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- Title
Protein Acetylation Is Involved in Salmonella enterica Serovar Typhimurium Virulence.
- Authors
Yu Sang; Jie Ren; Jinjing Ni; Jing Tao; Jie Lu; Yu-Feng Yao; Sang, Yu; Ren, Jie; Ni, Jinjing; Tao, Jing; Lu, Jie; Yao, Yu-Feng
- 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.
- Subjects
ACETYLATION; THERAPEUTIC use of proteins; PROTEIN synthesis; SALMONELLA enterica serovar typhimurium; MICROBIAL virulence genetics; BACTERIAL protein metabolism; ACETYLTRANSFERASES; ANIMAL experimentation; BIOCHEMISTRY; CELLS; CYTOKINES; ESTERASES; MACROPHAGES; PHENOMENOLOGY; METABOLISM; MICE; GENETIC mutation; SALMONELLA; MICROBIAL virulence; GENE expression profiling
- Publication
Journal of Infectious Diseases, 2016, Vol 213, Issue 11, p1836
- ISSN
0022-1899
- Publication type
journal article
- DOI
10.1093/infdis/jiw028