HtpG contributes to Salmonella Typhimurium intestinal persistence in pigs

Verbrugghe, Elin; Parys, Alexander Van; Leyman, Bregje; Boyen, Filip; Haesebrouck, Freddy; Pasmans, Frank

doi:10.1186/s13567-015-0261-5

Cited by 27 publications

(26 citation statements)

References 17 publications

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“…As observed for certain pathogenic E. coli strains, Hsp90 participates in the virulence of other pathogenic bacteria, including Salmonella typhimurium (125), Edwardsiella tarda (126), Pseudomonas aeruginosa (127), and the phytopathogenic bacteria Xanthomonas albilineans (128). However, the molecular mechanism for Hsp90 in these processes is still unknown.…”

Section: Additional Bacteriamentioning

confidence: 99%

Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling

Genest¹,

Wickner²,

Doyle³

2019

Journal of Biological Chemistry

262

194

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Heat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conserved ATP-dependent molecular chaperones that fold and remodel proteins. Both are important components of the cellular machinery involved in protein homeostasis and participate in nearly every cellular process. Although Hsp90 and Hsp70 each carry out some chaperone activities independently, they collaborate in other cellular remodeling reactions. In eukaryotes, both Hsp90 and Hsp70 function with numerous Hsp90 and Hsp70 co-chaperones. In contrast, bacterial Hsp90 and Hsp70 are less complex; Hsp90 acts independently of cochaperones, and Hsp70 uses two co-chaperones. In this review, we focus on recent progress toward understanding the basic mechanisms of Hsp90-mediated protein remodeling and the collaboration between Hsp90 and Hsp70, with an emphasis on bacterial chaperones. We describe the structure and conformational dynamics of these chaperones and their interactions with each other and with client proteins. The physiological roles of Hsp90 in Escherichia coli and other bacteria are also discussed. We anticipate that the information gained from exploring the mechanism of the bacterial chaperone system will provide the groundwork for understanding the more complex eukaryotic Hsp90 system and its modulation by Hsp90 co-chaperones.

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Section: Additional Bacteriamentioning

confidence: 99%

Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling

Genest¹,

Wickner²,

Doyle³

2019

Journal of Biological Chemistry

262

194

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“…S. typhimurium infection in pigs must not be underestimated, since it can cause enterocolitis, but it can also persist asymptomatically, making the pig an important reservoir of the pathogen, reducing productivity and average daily gain [4,5]. In the latter case, S. typhimurium colonizes the gastrointestinal tract of the pig in a persistent and chronic way and, during periods of stress, this asymptomatic colonization often flares up [6]. The most dangerous situations are during transport and at the slaughterhouse, where the spread of this pathogen is amplified and the contamination of food through fecal matter becomes the main route of transmission to humans [7,8].…”

Section: Introductionmentioning

confidence: 99%

Thymol and Carvacrol Downregulate the Expression of Salmonella typhimurium Virulence Genes during an In Vitro Infection on Caco-2 Cells

Giovagnoni

Rossi²,

Tugnoli³

et al. 2020

Microorganisms

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Salmonella typhimurium is one of the major bacteria responsible for gastroenteritis in humans caused by foodborne pathogens. As pork is one of the main routes of transmission, bioactive compounds used as feed additives may be an important strategy to control Salmonella typhimurium. The aim of this study was to assess the antimicrobial activity of several organic acids and nature identical compounds against Salmonella typhimurium ATCC®® 6994™. Moreover, the effect of sub-lethal concentrations of thymol and carvacrol in counteracting a Salmonella typhimurium in vitro infection on Caco-2 cells was evaluated, focusing on the maintenance of the epithelial barrier and the alteration of Salmonella virulence genes. The results showed a protective effect of the compounds on the integrity of the intestinal monolayer, improving transepithelial electrical resistance and bacterial translocation compared to the non-treated cells. A real-time PCR study highlighted a significant downregulation of the main virulence genes of Salmonella (hilA, prgH, invA, sipA, sipC, sipD, sopB, sopE2). These findings indicate that thymol and carvacrol could be good candidates for the control of Salmonella typhimurium in pigs.

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“…In E. coli, the absence of Hsp90 (HtpG) leads to slight effects at very high temperature (Bardwell and Craig, 1988;Grudniak et al, 2013;Press et al, 2013;Thomas and Baneyx, 2000). In addition, Hsp90 participates in bacterial immunity via the CRISPR system (Yosef et al, 2011), in the virulence of some bacteria like extraintestinal pathogenic E. coli strains, Edwardsiella tarda, or Salmonella typhimurium and plays a role in the biosynthesis of antibiotic and toxins (Dang et al, 2011;Garcie et al, 2016;Verbrugghe et al, 2015;Vivien et al, 2005). However, the precise function of Hsp90 in virulence, i.e., the client proteins involved, is unknown.…”

Section: Introductionmentioning

confidence: 99%

Hsp90 Is Essential under Heat Stress in the Bacterium Shewanella oneidensis

Honoré¹,

Méjean²,

Genest³

2017

Cell Reports

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The Hsp90 chaperone is essential in eukaryotes and activates a large array of client proteins. In contrast, its role is still elusive in bacteria, and only a few Hsp90 bacterial clients are known. Here, we found that Hsp90 is essential in the model bacterium Shewanella oneidensis under heat stress. A genetic screen for Hsp90 client proteins identified TilS, an essential protein involved in tRNA maturation. Overexpression of TilS rescued the growth defect of the hsp90 deletion strain under heat stress. In vivo, the activity and the amount of TilS were significantly reduced in the absence of Hsp90 at high temperature. Furthermore, we showed that Hsp90 interacts with TilS, and Hsp90 prevents TilS aggregation in vitro at high temperature. Together, our results indicate that TilS is a client of Hsp90 in S. oneidensis. Therefore, our study links the essentiality of bacterial Hsp90 at high temperature with the identification of a client.

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HtpG contributes to Salmonella Typhimurium intestinal persistence in pigs

Cited by 27 publications

References 17 publications

Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling

Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling

Thymol and Carvacrol Downregulate the Expression of Salmonella typhimurium Virulence Genes during an In Vitro Infection on Caco-2 Cells

Hsp90 Is Essential under Heat Stress in the Bacterium Shewanella oneidensis

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