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Mammalian peptidoglycan recognition proteins (PGRPs or PGLYRPs) kill bacteria through induction of synergistic oxidative, thiol, and metal stress. Tn-seq screening of  Bacillus subtilis  transposon insertion library revealed that mutants in the shikimate pathway of chorismate synthesis had high survival following PGLYRP4 treatment. Deletion mutants for these genes had decreased amounts of menaquinone (MK), increased resistance to killing, and attenuated depletion of thiols following PGLYRP4 treatment. These effects were reversed by MK or reproduced by inhibiting MK synthesis. Deletion of cytochrome  aa   3  -600 or NADH dehydrogenase (NDH) genes also increased  B. subtilis  resistance to PGLYRP4-induced killing and attenuated thiol depletion. PGLYRP4 treatment also inhibited  B. subtilis  respiration. Similarly in  Escherichia coli , deletion of ubiquinone (UQ) synthesis, formate dehydrogenases (FDH), NDH-1, or cytochrome  bd -I genes attenuated PGLYRP4-induced thiol depletion. PGLYRP4-induced low level of cytoplasmic membrane depolarization in  B. subtilis  and  E. coli  was likely not responsible for thiol depletion. Thus, our results show that the respiratory electron transport chain components, cytochrome  aa   3  -600, MK, and NDH in  B. subtilis , and cytochrome  bd -I, UQ, FDH-O, and NDH-1 in  E. coli , are required for both PGLYRP4-induced killing and thiol depletion and indicate conservation of the PGLYRP4-induced thiol depletion and killing mechanisms in Gram-positive and Gram-negative bacteria.

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Respiratory chain components are required for peptidoglycan recognition protein-induced thiol depletion and killing in Bacillus subtilis and Escherichia coli