Phage Shock Protein G, a Novel Ethanol-Induced Stress Protein in Salmonella typhimurium

Transcriptional profiles of 2 unrelated clinical methicillin-resistant Staphylococcus aureus (MRSA) isolates were analyzed following 10% (v/v) ethanol challenge (15 min), which arrested growth but did not reduce viability. Ethanol-induced stress (EIS) resulted in differential gene expression of 1091 genes, 600 common to both strains, of which 291 were upregulated. With the exception of the downregulation of genes involved with osmotic stress functions, EIS resulted in the upregulation of genes that contribute to stress response networks, notably those altered by oxidative stress, protein quality control in general, and heat shock in particular. In addition, genes involved with transcription, translation, and nucleotide biosynthesis were downregulated. relP, which encodes a small alarmone synthetase (RelP), was highly upregulated in both MRSA strains following ethanol challenge, and relP inactivation experiments indicated that this gene contributed to EIS growth arrest. A number of persistence-associated genes were also upregulated during EIS, including those that encode toxin–antitoxin systems. Overall, transcriptional profiling indicated that the MRSA investigated responded to EIS by entering a state of dormancy and by altering the expression of elements from cross protective stress response systems in an effort to protect preexisting proteins.

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The small RNA RyhB homologs from Salmonella typhimurium participate in the response to S-nitrosoglutathione-induced stress

Biochemical and Biophysical Research Communications ◽

10.1016/j.bbrc.2014.06.031 ◽

2014 ◽

Vol 450 (1) ◽

pp. 641-645 ◽

Cited By ~ 18

Author(s):

Paulina F. Calderón ◽

Eduardo H. Morales ◽

Lillian G. Acuña ◽

Danitza N. Fuentes ◽

Fernando Gil ◽

...

Keyword(s):

Salmonella Typhimurium ◽

Small Rna ◽

Induced Stress

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Phenytoin-Induced Stress Protein Synthesis In Mouse Embryonic Tissue

Experimental Biology and Medicine ◽

10.3181/00379727-189-1-rc2 ◽

1988 ◽

Vol 189 (1) ◽

pp. 136-140 ◽

Cited By ~ 17

Author(s):

D. K. Hansen ◽

J. F. Anson ◽

W. G. Hinson ◽

J. L. Pipkin

Keyword(s):

Protein Synthesis ◽

Stress Protein ◽

Embryonic Tissue ◽

Induced Stress

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Structural investigation on SPI ‐6 associated Salmonella Typhimurium VirG ‐like stress protein that promotes pathogen survival in macrophages

Protein Science ◽

10.1002/pro.4272 ◽

2022 ◽

Author(s):

Shilpa Ray ◽

Nishant Kumar Pandey ◽

Gajraj Singh Kushwaha ◽

Susmita Das ◽

Akshay Kumar Ganguly ◽

...

Keyword(s):

Salmonella Typhimurium ◽

Structural Investigation ◽

Stress Protein ◽

Pathogen Survival

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Comparative Analysis of the Roles of HtrA-Like Surface Proteases in Two Virulent Staphylococcus aureus Strains

Infection and Immunity ◽

10.1128/iai.73.1.563-572.2005 ◽

2005 ◽

Vol 73 (1) ◽

pp. 563-572 ◽

Cited By ~ 43

Author(s):

Candice Rigoulay ◽

José M. Entenza ◽

David Halpern ◽

Eleonora Widmer ◽

Philippe Moreillon ◽

...

Keyword(s):

Staphylococcus Aureus ◽

Rat Model ◽

Stress Protein ◽

Bacterial Survival ◽

Slight Effect ◽

Induced Stress ◽

Bacterial Dissemination ◽

Virulent Strains ◽

Stress Survival ◽

Insertion Mutants

ABSTRACT The HtrA surface protease is involved in the virulence of many pathogens, mainly by its role in stress resistance and bacterial survival. Staphylococcus aureus encodes two putative HtrA-like proteases, referred to as HtrA1 and HtrA2. To investigate the roles of HtrA proteins in S. aureus, we constructed htrA 1, htrA 2, and htrA 1 htrA 2 insertion mutants in two genetically different virulent strains, RN6390 and COL. In the RN6390 context, htrA 1 inactivation resulted in sensitivity to puromycin-induced stress. The RN6390 htrA 1 htrA 2 mutant was affected in the expression of several secreted virulence factors comprising the agr regulon. This observation was correlated with the disappearance of the agr RNA III transcript in the RN6390 htrA 1 htrA 2 mutant. The virulence of this mutant was diminished in a rat model of endocarditis. In the COL context, both HtrA1 and HtrA2 were essential for thermal stress survival. However, only HtrA1 had a slight effect on exoprotein expression. The htrA mutations did not diminish the virulence of the COL strain in the rat model of endocarditis. Our results indicate that HtrA proteins have different roles in S. aureus according to the strain, probably depending on specific differences in the regulation of virulence factor and stress protein expression. We propose that HtrA1 and HtrA2 contribute to pathogenicity by controlling the production of certain extracellular factors that are crucial for bacterial dissemination, as revealed in the RN6390 background. We speculate that HtrA proteins act in the agr-dependent regulation pathway by assuring folding and/or maturation of some surface components of the agr system.

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Neutralization by Insulin of the Hypertensive Effect of Dermcidin Isoform 2: An Environmentally Induced Diabetogenic and Hypertensive Protein

Cardiology Research and Practice ◽

10.1155/2014/412815 ◽

2014 ◽

Vol 2014 ◽

pp. 1-10 ◽

Cited By ~ 4

Author(s):

Rajeshwary Ghosh ◽

Sarbashri Bank ◽

Rabindra Bhattacharya ◽

Nighat N. Khan ◽

A. Kumar Sinha

Keyword(s):

Diabetes Mellitus ◽

Salicylic Acid ◽

Stress Protein ◽

Insulin Level ◽

Acetyl Salicylic Acid ◽

Kidney Cortex ◽

Atherosclerotic Risk Factor ◽

Induced Stress ◽

Atherosclerotic Risk Factors

The effect of dermcidin isoform 2 (dermcidin), an environmentally induced stress protein, was investigated on the genesis of diabetes mellitus and hypertension, the two major atherosclerotic risk factors. The role of dermcidin as an atherosclerotic risk factor related to the impaired systemic insulin level was investigated. Dermcidin was prepared by electrophoresis using plasma from the subjects with acute ischemic heart disease. Injection of 0.2 μM dermcidin in mice increased the blood glucose level from98±2.45 mg/dL to350 ±10.2 mg/dL which was normalized by the oral administration of acetyl salicylic acid (aspirin) after 24 h. Hypertensive subjects with systolic and diastolic blood pressure of 165 mm and 95 mm of Hg, respectively, had plasma dermcidin level of 95 nM. Ingestion of acetyl salicylic acid (aspirin) (150 mg/70 kg body weight) decreased the systolic and diastolic pressures to 125 mm and 80 mm of Hg, respectively, with decrease of dermcidin level to 15 nM. Incubation of kidney cortex cells with 0.2 μM dermcidin-inhibited synthesis of (r)-cortexin, an antihypertensive protein, and the basal (r)-cortexin level was reduced from 33 nM to 15 nM. Addition of 25 μunits of insulin/mL was found to reverse the inhibition of cortexin synthesis. The effect of dermcidin as a diabetogenic and a hypertensive agent could be controlled either by aspirin or by insulin.

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