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Peptidoglycan recycling is critical for cell division, cell wall integrity and β-lactam resistance in Caulobacter crescentus

ABSTRACT: Most bacteria possess a peptidoglycan cell wall, which is continuously remodeled during cell growth and divi¬sion. The peptidoglycan (PG) fragments generated in this process are typically imported into the cell and recycles through the PG biosynthesis pathway. While the underlying pathways have been studied intens¬ively in gamma¬proteobacteria, knowledge of their presence and physiological roles in other bacterial line¬ages remains limited. Here, we comprehensively investigate PG recycling in the alphaproteo¬bacterial model organism Caulo¬bacter crescentus. We show that this species contains a func¬tional PG recycling pathway by char¬acterizing the activities of key enzymes both in vitro and in vivo. Our results reveal that PG recycling is critical for maintaining C. crescentus cell morphology and division and is dynamically regu¬lated to balance the flux of metabolic intermediates toward PG biosynthesis and central carbon metabol¬ism. Im¬portantly, defects in PG recyc¬ling strongly impair the intrinsic ampicillin resistance of C. crescentus without changing the activity of its β-lactamase BlaA, likely by limiting PG precursor biosynthesis and thereby increasing the sensitivity of the septal FtsW-FtsI com-plex to residual antibiotic molecules. These findings underscore the central role of PG recyc¬¬ling in bacterial fitness and suggest that inhibiting this process could provide a promising strategy to combat β-lactam-resistant pathogens.

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ORGANISM(S): Caulobacter Crescentus (strain Na1000 / Cb15n)

SUBMITTER: Timo Glatter

LAB HEAD: Timo Glatter

PROVIDER: PXD069004 | Pride | 2026-03-11

REPOSITORIES: Pride

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Project description:Metabolism is fundamental to life, all life activities are sustained through metabolism. Metabolic engineering, while modifying host endogenous metabolic network or introducing heterologous pathway for biotechnological applications, often results in unfitness and suboptimal characteristics, because of the lack of full knowledge on host metabolism. Adaptive laboratory evolution (ALE), harnessing the nature of life -- evolution, has become a potent approach in phenotype optimization, environmental adaptation, and cell biology study1–3. Through ALE, alternative pathways of β-alanine biosynthesis4, pyridoxal 5’-phosphate (PLP) biosynthesis5, isoleucine biosynthesis6, as well as ATP generation7 have been uncovered; E. coli aerobic citrate utilization8,9 and various synthetic C1-trophy10–14 have been realized. In this study, we describe E. coli recruits the same workforce, Sad, in evolution through various strategies, i.e., catalytic efficiency improvement, gene dose increase, and gene expression regulations, to overcome metabolic damages (Fig. 1). Sad, i.e. NAD(P)+-dependent succinate semialdehyde dehydrogenase (SSADH), is an aldehyde dehydrogenase (ALDH) family protein. Sad oxidizes succinate semialdehyde to succinate, preventing accumulation of the toxic aldehyde intermediate in nitrogen metabolism, such as putrescine, arginine and γ-aminobutyrate (GABA) degradations15–17. Some bacteria, for example E. coli, possess also a NADP+-dependent SSADH, GabD15,18. SSADH is ubiquitous in both prokaryotes and eukaryotes. In human, it involves in catabolism of GABA, a major neurotransmitter, its malfunction leads to a disorder SSADH deficiency19. In plants, SSADH involves in leaf development and morphogenesis20 as well as defense of abiotic stress21. And in cyanobacteria, SSADH is an essential enzyme of its uncanonical tricarboxylic acid cycle. SSADH was also found to be able to oxidize glutarate semialdehyde, participating in lysine catabolism in bacteria.

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Peptidoglycan recycling is critical for cell division, cell wall integrity and β-lactam resistance in Caulobacter crescentus

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