken together, these results suggest that a protein acetylation system regulates SPI-1 expression by controlling HilD in a posttranslational manner to mediate S. Typhimurium virulence.

Type VI secretion system contributes to Enterohemorrhagic Escherichia coli virulence by secreting catalase against host reactive oxygen species (ROS)

“…Samples were run in triplicates and amplified using SYBR Premix Ex Taq II (TAKARA) in the 7500 fast Real-Time PCR System. The relative transcriptional level was determined by the methods of 2 −ΔΔCt [73]. 16S rRNA was used as a reference gene.…”

“…The RAW264.7 cells were maintained in DMEM supplemented with 10% fetal bovine serum (FBS) for survival experiment [73,74]. The RAW264.7 cells were seeded at 2×10 5 cells per well in a 24-well tissue culture plate and cultured at 37°C under 5% of CO 2 overnight.…”

Regulation, Function, and Detection of Protein Acetylation in Bacteria

“…A number of virulence factors are acetylated, but the significance of these findings needs to be explored. So far, acetylation likely affects the virulence of Erwinia amylovora, Pseudomonas aeruginosa, Salmonella spp., and M. tuberculosis (32,38,44,46,102,103). With an alarming rise in antibiotic drug resistance, there is an imperative need for new drug targets.…”

Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

“…Lysine acetylation is an abundant post-translational modification in bacteria, and it is involved in a broad range of cellular events such as central metabolism (Wang et al, 2010), transcription (Qin et al, 2016), virulence (Starai and Escalante-Semerena, 2004; Sang et al, 2016), and stress responses (Ma and Wood, 2011). Acetylation is catalyzed by the Gcn5-like acetyltransferase YfiQ (Starai and Escalante-Semerena, 2004) and chemically by AcP (Weinert et al, 2013; Kuhn et al, 2014) in E. coli .…”