scholarly journals A Computational Evaluation of the Mechanism of Penicillin-Binding Protein-Catalyzed Cross-Linking of the Bacterial Cell Wall

2011 ◽  
Vol 133 (14) ◽  
pp. 5274-5283 ◽  
Author(s):  
Qicun Shi ◽  
Samy O. Meroueh ◽  
Jed F. Fisher ◽  
Shahriar Mobashery
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Binding Protein ◽  
Bacterial Cell Wall ◽  
Cross Linking ◽  
Penicillin Binding Protein ◽  
Computational Evaluation

Activation for Catalysis of Penicillin-Binding Protein 2a from Methicillin-ResistantStaphylococcusaureusby Bacterial Cell Wall

2005 ◽  
Vol 127 (7) ◽  
pp. 2056-2057 ◽  
Author(s):  
Cosimo Fuda ◽  
Dusan Hesek ◽  
Mijoon Lee ◽  
Ken-ichiro Morio ◽  
Thomas Nowak ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Binding Protein ◽  
Bacterial Cell Wall ◽  
Penicillin Binding Protein

scholarly journals Role of Penicillin-Binding Protein 2 (PBP2) in the Antibiotic Susceptibility and Cell Wall Cross-Linking of Staphylococcus aureus: Evidence for the Cooperative Functioning of PBP2, PBP4, and PBP2A

2005 ◽  
Vol 187 (5) ◽  
pp. 1815-1824 ◽  
Author(s):  
Tomasz A. Łęski ◽  
Alexander Tomasz
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Antimicrobial Agents ◽  
Binding Protein ◽  
Resistant Mutant ◽  
Site Directed Mutagenesis ◽  
Cross Linking ◽  
Penicillin Binding Protein ◽  
Beta Lactam ◽  
Experimental Proof

ABSTRACT Ceftizoxime, a beta-lactam antibiotic with high selective affinity for penicillin-binding protein 2 (PBP2) of Staphylococcus aureus, was used to select a spontaneous resistant mutant of S. aureus strain 27s. The stable resistant mutant ZOX3 had an increased ceftizoxime MIC and a decreased affinity of its PBP2 for ceftizoxime and produced peptidoglycan in which the proportion of highly cross-linked muropeptides was reduced. The pbpB gene of ZOX3 carried a single C-to-T nucleotide substitution at nucleotide 1373, causing replacement of a proline with a leucine at amino acid residue 458 of the transpeptidase domain of the protein, close to the SFN conserved motif. Experimental proof that this point mutation was responsible for the drug-resistant phenotype, and also for the decreased PBP2 affinity and reduced cell wall cross-linking, was provided by allelic replacement experiments and site-directed mutagenesis. Disruption of pbpD, the structural gene of PBP4, in either the parental strain or the mutant caused a large decrease in the highly cross-linked muropeptide components of the cell wall and in the mutant caused a massive accumulation of muropeptide monomers as well. Disruption of pbpD also caused increased sensitivity to ceftizoxime in both the parental cells and the ZOX3 mutant, while introduction of the plasmid-borne mecA gene, the genetic determinant of the beta-lactam resistance protein PBP2A, had the opposite effects. The findings provide evidence for the cooperative functioning of two native S. aureus transpeptidases (PBP2 and PBP4) and an acquired transpeptidase (PBP2A) in staphylococcal cell wall biosynthesis and susceptibility to antimicrobial agents.

An interaction between lysozyme and penicillin

1967 ◽  
Vol 167 (1009) ◽  
pp. 439-440 ◽  
Keyword(s):  
Cell Wall ◽  
Recent Work ◽  
Bacterial Cell ◽  
Structural Similarity ◽  
Antibiotic Activity ◽  
Bacterial Cell Wall ◽  
Cross Linking ◽  
Cell Wall Synthesis ◽  
Knowing That ◽  
Reactive Groups

