References of "Amoroso, Ana Maria"
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See detailStudy of the regulation of β-lactam resistance in Enterococcus hirae
Raymackers, Alice ULiege; Maréchal, Maxime; Verlaine, Olivier ULiege et al

Poster (2017, June 13)

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See detailStudy of the regulation of the operon ftsW-psr-pbp5 in Enterococcus hirae
Raymackers, Alice ULiege; Maréchal, Maxime; Verlaine, Olivier ULiege et al

Poster (2017, May 11)

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See detailStructure-Activity Relationships of Novel Tryptamine-Based Inhibitors of Bacterial Transglycosylase.
Sosic, Izidor; Anderluh, Marko; Sova, Matej et al

in Journal of medicinal chemistry (2015)

Penicillin-binding proteins represent well-established, validated, and still very promising targets for the design and development of new antibacterial agents. The transglycosylase domain of penicillin ... [more ▼]

Penicillin-binding proteins represent well-established, validated, and still very promising targets for the design and development of new antibacterial agents. The transglycosylase domain of penicillin-binding proteins is especially important, as it catalyzes polymerization of glycan chains, using the peptidoglycan precursor lipid II as a substrate. On the basis of the previous discovery of a noncovalent small-molecule inhibitor of transglycosylase activity, we systematically explored the structure-activity relationships of these tryptamine-based inhibitors. The main aim was to reduce the nonspecific cytotoxic properties of the initial hit compound and concurrently to retain the mode of its inhibition. A focused library of tryptamine-based compounds was synthesized, characterized, and evaluated biochemically. The results presented here show the successful reduction of the nonspecific cytotoxicity, and the retention of the inhibition of transglycosylase enzymatic activity, as well as the ability of these compounds to bind to lipid II and to have antibacterial actions. [less ▲]

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See detailFate of the coactivator in the induction of BlaP β-lactamase in Bacillus licheniformis 749/I
Dauvin, Marjorie ULiege; Amoroso, Ana Maria ULiege; Joris, Bernard ULiege

Poster (2015, June 23)

In bacteria, the production of a β-lactamase, an hydrolase specific to β-lactam antibiotics, may be constitutive or inducible. In Bacillus licheniformis 749/I the presence of a β-lactam in the external ... [more ▼]

In bacteria, the production of a β-lactamase, an hydrolase specific to β-lactam antibiotics, may be constitutive or inducible. In Bacillus licheniformis 749/I the presence of a β-lactam in the external media is detected by a protein relay producing an intracellular signal which leads to the induction of BlaP β-lactamase expression. The blaP gene is included in a divergeon along with blaI, coding for a cytoplasmic repressor, and blaR1, coding for a penicillin membrane receptor. Both, the acylation of the extracellular domain of BlaR1 by a β-lactam together with cellular stress due to the presence of the antibiotic outside the cell generate a dipeptide (coactivator) resulting from the peptidoglycan turnover that destabilizes BlaI repressor-DNA complex, leading to the expression of β-lactam resistance. [less ▲]

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See detailModeling β-lactamase induction in Bacillus licheniformis 749/I
Dauvin, Marjorie ULiege; Vandamme, François; Abujahrur, Nora et al

Poster (2015, May 13)

The intensive use of antibiotics in infectious diseases treatment has result in selection of resistance mechanisms among bacteria. The main one is the production of a β-lactamase that hydrolyzes the β ... [more ▼]

The intensive use of antibiotics in infectious diseases treatment has result in selection of resistance mechanisms among bacteria. The main one is the production of a β-lactamase that hydrolyzes the β-lactam ring of β-lactamines. β-lactamase could be expressed constitutively or in response to the presence of β-lactam antibiotic outside the cell. From the four β-lactamase induction mechanisms known so far, the ones from Gram positive S. aureus and B. licheniformis 749/i are very closed. Its induction system includes the divergeon blaP-blaI-blaR1 and an unrelated blaR2 gene still not identified. Recent results from our lab indicate that for the induction of β-lactamase two conditions must be fulfilled. The first one is a cellular stress due to the presence of the antibiotic outside, acylating PBP1, which triggers an increase of cell wall degradation. The second one is the acylation of the membrane receptor BlaR1 by the antibiotic, which results in the derepression of the β-lactamase gene blaP by the repressor BlaI. Amoroso et al. had showed that a fragment coming from peptidoglycan degradation interact with BlaI. In the same study, they propose that this fragment would be the result of the activity of proteins encoded by ykf operon. The aim of this project is the modeling of the β–lactamase induction mechanism in B. licheniformis 749/I. [less ▲]

