OmpA, a Common Virulence Factor, Is Under RNA Thermometer Control in Yersinia pseudotuberculosis.
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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.read more
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References
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RNA Thermometers in Bacterial Pathogens
Edmund Loh,Edmund Loh,Francesco Righetti,Hannes Eichner,Christian Twittenhoff,Franz Narberhaus +5 more
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.
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Multiple layers of control govern expression of the Escherichia coli ibpAB heat-shock operon
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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.
Xavier Vila-Farrés,Raquel Parra-Millán,Viviana Sánchez-Encinales,Monica Varese,Rafael Ayerbe-Algaba,Nuria Bayó,Salvador Guardiola,María Eugenia Pachón-Ibáñez,Martin Kotev,Jesús García,Meritxell Teixidó,Jordi Vila,Jerónimo Pachón,Ernest Giralt,Younes Smani +14 more
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.
Journal ArticleDOI
Overproduction of Outer Membrane Protein A by Acinetobacter baumannii as a Risk Factor for Nosocomial Pneumonia, Bacteremia, and Mortality Rate Increase.
Sánchez-Encinales,Rocío Álvarez-Marín,María Eugenia Pachón-Ibáñez,Felipe Fernández-Cuenca,Álvaro Pascual,José Garnacho-Montero,Luis Martínez-Martínez,Jordi Vila,Mar Tomás,José Miguel Cisneros,Germán Bou,Jesús Rodríguez-Baño,Jerónimo Pachón,Younes Smani +13 more
TL;DR: It is suggested that ompA overexpression is an associated factor for pneumonia, bacteremia, and death due to A. baumannii.