Faculty Opinions recommendation of Identification of Two Phosphate Starvation-induced Wall Teichoic Acid Hydrolases Provides First Insights into the Degradative Pathway of a Key Bacterial Cell Wall Component.

2017 ◽  
Author(s):  
Angelika Gründling
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Teichoic Acid ◽  
Phosphate Starvation ◽  
Bacterial Cell Wall ◽  
Acid Hydrolases ◽  
Wall Teichoic Acid ◽  
Cell Wall Component ◽  
Degradative Pathway

scholarly journals Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase

2021 ◽  
Author(s):  
Yang Shen ◽  
Ioanna Kalograiaki ◽  
Alessio Prunotto ◽  
Matthew Dunne ◽  
Samy Boulos ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Molecular Mechanisms ◽  
Teichoic Acid ◽  
Bacterial Cell Wall ◽  
Structural Basis ◽  
Peptidoglycan Hydrolase ◽  
Wall Teichoic Acid ◽  
Computational Approaches

Combining genetic, biochemical and computational approaches, we elucidated the molecular mechanisms underlying the recognition of Listeria wall teichoic acid by bacteriophage-encoded SH3b repeats.

scholarly journals Analysis of Bacillus subtilis tagAB andtagDEF Expression during Phosphate Starvation Identifies a Repressor Role for PhoP∼P

1998 ◽  
Vol 180 (3) ◽  
pp. 753-758 ◽  
Author(s):  
Wei Liu ◽  
Stephen Eder ◽  
F. Marion Hulett
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Teichoic Acid ◽  
Phosphate Starvation ◽  
Acid Synthesis ◽  
Pho Regulon ◽  
Wall Teichoic Acid ◽  
Negative Role ◽  
First Time ◽  
Starvation Conditions

ABSTRACT The tagAB and tagDEF operons, which are adjacent and divergently transcribed, encode genes responsible for cell wall teichoic acid synthesis in Bacillus subtilis. TheBacillus data presented here suggest that PhoP and PhoR are required for direct repression of transcription of the two operons under phosphate starvation conditions but have no regulatory role under phosphate-replete conditions. These data identify for the first time that PhoP∼P has a negative role in Pho regulon gene regulation.

scholarly journals Mass spectrometric quantitation of muramic acid, a bacterial cell wall component, in septic synovial fluids

1989 ◽  
Vol 32 (10) ◽  
pp. 1268-1272 ◽  
Author(s):  
Bertil Christensson ◽  
James Gilbart ◽  
Alvin Fox ◽  
Stephen L. Morgan
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Mass Spectrometric ◽  
Bacterial Cell Wall ◽  
Muramic Acid ◽  
Cell Wall Component ◽  
Synovial Fluids

scholarly journals Inflammasome Activation by Bacterial Outer Membrane Vesicles Requires Guanylate Binding Proteins

mBio ◽  
2017 ◽  
Vol 8 (5) ◽  
Author(s):  
Ryan Finethy ◽  
Sarah Luoma ◽  
Nichole Orench-Rivera ◽  
Eric M. Feeley ◽  
Arun K. Haldar ◽  
...  
Keyword(s):  
Cell Wall ◽  
Outer Membrane ◽  
Bacterial Cell ◽  
Binding Proteins ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Bacterial Cell Wall ◽  
Cell Wall Component ◽  
Gram Negative