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See detail5′-Methylene-triazole-substituted-aminoribosyl uridines as MraY inhibitors: synthesis, biological evaluation and molecular modeling
Fer, Michael; Bouhss,, Ahmed B; Patrão, Mariana et al

in Organic & Biomolecular Chemistry (2015), 13(26), 7193

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See detailStreptococcus pneumoniae GAPDH Is Released by Cell Lysis and Interacts with Peptidoglycan.
Terrasse, Remi; Amoroso, Ana Maria ULiege; Vernet, Thierry et al

in PloS one (2015), 10(4), 0125377

Release of conserved cytoplasmic proteins is widely spread among Gram-positive and Gram-negative bacteria. Because these proteins display additional functions when located at the bacterial surface, they ... [more ▼]

Release of conserved cytoplasmic proteins is widely spread among Gram-positive and Gram-negative bacteria. Because these proteins display additional functions when located at the bacterial surface, they have been qualified as moonlighting proteins. The GAPDH is a glycolytic enzyme which plays an important role in the virulence processes of pathogenic microorganisms like bacterial invasion and host immune system modulation. However, GAPDH, like other moonlighting proteins, cannot be secreted through active secretion systems since they do not contain an N-terminal predicted signal peptide. In this work, we investigated the mechanism of GAPDH export and surface retention in Streptococcus pneumoniae, a major human pathogen. We addressed the role of the major autolysin LytA in the delivery process of GAPDH to the cell surface. Pneumococcal lysis is abolished in the DeltalytA mutant strain or when 1% choline chloride is added in the culture media. We showed that these conditions induce a marked reduction in the amount of surface-associated GAPDH. These data suggest that the presence of GAPDH at the surface of pneumococcal cells depends on the LytA-mediated lysis of a fraction of the cell population. Moreover, we demonstrated that pneumococcal GAPDH binds to the bacterial cell wall independently of the presence of the teichoic acids component, supporting peptidoglycan as a ligand to surface GAPDH. Finally, we showed that peptidoglycan-associated GAPDH recruits C1q from human serum but does not activate the complement pathway. [less ▲]

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See detailHuman L-ficolin recognizes phosphocholine moieties of pneumococcal teichoic acid.
Vassal-Stermann, Emilie; Lacroix, Monique; Gout, Evelyne et al

in Journal of immunology (Baltimore, Md. : 1950) (2014), 193(11), 5699-708

Human L-ficolin is a soluble protein of the innate immune system able to sense pathogens through its fibrinogen (FBG) recognition domains and to trigger activation of the lectin complement pathway through ... [more ▼]

Human L-ficolin is a soluble protein of the innate immune system able to sense pathogens through its fibrinogen (FBG) recognition domains and to trigger activation of the lectin complement pathway through associated serine proteases. L-Ficolin has been previously shown to recognize pneumococcal clinical isolates, but its ligands and especially its molecular specificity remain to be identified. Using solid-phase binding assays, serum and recombinant L-ficolins were shown to interact with serotype 2 pneumococcal strain D39 and its unencapsulated R6 derivative. Incubation of both strains with serum triggered complement activation, as measured by C4b and C3b deposition, which was decreased by using ficolin-depleted serum. Recombinant L-ficolin and its FBG-like recognition domain bound to isolated pneumococcal cell wall extracts, whereas binding to cell walls depleted of teichoic acid (TA) was decreased. Both proteins were also shown to interact with two synthetic TA compounds, each comprising part structures of the complete lipoteichoic acid molecule with two PCho residues. Competition studies and direct interaction measurements by surface plasmon resonance identified PCho as a novel L-ficolin ligand. Structural analysis of complexes of the FBG domain of L-ficolin and PCho revealed that the phosphate moiety interacts with amino acids previously shown to define an acetyl binding site. Consequently, binding of L-ficolin to immobilized acetylated BSA was inhibited by PCho and synthetic TA. Binding of serum L-ficolin to immobilized synthetic TA and PCho-conjugated BSA triggered activation of the lectin complement pathway, thus further supporting the hypothesis of L-ficolin involvement in host antipneumococcal defense. [less ▲]

