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OmpA, a Common Virulence Factor, Is Under RNA Thermometer Control in Yersinia pseudotuberculosis.

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TLDR
This article found evidence for temperature-modulated RNA structure in the 5'-untranslated region (5'-UTR) of the Yersinia pseudotuberculosis ompA transcript suggesting that opening of the structure at host-body temperature might relieve translational repression.
Abstract
The outer membrane protein OmpA is a virulence factor in many mammalian pathogens. In previous global RNA structure probing studies, we found evidence for a temperature-modulated RNA structure in the 5'-untranslated region (5'-UTR) of the Yersinia pseudotuberculosis ompA transcript suggesting that opening of the structure at host-body temperature might relieve translational repression. Here, we support this hypothesis by quantitative reverse transcription PCR, translational reporter gene fusions, enzymatic RNA structure probing, and toeprinting assays. While ompA transcript levels decreased at 37°C compared to 25°C, translation of the transcript increased with increasing temperature. Biochemical experiments show that this is due to melting of the RNA structure, which permits ribosome binding to the 5'-UTR. A point mutation that locks the RNA structure in a closed conformation prevents translation by impairing ribosome access. Our findings add another common virulence factor to the growing list of pathogen-associated genes that are under RNA thermometer control.

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Lipopolysaccharide -mediated resistance to host antimicrobial peptides and hemocyte-derived reactive-oxygen species are the major Providencia alcalifaciens virulence factors in Drosophila melanogaster

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RNA thermometers in bacteria: Role in thermoregulation.

TL;DR: In this article , the authors discuss the role of RNA Thermometers in mediating expression of temperature-responsive genes like heat shock/cold attributing in heat/cold shock response and a cascade of virulence genes to evade host defence mechanisms.
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Developing New Tools to Fight Human Pathogens: A Journey through the Advances in RNA Technologies

TL;DR: In this paper , a review of the connection between RNA metabolism and pathogenesis in Gram-positive and Gram-negative bacteria is presented, and the authors discuss how RNA techniques have contributed to the building of this knowledge and the development of new tools in synthetic biology for the diagnosis and treatment of diseases caused by pathogenic microorganisms.
Posted ContentDOI

The oxidative stress response, in particular the<i>katY</i>gene, is temperature-regulated in<i>Yersinia pseudotuberculosis</i>

TL;DR: In this paper , the authors systematically analyzed the transcriptional and translational regulation of ROS defense genes by RNA-sequencing, qRT-PCR, translational reporter gene fusions, enzymatic RNA structure probing and toeprinting assays.
References
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Journal ArticleDOI

RNA Thermometers in Bacterial Pathogens

TL;DR: This review summarizes the present knowledge on virulence-related RNATs and discusses recent developments in the field to fine-tune virulence gene expression when the pathogen enters or exits the body of its host.
Journal ArticleDOI

Multiple layers of control govern expression of the Escherichia coli ibpAB heat-shock operon

TL;DR: It is reported that expression of ibpAB is a complex process involving at least four different layers of control, namely transcriptional control, RNA processing, translation control and protein stability.
Journal ArticleDOI

RNA-mediated thermoregulation of iron-acquisition genes in Shigella dysenteriae and pathogenic Escherichia coli.

TL;DR: This study examines the regulated production of ShuA, an outer-membrane receptor required for the utilization of heme as a source of nutrient iron by Shigella dysenteriae, a pathogenic bacterium that causes severe diarrheal diseases in humans and shows that shuA expression is subject to temperature-dependent post-transcriptional regulation resulting in increased ShuA production.
Journal ArticleDOI

Combating virulence of Gram-negative bacilli by OmpA inhibition.

TL;DR: A cyclic hexapeptide AOA-2 is identified that inhibits the adhesion of Acinetobacter baumannii, Pseudomonas aeruginosa and Escherichia coli to host cells and the formation of biofilm, thereby preventing the development of infection in vitro and in a murine sepsis peritoneal model.
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