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To withstand the membrane depolarization that potentiates the killing activity of reactive oxygen species (ROS) produced by the phagocyte NADPH oxidase,\n                      <jats:italic toggle=\"yes\">Salmonella<\/jats:italic>\n                      employs metabolic adaptations that maintain intracellular pH homeostasis and membrane energetics. Here, we identify amino acid decarboxylation as a critical determinant of\n                      <jats:italic toggle=\"yes\">Salmonella<\/jats:italic>\n                      virulence and resistance to the oxidative pressures within the host environment. The proton-consuming decarboxylation of L-arginine preserves intracellular \u2206pH and enhances\n                      <jats:italic toggle=\"yes\">Salmonella<\/jats:italic>\n                      survival against the bactericidal effects of ROS, while downstream polyamine biosynthesis aids in bacterial recovery following ROS exposure. Polyamines alone cannot substitute for the immediate, protective impact of proton-consuming decarboxylation during oxidative stress killing. Specifically, we show that\n                      <jats:italic toggle=\"yes\">Salmonella<\/jats:italic>\n                      relies on the combined activity of the inducible arginine AdiA and the ornithine SpeF decarboxylases for resistance to oxidative stress, and that this activity is essential for\n                      <jats:italic toggle=\"yes\">Salmonella<\/jats:italic>\n                      virulence during systemic infection. Together, amino acid decarboxylation and polyamine biosynthesis play complementary, but distinct roles in\n                      <jats:italic toggle=\"yes\">Salmonella<\/jats:italic>\n                      adaptation to phagocyte-derived oxidative stress, providing a new framework for understanding how amino acid catabolism influences bacterial survival in the host.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>IMPORTANCE<\/jats:title>\n                    <jats:p>\n                      Salmonellae have been causing disease in humans since at least the Neolithic Revolution, yet non-typhoidal Salmonella infections remain a significant public health challenge. The success of\n                      <jats:italic toggle=\"yes\">Salmonella<\/jats:italic>\n                      as a pathogen stems, in part, from its ability to subvert and survive the host response of macrophages. The amino acid L-arginine is critical for Salmonella enterica serovar Typhimurium virulence and resistance to reactive oxygen species produced by the phagocyte NADPH oxidase. The precise mechanisms by which L-arginine fosters oxidative stress resistance have remained unclear. In this report, we demonstrate that Salmonella relies on the proton-consuming decarboxylation of L-arginine and ornithine to promote resistance against the acute cytotoxicity emanating from the phagocyte NADPH oxidase. On the other hand, polyamines synthesized downstream of L-arginine and ornithine decarboxylation aid in the recovery phase. Our findings redefine the physiological role of amino acid decarboxylation, establishing it as a critical defense mechanism against oxidative stress that is functionally distinct from polyamine biosynthesis. By disentangling the regulatory and functional roles of individual decarboxylases, our study clarifies a long-standing ambiguity in the field and highlights how\n                      <jats:italic toggle=\"yes\">Salmonella<\/jats:italic>\n                      exploits complementary metabolic pathways during its adaptation to oxidative stress in the host.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/mbio.03147-25","type":"journal-article","created":{"date-parts":[[2025,11,24]],"date-time":"2025-11-24T14:00:26Z","timestamp":1763992826000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":4,"title":["Amino acid decarboxylation preserves\n                    <i>Salmonella<\/i>\n                    fitness during phagocyte-derived oxidative 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