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See detailActivity of ceftaroline against Enterococcus faecium PBP5.
Henry, Xavier; Verlaine, Olivier ULiege; Amoroso, Ana Maria ULiege et al

in Antimicrobial Agents and Chemotherapy (2013), 57(12), 6358

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See detailModeling β-lactamase induction in Bacillus licheniformis
Dauvin, Marjorie ULiege; Amoroso, Ana Maria ULiege; Joris, Bernard ULiege

Poster (2013, April 18)

The intensive use of antibiotics in infectious diseases treatment has result in selection of resistance mechanisms among bacteria. The main one is the production of a β-lactamase that hydrolyzes the β ... [more ▼]

The intensive use of antibiotics in infectious diseases treatment has result in selection of resistance mechanisms among bacteria. The main one is the production of a β-lactamase that hydrolyzes the β-lactam core of β-lactamines. β-lactamase could be expressed constitutively or in response to the presence of β-lactam antibiotic outside the cell. From the four β-lactamase induction mechanisms known so far, the ones from Gram positive S. aureus and B. licheniformis 749/i are very closed. Its induction system includes the divergeon blaP-blaI-blaR1 and an unrelated blaR2 gene still not identified. Recent results from our lab indicate that for the induction of β-lactamase two conditions must be fulfilled. The first one is a cellular stress due to the presence of the antibiotic outside, acylating PBP1, which triggers an increase of cell wall degradation. The second one is the acylation of the membrane receptor BlaR1 by the antibiotic, which results in the derepression of the β-lactamase gene blaP by the repressor BlaI. Amoroso et al. had showed that a fragment coming from peptidoglycan degradation interact with BlaI. In the same study, they propose that this fragment would be the result of the activity of proteins encoded by ykf operon. The aim of this project is the modeling of the β–lactamase induction mechanism in B. licheniformis. [less ▲]

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See detailSynthesis and evaluation of boronic acids as inhibitors of Penicillin Binding Proteins of classes A, B and C
Zervosen, Astrid ULiege; Sauvage, Eric ULiege; Bouillez, André ULiege et al

Poster (2012, April 18)

The widespread use of beta-lactam antibiotics has lead to the worldwide appearance of drug-resistant strains. Bacteria have developed resistance to beta-lactams by three main mechanisms: the production of ... [more ▼]

The widespread use of beta-lactam antibiotics has lead to the worldwide appearance of drug-resistant strains. Bacteria have developed resistance to beta-lactams by three main mechanisms: the production of beta-lactamases that catalyze hydrolysis of beta-lactams, the production of low-affinity, drug resistant Penicillin Binding Proteins (PBPs) and the over expression of resistant PBPs. PBPs are interesting targets because they catalyse the last steps of the biosynthesis of peptidoglycan, which is unique in bacteria and has no mammalian analogs, outside the cytoplasmic membrane. Various non-ß-lactam inhibitors of PBPs have been developed with the objective of attempting to stall the development of ß-lactam resistance. Boronic acids are potent beta-lactamase inhibitors and have been shown to display some specificity for soluble transpeptidases and PBPs, but their potential as inhibitors of the latter enzymes is yet to be widely explored. Recently, a (2, 6-dimethoxybenzamido)methylboronic acid was identified as being a potent inhibitor of Actinomadura sp. R39 transpeptidase (IC50: 1.3 µM). Here, we will discuss the synthesis of a number of acylaminomethylboronic acids, analogs of (2, 6-dimethoxybenzamido)methylboronic acid, and their potential as inhibitors of PBPs. Several boronic acids of this library were able to inhibit PBPs of classes A, B and C from penicillin sensitive strains. Thus (2-nitrobenzamido)methylboronic acid was identified as a good inhibitor of class A PBP (PBP1b from S. pneumoniae, IC50 = 26 µM), class B PBP (PBP2xR6 from S. pneumoniae, IC50 = 138 µM) and class C PBP (R39 from Actinomadura sp., IC50 = 0.6 µM). Crystal structures of complexes of R39 and PBP1b with boronic acid analogs of our library have already been solved and allowed an interpretation of results. We believe that this work opens new avenues towards the development of molecules that will inhibit PBPs, and eventually display bactericidal effect, on distinct bacterial species. [less ▲]

