Imbalance of peptidoglycan biosynthesis alters the cell surface charge of Listeria monocytogenes

Schulz, Lisa Maria; Rothe, Patricia; Halbedel, Sven; Gründling, Angelika; Rismondo, Jeanine

doi:10.1016/j.tcsw.2022.100085

Cited by 3 publications

(3 citation statements)

References 81 publications

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“…The IreB-IreB self-interaction is used as a positive control while leucine zipper domains (Zip) were used for negative controls. Strains are wild-type, OG1; ΔmurAB, CM1; murAB C116S, CM40.Mg 2+ has been proposed to have stabilizing effects on peptidoglycan through unknown mechanisms(Schulz et al, 2022;Tesson et al, 2022). Taken together, these results are consistent with a hypothesis that in the absence of IreK, cells cannot properly adapt to cell envelope stress, at least in part, due to their inability to modulate MurAA levels.…”

supporting

confidence: 83%

“…Supplementation of the growth media with 20 mM MgCl 2 also partially rescued the growth defect of the Δ ireK strain during heat‐stress (Figure S15b). Mg 2+ has been proposed to have stabilizing effects on peptidoglycan through unknown mechanisms (Schulz et al, 2022; Tesson et al, 2022). Taken together, these results are consistent with a hypothesis that in the absence of IreK, cells cannot properly adapt to cell envelope stress, at least in part, due to their inability to modulate MurAA levels.…”

Section: Resultsmentioning

confidence: 99%

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PASTA‐kinase‐mediated signaling drives accumulation of the peptidoglycan synthesis protein MurAA to promote cephalosporin resistance in Enterococcus faecalis

Mascari,

Little,

Kristich

2023

Molecular Microbiology

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The bacterial PASTA kinase, IreK, is required for intrinsic cephalosporin resistance in the Gram‐positive opportunistic pathogen, Enterococcus faecalis. IreK activity is enhanced in response to cell wall stress, such as cephalosporin exposure. The downstream consequences of IreK activation are not well understood in E. faecalis, but recent work in other low‐GC Gram‐positive bacteria demonstrated PASTA kinase‐dependent regulation of MurAA, an enzyme that performs the first committed step in the peptidoglycan synthesis pathway. Here, we used genetic suppressor selections to identify MurAA as a downstream target of IreK signaling in E. faecalis. Using complementary genetic and biochemical approaches, we demonstrated that MurAA abundance is regulated by IreK signaling in response to physiologically relevant cell wall stress to modulate substrate flux through the peptidoglycan synthesis pathway. Specifically, the IreK substrate, IreB, promotes proteolysis of MurAA through a direct physical interaction in a manner responsive to phosphorylation by IreK. MurAB, a homolog of MurAA, also promotes MurAA proteolysis and interacts directly with IreB. Our results therefore establish a connection between the cell wall stress sensor IreK and one critical physiological output to modulate peptidoglycan synthesis and drive cephalosporin resistance.

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supporting

confidence: 83%

Section: Resultsmentioning

confidence: 99%

PASTA‐kinase‐mediated signaling drives accumulation of the peptidoglycan synthesis protein MurAA to promote cephalosporin resistance in Enterococcus faecalis

Mascari,

Little,

Kristich

2023

Molecular Microbiology

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“…We attempted to determine whether this increase in PG labeling was PrkA-dependent, but transduction of the ΔprkA::erm allele into strains harboring trans-encoded gpsB, gpsBT88A, and gpsBT88D resulted frequently in suppressor formation at routine growth temperature, and therefore detailed analyses using these strains was not possible. In addition to the role of GpsB homologs in regulating PBP activity, a recent study by Hammond et al (41) determined that GpsB also modulates wall teichoic acid synthesis in B. subtilis, and Schulz et al recently demonstrated that changes in wall teichoic acid composition can affect resistance of L. monocytogenes to cell wall insults (42). Future studies are warranted to understand whether GpsB has PrkA-independent roles in resisting cell wall stress responses in L. monocytogenes.…”

Section: Discussionmentioning

confidence: 99%

GpsB control of PASTA kinase activity inListeria monocytogenesinfluences peptidoglycan synthesis during cell wall stress and cytosolic survival

Kelliher

Daanen

Sauer

2023

Preprint

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The ability to respond quickly to changing environmental conditions in the host is critical for bacterial pathogens. Penicillin-binding protein and serine/threonine-associated (PASTA) kinases are a conserved family of kinases important for cell envelope stress responses inFirmicutesandActinobacteria, including the cytosolic pathogenListeria monocytogenes. As serine/threonine kinases, PASTA kinases phosphorylate multiple substrates, yet the mechanisms through which these substrates promote resistance to cell wall stress remain poorly understood. We previously identified GpsB as a target of PrkA, the PASTA kinase inL. monocytogenes, through a phosphoproteomics screen. Here, we demonstrate that GpsB can be directly phosphorylated by PrkA, and that mutation of the PrkA-dependent phosphosite T88 to a phosphoablative residue enhances PrkA activityin vitro. We find that relative to a strain ofL. monocytogenesharboring thegpsBT88Aallele, a strain with the phosphomimeticgpsBT88Dallele is more sensitive to the cephalosporin antibiotic ceftriaxone and has a diminished capacity to increase peptidoglycan synthesis during stress. We find that GpsB-dependent control of PrkA activity is required for optimal survival and replication ofL. monocytogenesin the macrophage cytosol. Finally, we show that GpsB is required for full virulence ofL. monocytogenes, due in part to its role in modulating PrkA activity. Cumulatively, these results demonstrate that phosphorylative feedback between GpsB and PrkA is important for the ability ofL. monocytogenesto respond to cell wall stress, survive in its cytosolic niche, and cause infection.

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Adaptive responses of Dermacoccus abyssi HZAU 226 to lysozyme stress

Zhang,

Chen,

Guo

et al. 2024

Food Bioscience

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Imbalance of peptidoglycan biosynthesis alters the cell surface charge of Listeria monocytogenes

Cited by 3 publications

References 81 publications

PASTA‐kinase‐mediated signaling drives accumulation of the peptidoglycan synthesis protein MurAA to promote cephalosporin resistance in Enterococcus faecalis

PASTA‐kinase‐mediated signaling drives accumulation of the peptidoglycan synthesis protein MurAA to promote cephalosporin resistance in Enterococcus faecalis

GpsB control of PASTA kinase activity inListeria monocytogenesinfluences peptidoglycan synthesis during cell wall stress and cytosolic survival

Adaptive responses of Dermacoccus abyssi HZAU 226 to lysozyme stress

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