ABSTRACT The Gram-negative bacterial cell wall component lipopolysaccharide (LPS) is recognized by the noncanonical inflammasome protein caspase-11 in the cytosol of infected host cells and thereby prompts an inflammatory immune response linked to sepsis. Host guanylate binding proteins (GBPs) promote infection-induced caspase-11 activation in tissue culture models, and yet their in vivo role in LPS-mediated sepsis has remained unexplored. LPS can be released from lysed bacteria as “free” LPS aggregates or actively secreted by live bacteria as a component of outer membrane vesicles (OMVs). Here, we report that GBPs control inflammation and sepsis in mice injected with either free LPS or purified OMVs derived from Gram-negative Escherichia coli. In agreement with our observations from in vivo experiments, we demonstrate that macrophages lacking GBP2 expression fail to induce pyroptotic cell death and proinflammatory interleukin-1β (IL-1β) and IL-18 secretion when exposed to OMVs. We propose that in order to activate caspase-11 in vivo, GBPs control the processing of bacterium-derived OMVs by macrophages as well as the processing of circulating free LPS by as-yet-undetermined cell types. IMPORTANCE The bacterial cell wall component LPS is a strong inducer of inflammation and is responsible for much of the toxicity of Gram-negative bacteria. Bacteria shed some of their cell wall and its associated LPS in the form of outer membrane vesicles (OMVs). Recent work demonstrated that secreted OMVs deliver LPS into the host cell cytosol by an unknown mechanism, resulting in the activation of the proinflammatory LPS sensor caspase-11. Here, we show that activation of cytosolic caspase-11 by OMVs requires additional host factors, the so-called guanylate binding proteins (GBPs). The discovery of GBPs as regulators of OMV-mediated inflammation paves the way toward a mechanistic understanding of the host response toward bacterial OMVs and may lead to effective strategies to ameliorate inflammation induced by bacterial infections. IMPORTANCE The bacterial cell wall component LPS is a strong inducer of inflammation and is responsible for much of the toxicity of Gram-negative bacteria. Bacteria shed some of their cell wall and its associated LPS in the form of outer membrane vesicles (OMVs). Recent work demonstrated that secreted OMVs deliver LPS into the host cell cytosol by an unknown mechanism, resulting in the activation of the proinflammatory LPS sensor caspase-11. Here, we show that activation of cytosolic caspase-11 by OMVs requires additional host factors, the so-called guanylate binding proteins (GBPs). The discovery of GBPs as regulators of OMV-mediated inflammation paves the way toward a mechanistic understanding of the host response toward bacterial OMVs and may lead to effective strategies to ameliorate inflammation induced by bacterial infections.

Analysis of teichoic acid biosynthesis regulation reveals that the extracytoplasmic function sigma factor σ M is induced by phosphate depletion in Bacillus subtilis W23

Microbiology ◽  
2005 ◽  
Vol 151 (9) ◽  
pp. 3041-3049 ◽  
Author(s):  
Kathrin Minnig ◽  
Vladimir Lazarevic ◽  
Blazenka Soldo ◽  
Catherine Mauël
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Teichoic Acid ◽  
Regulatory System ◽  
Phosphate Starvation ◽  
Phosphate Limitation ◽  
Wall Structure ◽  
Wall Teichoic Acid ◽  
Activity Data ◽  
Two Component

The expression of the Bacillus subtilis W23 tar genes specifying the biosynthesis of the major wall teichoic acid, the poly(ribitol phosphate), was studied under phosphate limitation using lacZ reporter fusions. Three different regulation patterns can be deduced from these β-galactosidase activity data: (i) tarD and tarL gene expression is downregulated under phosphate starvation; (ii) tarA and, to a minor extent, tarB expression after an initial decrease unexpectedly increases; and (iii) tarO is not influenced by phosphate concentration. To dissect the tarA regulatory pattern, its two promoters were analysed under phosphate limitation: The P tarA -ext promoter is repressed under phosphate starvation by the PhoPR two-component system, whereas, under the same conditions, the P tarA -int promoter is upregulated by the action of an extracytoplasmic function (ECF) σ factor, σ M. In contrast to strain 168, σ M is activated in strain W23 in phosphate-depleted conditions, a phenomenon indirectly dependent on PhoPR, the two-component regulatory system responsible for the adaptation to phosphate starvation. These results provide further evidence for the role of σ M in cell-wall stress response, and suggest that impairment of cell-wall structure is the signal activating this ECF σ factor.

scholarly journals Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis

Science ◽  
2013 ◽  
Vol 341 (6149) ◽  
pp. 1012-1016 ◽  
Author(s):  
Ben C. Chung ◽  
Jinshi Zhao ◽  
Robert A. Gillespie ◽  
Do-Yeon Kwon ◽  
Ziqiang Guan ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cell Wall ◽  
Bacterial Cell ◽  
Teichoic Acid ◽  
Bacterial Cell Wall ◽  
Structural Basis ◽  
Aquifex Aeolicus ◽  
Membrane Enzyme ◽  
Promising Target ◽  
Undecaprenyl Phosphate

MraY (phospho-MurNAc-pentapeptide translocase) is an integral membrane enzyme that catalyzes an essential step of bacterial cell wall biosynthesis: the transfer of the peptidoglycan precursor phospho-MurNAc-pentapeptide to the lipid carrier undecaprenyl phosphate. MraY has long been considered a promising target for the development of antibiotics, but the lack of a structure has hindered mechanistic understanding of this critical enzyme and the enzyme superfamily in general. The superfamily includes enzymes involved in bacterial lipopolysaccharide/teichoic acid formation and eukaryotic N-linked glycosylation, modifications that are central in many biological processes. We present the crystal structure of MraY from Aquifex aeolicus (MraYAA) at 3.3 Å resolution, which allows us to visualize the overall architecture, locate Mg2+ within the active site, and provide a structural basis of catalysis for this class of enzyme.

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