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Multiple targets of nitric oxide in the tricarboxylic acid cycle of Salmonella enterica serovar typhimurium.

Abstract：

:Host nitric oxide (NO⋅) production is important for controlling intracellular bacterial pathogens, including Salmonella enterica serovar Typhimurium, but the underlying mechanisms are incompletely understood. S. Typhmurium 14028s is prototrophic for all amino acids but cannot synthesize methionine (M) or lysine (K) during nitrosative stress. Here, we show that NO⋅-induced MK auxotrophy results from reduced succinyl-CoA availability as a consequence of NO⋅ targeting of lipoamide-dependent lipoamide dehydrogenase (LpdA) activity. LpdA is an essential component of the pyruvate and α-ketoglutarate dehydrogenase complexes. Additional effects of NO⋅ on gene regulation prevent compensatory pathways of succinyl-CoA production. Microarray analysis indicates that over 50% of the transcriptional response of S. Typhimurium to nitrosative stress is attributable to LpdA inhibition. Bacterial methionine transport is essential for virulence in NO⋅-producing mice, demonstrating that NO⋅-induced MK auxotrophy occurs in vivo. These observations underscore the importance of metabolic targets for antimicrobial actions of NO⋅.

journal_name

Cell Host Microbe

journal_title

Cell host & microbe

authors

Richardson AR,Payne EC,Younger N,Karlinsey JE,Thomas VC,Becker LA,Navarre WW,Castor ME,Libby SJ,Fang FC

doi

10.1016/j.chom.2011.06.004

subject

Has Abstract

pub_date

2011-07-21 00:00:00

pages

33-43

issue

1

eissn

1931-3128

issn

1934-6069

pii

S1931-3128(11)00194-6

journal_volume

10

pub_type

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