Collins & Richmond (1962) have drawn attention to the close structural similarity between the reactive groups of penicillin and the reactive groups of N -acetylmuramic acid and, knowing that penicillin interferes with the synthesis of the bacterial cell wall, they have suggested that the antibiotic activity might possibly be explained in terms of a confusion between these two molecules by the cell wall synthesizing enzymes. Although recent work (Anderson, Matsukashi, Haskin & Strominger 1965; Wise & Park 1965; Tipper & Strominger 1965) has shown that penicillin appears to act by blocking the peptide cross-linking stage of bacterial cell wall synthesis rather than the polysaccharide polymerization stage, we wondered if lysozyme might bind penicillin purely on the basis of its structural similarity to N -acetylmuramic acid, a molecule for which lysozyme must have a specificity since it is part of the substrate of lysozyme.

scholarly journals The importance of being cross-linked for the bacterial cell wall

2019 ◽  
Author(s):  
Garima Rani ◽  
Issan Patri
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Turgor Pressure ◽  
Length Distribution ◽  
Peptide Bond ◽  
Vital Role ◽  
Bacterial Cell Wall ◽  
Cross Linking ◽  
Strand Length

AbstractThe bacterial cell wall is primarily composed of a mesh of stiff glycan strands cross-linked by peptide bridges and is essential for safeguarding the cell. The structure of the cell wall has to be stiff enough to bear the high turgor pressure and sufficiently tough to ensure protection against failure. Here we explore the role of various design features of the cell in enhancing the toughness of the cell wall. We explain how the glycan strand length distribution and the degree of cross-linking can play a vital role in ensuring that the cell wall offers sufficient resistance to propagation of cracks. We suggest a possible mechanism by which peptide bond hydrolysis can also help mitigate this risk of failure. We also study the reinforcing effect of MreB on the cell wall and conclude that the cross-linked structure of the cell wall plays the more important role in safeguarding against mechanical failure due to cracking.

scholarly journals Unipolar Peptidoglycan Synthesis in the Rhizobiales Requires an Essential Class A Penicillin-Binding Protein

mBio ◽  
2021 ◽  
Author(s):  
Michelle A. Williams ◽  
Alena Aliashkevich ◽  
Elizaveta Krol ◽  
Erkin Kuru ◽  
Jacob M. Bouchier ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Structure And Function ◽  
Bacterial Cell Wall ◽  
Cell Wall Biosynthesis ◽  
Growth Strategies ◽  
Penicillin Binding Protein ◽  
Class A ◽  
Peptidoglycan Synthesis ◽  
And Function

While the structure and function of the bacterial cell wall are well conserved, the mechanisms responsible for cell wall biosynthesis during elongation are variable. It is increasingly clear that rod-shaped bacteria use a diverse array of growth strategies with distinct spatial zones of cell wall biosynthesis, including lateral elongation, unipolar growth, bipolar elongation, and medial elongation.

scholarly journals The Monofunctional Glycosyltransferase of Escherichia coli Localizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN

2007 ◽  
Vol 190 (5) ◽  
pp. 1831-1834 ◽  
Author(s):  
Adeline Derouaux ◽  
Benoît Wolf ◽  
Claudine Fraipont ◽  
Eefjan Breukink ◽  
Martine Nguyen-Distèche ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Cycle ◽  
Cell Wall ◽  
Cell Division ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Chain Elongation ◽  
Penicillin Binding Protein ◽  
Division Site ◽  
Glycan Chain

ABSTRACT The monofunctional peptidoglycan glycosyltransferase (MtgA) catalyzes glycan chain elongation of the bacterial cell wall. Here we show that MtgA localizes at the division site of Escherichia coli cells that are deficient in PBP1b and produce a thermosensitive PBP1a and is able to interact with three constituents of the divisome, PBP3, FtsW, and FtsN, suggesting that MtgA may play a role in peptidoglycan assembly during the cell cycle in collaboration with other proteins.

Allostery, Recognition of Nascent Peptidoglycan, and Cross-linking of the Cell Wall by the Essential Penicillin-Binding Protein 2x of Streptococcus pneumoniae

2018 ◽  
Vol 13 (3) ◽  
pp. 694-702 ◽  
Author(s):  
Noelia Bernardo-García ◽  
Kiran V. Mahasenan ◽  
María T. Batuecas ◽  
Mijoon Lee ◽  
Dusan Hesek ◽  
...  
Keyword(s):  
Cell Wall ◽  
Streptococcus Pneumoniae ◽  
Binding Protein ◽  
Cross Linking ◽  
Penicillin Binding Protein
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