Involvement of the Heat Shock Protein HtpG of Salmonella Typhimurium in Infection and Proliferation in Hosts

Abstract

Salmonella Typhimurium is a common pathogen infecting the gastrointestinal tract of humans and animals, causing host gastroenteritis and typhoid fever. Heat shock protein (HtpG) as a molecular chaperone is involved in the various cellular processes of bacteria, especially under environmental stress. However, the potential association of HtpG with S. Typhimurium infection remains unknown. In this study, we clarified that HtpG could also play a role as an effector in S. Typhimurium infection. RNA-seq indicated that the flagellar assembly pathway, infection pathway, and chemotaxis pathway genes of S. Typhimurium were downregulated after the mutation of HtpG, which resulted in compromises of S. Typhimurium motility, biofilm formation, adhesion, invasion, and inflammation-inducing ability. In addition, HtpG recombinant protein was capable of promoting the proliferation of S. Typhimurium in host cells and the resultant inflammation. Collectively, our results illustrated an important role of HtpG in S. Typhimurium infection.

The role and mechanisms of the two‐component system EnvZ/OmpR on the intracellular survival of Aeromonas hydrophila

“…The proteins, such as HtpG, GroEL, DnaK, GrpE and ClpB, have been regarded as molecular chaperones that involved in various cellular processes of bacteria, especially under environmental stress, and these molecular chaperones were also reported to be associated with invasion, intracellular survival and multiplication of bacteria (Dong et al, 2021; Liu et al, 2018; Tripathi et al, 2020; Verbrugghe et al, 2015; Winardhi et al, 2018). For example, the study on Salmonella Typhimurium revealed that HtpG contributed to bacterial invasion and survival in porcine enterocytes and macrophages (Verbrugghe et al, 2015), and the study on bacteria such as Mycobacterium tuberculosis , Staphylococcus aureus and Porphyromonas gingivalis also confirmed that ClpB was associated with intracellular survival and multiplication of the bacteria (Tripathi et al, 2020).…”

Propionate and Butyrate Inhibit Biofilm Formation of Salmonella Typhimurium Grown in Laboratory Media and Food Models

“…The swimming ability was significantly decreased when exposed to SICs ferulic acid and p-coumaric acid, and it was proved that related gene expression of S. Enteritidis was repressed [ 35 ]. Moreover, motility is an important role in Salmonella adhering to biotic or unbiotic surfaces [ 44 ]. On the other side, we observed the adhesion and invasion gene of Salmonella decreased, which is consistent with the result of motility.…”

Uncoupling the Hsp90 and DnaK chaperone activities revealed the in vivo relevance of their collaboration in bacteria

“…Nowadays, we know that bacterial Hsp90 is essential in some environmental bacteria and that it plays crucial roles in other bacteria where it is involved in unanticipated pathways, including, for example, the CRISPR system or the biosynthesis of complex molecules such as toxins and siderophores ( 15 , 19 , 20 , 22 ). Its role in the virulence of several pathogenic bacteria has also been documented ( 21 – 25 ). In parallel, many biochemical studies have been performed to characterize the in vitro chaperone activity of E. coli Hsp90 (Hsp90 Ec ) ( 38 , 39 , 41 , 57 ).…”

“…In bacteria, although few clients are known, Hsp90 (also called HtpG) has been shown to be essential under stress in some genera, including the aquatic model bacterium Shewanella oneidensis and the cyanobacterium Synechococcus elongatus ( 11 , 14 – 20 ). In addition, Hsp90 participates by still unknown mechanisms in the virulence of pathogenic bacteria like extraintestinal pathogenic Escherichia coli , Salmonella Typhimurium, or Pseudomonas aeruginosa ( 21 – 25 ).…”