Glycolytic reprograming in Salmonella counters NOX2-mediated dissipation of ΔpH

Sangeeta Chakraborty, Lin Liu, Liam Fitzsimmons, Steffen Porwollik, Ju-Sim Kim, Prerak Desai, Michael McClelland and Andres Vazquez-Torres ()
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Sangeeta Chakraborty: University of Colorado School of Medicine
Lin Liu: University of Colorado School of Medicine
Liam Fitzsimmons: University of Colorado School of Medicine
Steffen Porwollik: University of California Irvine School of Medicine
Ju-Sim Kim: University of Colorado School of Medicine
Prerak Desai: University of California Irvine School of Medicine
Michael McClelland: University of California Irvine School of Medicine
Andres Vazquez-Torres: University of Colorado School of Medicine

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: Abstract The microbial adaptations to the respiratory burst remain poorly understood, and establishing how the NADPH oxidase (NOX2) kills microbes has proven elusive. Here we demonstrate that NOX2 collapses the ΔpH of intracellular Salmonella Typhimurium. The depolarization experienced by Salmonella undergoing oxidative stress impairs folding of periplasmic proteins. Depolarization in respiring Salmonella mediates intense bactericidal activity of reactive oxygen species (ROS). Salmonella adapts to the challenges oxidative stress imposes on membrane bioenergetics by shifting redox balance to glycolysis and fermentation, thereby diminishing electron flow through the membrane, meeting energetic requirements and anaplerotically generating tricarboxylic acid intermediates. By diverting electrons away from the respiratory chain, glycolysis also enables thiol/disulfide exchange-mediated folding of bacterial cell envelope proteins during periods of oxidative stress. Thus, primordial metabolic pathways, already present in bacteria before aerobic respiration evolved, offer a solution to the stress ROS exert on molecular targets at the bacterial cell envelope.

Date: 2020
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DOI: 10.1038/s41467-020-15604-2

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