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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

A Novel Interaction of Outer Membrane Protein A with C4b Binding Protein Mediates Serum Resistance of Escherichia coli K1.

TL;DR: It is reported that outer membrane protein A of Escherichia coli contributes to serum resistance by binding to C4b binding protein (C4bp), a complement fluid phase regulator, and it is demonstrated that the N terminus of OmpA interacts with C4bp.
Journal ArticleDOI

FourU: a novel type of RNA thermometer in Salmonella

TL;DR: This work has identified a new type of RNA thermometer in the 5′‐UTR of the Salmonella agsA gene, which codes for a small heat shock protein, and proposes to name ‘fourU’ thermometers, which are based on a stretch of four uridines that pair with the SD sequence.
Journal ArticleDOI

Concerted Actions of a Thermo-labile Regulator and a Unique Intergenic RNA Thermosensor Control Yersinia Virulence

TL;DR: It is shown that a protein- and RNA-dependent hierarchy of thermosensors induce LcrF synthesis at body temperature, and that Y.ersinia strains with a destabilized version of the thermosensor were attenuated or exhibited a similar, but not a higher mortality.
Journal ArticleDOI

TolB protein of Escherichia coli K‐12 interacts with the outer membrane peptidoglycan‐associated proteins Pal, Lpp and OmpA

TL;DR: It is proposed that TolB and Pal are part of a multiprotein complex that links the peptidoglycan to the outer membrane and might form transenvelope complexes that bring the two membranes into close proximity and help some outer membrane components to reach their final destination.
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