Effects of Null Mutation of the Heat-Shock Gene
            <i>htpG</i>
            on the Production of Virulence Factors by
            <i>Pseudomonas Aeruginosa</i>

Grudniak, Anna M.; Klecha, Barbara; Wolska, Krystyna I.

doi:10.2217/fmb-2017-0111

Cited by 20 publications

(17 citation statements)

References 47 publications

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“…We examined the biofilm formation of S. Typhimurium on cell culture plates made of polystyrene, which revealed that the biofilm formation ability of S. Typhimurium was significantly reduced by nearly 30% after the deletion of HtpG, indicating that HtpG is involved in the formation of S. Typhimurium biofilm. Grudniak et al found similar results to us, for the HtpG mutant strain of P. plecoglossicida, and the migrating ability and biofilm formation ability were significantly downregulated (Grudniak et al, 2018). We speculate that the reason for this phenomenon may be related to the downregulation of gene expression in the flagellar assembly pathway.…”

Section: Discussionsupporting

confidence: 86%

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

Dong

Wang

Xia

et al. 2021

Front. Cell. Infect. Microbiol.

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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.

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Section: Discussionsupporting

confidence: 86%

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

Dong

Wang

Xia

et al. 2021

Front. Cell. Infect. Microbiol.

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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

245

186

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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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“…htpG encodes the protein HtpG, a member of heat-shock proteins (HSPs) family (18, 19), which was first described in Escherichia coli (20). Null mutation of this gene is not lethal to bacterial cells and only results in impaired growth at high temperatures (21). HtpG acts as a chaperone that enables the optimal folding of newly synthesized proteins under stress conditions.…”

Section: Introductionmentioning

confidence: 99%

“…In E. coli , HtpG interacts with the DnaK/DnaJ/GrpE chaperone complex (23). Null mutation of htpG affects many physiological processes in Pseudomonas aeruginosa , including those that are important for virulence, such as motility, biofilm formation, proteolytic activity, and pigment and biosurfactant production (21). Many virulence factors of P. aeruginosa are extracellular and HtpG could play a role in their secretion (21).…”

Section: Introductionmentioning

confidence: 99%

“…Null mutation of htpG affects many physiological processes in Pseudomonas aeruginosa , including those that are important for virulence, such as motility, biofilm formation, proteolytic activity, and pigment and biosurfactant production (21). Many virulence factors of P. aeruginosa are extracellular and HtpG could play a role in their secretion (21). In addition, HtpG participates in bacterial immunity via the CRISPR system (24), in the virulence of some bacteria like extra-intestinal pathogenic E. coli strains, Edwardsiella tarda , or Salmonella typhimurium , and plays a role in the biosynthesis of antibiotic and toxins (25–27).…”

Section: Introductionmentioning

confidence: 99%

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Dual RNA-Seq Unveils Pseudomonas plecoglossicida htpG Gene Functions During Host-Pathogen Interactions With Epinephelus coioides

et al. 2019

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Pseudomonas plecoglossicida is a temperature-dependent opportunistic pathogen which is associated with a variety of diseases in fish. During the development of “white nodules” disease, the expression of htpG in P. plecoglossicida was found to be significantly up-regulated at its virulent temperature of 18°C. The infection of htpG -RNAi strain resulted in the onset time delay, reduction in mortality and infection symptoms in spleen of Epinephelus coioides , and affected the bacterial tissue colonization. In order to reveal the effect of htpG silencing of P. plecoglossicida on the virulence regulation in P. plecoglossicida and immune response in E. coioides , dual RNA-seq was performed and a pathogen-host integration network was constructed. Our results showed that infection induced the expression of host genes related to immune response, but attenuated the expression of bacterial virulence genes. Novel integration was found between host immune genes and bacterial virulence genes, while IL6, IL1R2, IL1B , and TLR5 played key roles in the network. Further analysis with GeneMANIA indicated that flgD and rplF might play key roles during the htpG -dependent virulence regulation, which was in accordance with the reduced biofilm production, motility and virulence in htpG -RNAi strain. Meanwhile, IL6 and IL1B were found to play key roles during the defense against P. plecoglossicida , while CELA2, TRY, CPA1, CPA2 , and CPB1 were important targets for P. plecoglossicida attacking to the host.

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Effects of Null Mutation of the Heat-Shock Gene htpG on the Production of Virulence Factors by Pseudomonas Aeruginosa

Cited by 20 publications

References 47 publications

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

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

Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling

Dual RNA-Seq Unveils Pseudomonas plecoglossicida htpG Gene Functions During Host-Pathogen Interactions With Epinephelus coioides

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