Abstract
Translational fidelity is maintained by multiple quality control steps in all three domains of life. Increased translational errors (mistranslation) occur due to genetic mutations and external stresses. Severe mistranslation is generally harmful, but moderate levels of mistranslation may be favored under certain conditions. To date, little is known about the link between translational fidelity and host–pathogen interactions. Salmonella enterica can survive in the gall bladder during systemic or chronic infections due to bile resistance. Here we show that increased translational fidelity contributes to the fitness of Salmonella upon bile salt exposure, and the improved fitness depends on an increased level of intracellular adenosine triphosphate (ATP). Our work thus reveals a previously unknown linkage between translational fidelity and bacterial fitness under bile stress.
Highlights
The transfer of genetic information from DNA to protein requires optimized levels of fidelity and speed
We have recently shown that optimal translational fidelity is pivotal for the adaptation of Salmonella to interact with host cells [20]
To understand the link between translational fidelity and fitness during exposure in bile salts, we separately introduced mutations I199N and K42N into the ribosomal genes rpsD and rpsL in the S. enterica Typhimurium strain ATCC 14028
Summary
The transfer of genetic information from DNA to protein requires optimized levels of fidelity and speed. It has been suggested that natural E. coli isolates have a wide range of ribosomal fidelity, implying that some degree of mistranslation may be favored under distinct environments [14]. Growing evidence suggests that increased translational errors could be adaptive and beneficial under certain conditions [15,16,17,18]. We have recently shown that optimal translational fidelity is pivotal for the adaptation of Salmonella to interact with host cells [20]. We demonstrate that an increase in ribosomal fidelity enhances the growth of Salmonella in the presence of bile salts.
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