scholarly journals Structural Basis of the Inhibition of Class A β-Lactamases and Penicillin-Binding Proteins by 6-β-Iodopenicillanate

2009 ◽  
Vol 131 (42) ◽  
pp. 15262-15269 ◽  
Author(s):  
Eric Sauvage ◽  
Astrid Zervosen ◽  
Georges Dive ◽  
Raphael Herman ◽  
Ana Amoroso ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Structural Basis ◽  
Penicillin Binding Proteins ◽  
Class A

scholarly journals Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin binding proteins

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Victor M Hernández-Rocamora ◽  
Natalia Baranova ◽  
Katharina Peters ◽  
Eefjan Breukink ◽  
Martin Loose ◽  
...  
Keyword(s):  
Real Time ◽  
Lipid Bilayers ◽  
High Throughput Screening ◽  
Binding Proteins ◽  
Cell Envelope ◽  
Penicillin Binding Proteins ◽  
Peptidoglycan Biosynthesis ◽  
Class A ◽  
Peptidoglycan Synthesis ◽  
Osmotic Lysis

Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin binding proteins are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here we developed a novel FRET-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and we applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high throughput screening for new antimicrobials.

scholarly journals The Importance of a Critical Protonation State and the Fate of the Catalytic Steps in Class A β-Lactamases and Penicillin-binding Proteins

2004 ◽  
Vol 279 (33) ◽  
pp. 34665-34673 ◽  
Author(s):  
Dasantila Golemi-Kotra ◽  
Samy O. Meroueh ◽  
Choonkeun Kim ◽  
Sergei B. Vakulenko ◽  
Alexey Bulychev ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Protonation State ◽  
Penicillin Binding Proteins ◽  
Class A

scholarly journals Author response: Class-A penicillin binding proteins do not contribute to cell shape but repair cell-wall defects

2020 ◽  
Author(s):  
Antoine Vigouroux ◽  
Baptiste Cordier ◽  
Andrey Aristov ◽  
Laura Alvarez ◽  
Gizem Özbaykal ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Shape ◽  
Binding Proteins ◽  
Author Response ◽  
Response Class ◽  
Penicillin Binding Proteins ◽  
Class A

scholarly journals Dual multimodular class A penicillin-binding proteins in Mycobacterium leprae.

1997 ◽  
Vol 179 (14) ◽  
pp. 4627-4630 ◽  
Author(s):  
S Lepage ◽  
P Dubois ◽  
T K Ghosh ◽  
B Joris ◽  
S Mahapatra ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Mycobacterium Leprae ◽  
Penicillin Binding Proteins ◽  
Class A

scholarly journals The ponA Gene of Enterococcus faecalis JH2-2 Codes for a Low-Affinity Class A Penicillin-Binding Protein

2004 ◽  
Vol 186 (13) ◽  
pp. 4412-4416 ◽  
Author(s):  
Colette Duez ◽  
Séverine Hallut ◽  
Noureddine Rhazi ◽  
Séverine Hubert ◽  
Ana Amoroso ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Enterococcus Faecalis ◽  
Binding Proteins ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Penicillin Binding Proteins ◽  
Class A ◽  
Lipid Ii

ABSTRACT A soluble derivative of the Enterococcus faecalis JH2-2 class A PBP1 (*PBP1) was overproduced and purified. It exhibited a glycosyltransferase activity on the Escherichia coli 14C-labeled lipid II precursor. As a dd- peptidase, it could hydrolyze thiolester substrates with efficiencies similar to those of other class A penicillin-binding proteins (PBPs) and bind β-lactams, but with k 2/K (a parameter accounting for the acylation step efficiency) values characteristic of penicillin-resistant PBPs.

scholarly journals Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin binding proteins

2020 ◽  
Author(s):  
Víctor M. Hernández-Rocamora ◽  
Natalia Baranova ◽  
Katharina Peters ◽  
Eefjan Breukink ◽  
Martin Loose ◽  
...  
Keyword(s):  
Real Time ◽  
Lipid Bilayers ◽  
High Throughput Screening ◽  
Binding Proteins ◽  
Cell Envelope ◽  
Penicillin Binding Proteins ◽  
Peptidoglycan Biosynthesis ◽  
Class A ◽  
Peptidoglycan Synthesis ◽  
Osmotic Lysis

ABSTRACTPeptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin binding proteins are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here we developed a novel FRET-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and we demonstrate this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay allows unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high throughput screening for new antimicrobials.

scholarly journals Class-A penicillin binding proteins do not contribute to cell shape but repair cell-wall defects

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Antoine Vigouroux ◽  
Baptiste Cordier ◽  
Andrey Aristov ◽  
Laura Alvarez ◽  
Gizem Özbaykal ◽  
...  
Keyword(s):  
Cell Wall ◽  
Single Molecule ◽  
Cell Shape ◽  
Binding Proteins ◽  
Mechanical Stability ◽  
Cell Envelope ◽  
Cylindrical Part ◽  
Penicillin Binding Proteins ◽  
Class A ◽  
Wall Stiffness

Cell shape and cell-envelope integrity of bacteria are determined by the peptidoglycan cell wall. In rod-shaped Escherichia coli, two conserved sets of machinery are essential for cell-wall insertion in the cylindrical part of the cell: the Rod complex and the class-A penicillin-binding proteins (aPBPs). While the Rod complex governs rod-like cell shape, aPBP function is less well understood. aPBPs were previously hypothesized to either work in concert with the Rod complex or to independently repair cell-wall defects. First, we demonstrate through modulation of enzyme levels that aPBPs do not contribute to rod-like cell shape but are required for mechanical stability, supporting their independent activity. By combining measurements of cell-wall stiffness, cell-wall insertion, and PBP1b motion at the single-molecule level, we then present evidence that PBP1b, the major aPBP, contributes to cell-wall integrity by repairing cell wall defects.

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