Differential modes of crosslinking establish spatially distinct regions of peptidoglycan in <i>Caulobacter crescentus</i>

Stankeviciute, Gabriele; Miguel, Amanda; Radkov, Atanas; Chou, Seemay; Huang, Kerwyn Casey; Klein, Eric A.

doi:10.1111/mmi.14199

Cited by 24 publications

(26 citation statements)

References 56 publications

(77 reference statements)

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“…In fact, there is a certain correlation between the amount of LD-cross-linkage and sensitivity to lysozyme in other Gram-negative bacteria as well. For instance, A. tumefaciens has a PG rich in LD-cross-links and is also highly resistant to lysozyme degradation [75]. In E. coli, the lower susceptibility to…”

Section: Ld-cross-links Might Provide Lysozyme Resistancementioning

confidence: 99%

LD‐transpeptidases: the great unknown among the peptidoglycan cross‐linkers

Aliashkevich

Cava

2021

The FEBS Journal

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The peptidoglycan (PG) cell wall is an essential polymer for the shape and viability of bacteria. Its protective role is in great part provided by its mesh-like character. Therefore, PG-cross-linking enzymes like the penicillin-binding proteins (PBPs) are among the best targets for antibiotics. However, while PBPs have been in the spotlight for more than 50 years, another class of PG-cross-linking enzymes called LDtranspeptidases (LDTs) seemed to contribute less to PG synthesis and, thus, has kept an aura of mystery. In the last years, a number of studies have associated LDTs with cell wall adaptation to stress including blactam antibiotics, outer membrane stability, and toxin delivery, which has shed light onto the biological meaning of these proteins. Furthermore, as some species display a great abundance of LD-cross-links in their cell wall, it has been hypothesized that LDTs could also be the main synthetic PGtranspeptidases in some bacteria. In this review, we introduce these enzymes and their role in PG biosynthesis and we highlight the most recent advances in understanding their biological role in diverse species.

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Section: Ld-cross-links Might Provide Lysozyme Resistancementioning

confidence: 99%

LD‐transpeptidases: the great unknown among the peptidoglycan cross‐linkers

Aliashkevich

Cava

2021

The FEBS Journal

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“…Upregulation of PG-modifying enzymes may serve to reinforce the envelope during stress in other compartments of the envelope so as to increase its overall stability. Interestingly, it was recently shown that increased levels of DAP-DAP crosslinkages increases resistance to lysozyme (Stankeviciute et al, 2019). It is possible that Cpx-regulation of ldtD and ygaU may be a strategy for dealing with envelope stress arising from host innate immunity.…”

Section: The Cpxra Two-component Systemmentioning

confidence: 99%

Maintaining Integrity Under Stress: Envelope Stress Response Regulation of Pathogenesis in Gram-Negative Bacteria

Cho

Rowley

Raivio

2019

Front. Cell. Infect. Microbiol.

114

129

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The Gram-negative bacterial envelope is an essential interface between the intracellular and harsh extracellular environment. Envelope stress responses (ESRs) are crucial to the maintenance of this barrier and function to detect and respond to perturbations in the envelope, caused by environmental stresses. Pathogenic bacteria are exposed to an array of challenging and stressful conditions during their lifecycle and, in particular, during infection of a host. As such, maintenance of envelope homeostasis is essential to their ability to successfully cause infection. This review will discuss our current understanding of the σE- and Cpx-regulated ESRs, with a specific focus on their role in the virulence of a number of model pathogens.

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“…In contrast to the PG transglycosylases, inhibition of the transpeptidase PBP2 blocks stalk elongation (9,10), as does depletion of MreB or RodA (11), which are regulators of PBP2 activity in E. coli (12,13). Additionally, the stalk PG is enriched for LD-cross-links (between meso-DAP residues on neighboring peptide stems) (9,14); while these LD-cross-links increase stalk PG resistance to lysozyme-mediated degradation (14), abrogation of LD-transpeptidation has no effect on stalk elongation (9,14).…”

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confidence: 99%

Sugar-Phosphate Metabolism Regulates Stationary-Phase Entry and Stalk Elongation in Caulobacter crescentus

2020

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Bacteria have a variety of mechanisms for adapting to environmental perturbations. Changes in oxygen availability result in a switch between aerobic and anaerobic respiration, whereas iron limitation may lead to siderophore secretion. In addition to metabolic adaptations, many organisms respond by altering their cell shape. Caulobacter crescentus, when grown under phosphate-limiting conditions, dramatically elongates its polar stalk appendage. The stalk is hypothesized to facilitate phosphate uptake; however, the mechanistic details of stalk synthesis are not well characterized. We used a chemical mutagenesis approach to isolate and characterize stalk-deficient mutants, one of which had two mutations in the phosphomannose isomerase gene (manA) that were necessary and sufficient to inhibit stalk elongation. Transcription of the pho regulon was unaffected in the manA mutant; therefore, ManA plays a unique regulatory role in stalk synthesis. The mutant ManA had reduced enzymatic activity, resulting in a 5-fold increase in the intracellular fructose 6-phosphate/mannose 6-phosphate ratio. This metabolic imbalance impaired the synthesis of cellular envelope components derived from mannose 6-phosphate, namely, lipopolysaccharide O-antigen and exopolysaccharide. Furthermore, the manA mutations prevented C. crescentus cells from efficiently entering stationary phase. Deletion of the stationary-phase response regulator gene spdR inhibited stalk elongation in wild-type cells, while overproduction of the alarmone ppGpp, which triggers growth arrest and stationary-phase entry, increased stalk length in the manA mutant strain. These results demonstrate that sugar-phosphate metabolism regulates stalk elongation independently of phosphate starvation. IMPORTANCE Metabolic control of bacterial cell shape is an important mechanism for adapting to environmental perturbations. Caulobacter crescentus dramatically elongates its polar stalk appendage in response to phosphate starvation. To investigate the mechanism of this morphological adaptation, we isolated stalk-deficient mutants, one of which had mutations in the phosphomannose isomerase gene (manA) that blocked stalk elongation, despite normal activation of the phosphate starvation response. The mutant ManA resulted in an imbalance in sugar-phosphate concentrations, which had effects on the synthesis of cellular envelope components and entry into stationary phase. Due to the interconnectivity of metabolic pathways, our findings may suggest more generally that the modulation of bacterial cell shape involves the regulation of growth phase and the synthesis of cellular building blocks.

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Differential modes of crosslinking establish spatially distinct regions of peptidoglycan in Caulobacter crescentus

Cited by 24 publications

References 56 publications

LD‐transpeptidases: the great unknown among the peptidoglycan cross‐linkers

LD‐transpeptidases: the great unknown among the peptidoglycan cross‐linkers

Maintaining Integrity Under Stress: Envelope Stress Response Regulation of Pathogenesis in Gram-Negative Bacteria

Sugar-Phosphate Metabolism Regulates Stationary-Phase Entry and Stalk Elongation in Caulobacter crescentus

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