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See detailExploration of the chemical space of novel naphthalene-sulfonamide and anthranilic acid-based inhibitors of penicillin-binding Proteins
Sosic, Izidor; Turk, Samo; Sinreih, Masa et al

in Acta Chimica Slovenica (2012), 59(2), 380-388

Penicillin-binding proteins are a well established, validated and still a very promising target for the design and development of new antibacterial agents. Based on our previous discovery of several ... [more ▼]

Penicillin-binding proteins are a well established, validated and still a very promising target for the design and development of new antibacterial agents. Based on our previous discovery of several noncovalent small-molecule inhibitor hits for resistant PBPs we decided to additionally explore the chemical space around these compounds. In order to clarify their structure-activity relationships for PBP inhibition two new series of compounds were synthesized, characterized and evaluated biochemically: the derivatives of anthranilic acid and naphthalene-sulfonamide derivatives. The target compounds were tested for their inhibitory activities on three different transpeptidases: PBP2a from methicillin-resistant Staphylococcus aureus (MRSA) strains, PBP5fm from Enterococcus faecium strains, and PBP1b from Streptococcus pneumoniae strains. The most promising results for both of these series of compounds were obtained against the PBP2a enzyme with the IC50 values in the micromolar range. Although these results do not represent a significant breakthrough in the field of noncovalent PBP inhibitors, they do provide useful structure-activity relationship data, and thus a more solid basis for the design of potent and noncovalent inhibitors of resistant PBPs. [less ▲]

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See detailSynthesis and evaluation of boronic acids as inhibitors of Penicillin Binding Proteins of classes A, B and C.
Zervosen, Astrid ULiege; Bouillez, André ULiege; Herman, Alexandre et al

in Bioorganic & Medicinal Chemistry (2012), 20(12), 3915-24

In response to the widespread use of beta-lactam antibiotics bacteria have evolved drug resistance mechanisms that include the production of resistant Penicillin Binding Proteins (PBPs). Boronic acids are ... [more ▼]

In response to the widespread use of beta-lactam antibiotics bacteria have evolved drug resistance mechanisms that include the production of resistant Penicillin Binding Proteins (PBPs). Boronic acids are potent beta-lactamase inhibitors and have been shown to display some specificity for soluble transpeptidases and PBPs, but their potential as inhibitors of the latter enzymes is yet to be widely explored. Recently, a (2,6-dimethoxybenzamido)methylboronic acid was identified as being a potent inhibitor of Actinomadura sp. R39 transpeptidase (IC(50): 1.3muM). In this work, we synthesized and studied the potential of a number of acylaminomethylboronic acids as inhibitors of PBPs from different classes. Several derivatives inhibited PBPs of classes A, B and C from penicillin sensitive strains. The (2-nitrobenzamido)methylboronic acid was identified as a good inhibitor of a class A PBP (PBP1b from Streptococcus pneumoniae, IC(50)=26muM), a class B PBP (PBP2xR6 from Streptococcus pneumoniae, IC(50)=138muM) and a class C PBP (R39 from Actinomadura sp., IC(50)=0.6muM). This work opens new avenues towards the development of molecules that inhibit PBPs, and eventually display bactericidal effects, on distinct bacterial species. [less ▲]

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See detailA peptidoglycan fragment triggers beta-lactam resistance in Bacillus licheniformis.
Amoroso, Ana Maria ULiege; Boudet, Julien; Berzigotti, Stephanie et al

in PLoS Pathogens (2012), 8(3), 1002571

To resist to beta-lactam antibiotics Eubacteria either constitutively synthesize a beta-lactamase or a low affinity penicillin-binding protein target, or induce its synthesis in response to the presence ... [more ▼]

To resist to beta-lactam antibiotics Eubacteria either constitutively synthesize a beta-lactamase or a low affinity penicillin-binding protein target, or induce its synthesis in response to the presence of antibiotic outside the cell. In Bacillus licheniformis and Staphylococcus aureus, a membrane-bound penicillin receptor (BlaR/MecR) detects the presence of beta-lactam and launches a cytoplasmic signal leading to the inactivation of BlaI/MecI repressor, and the synthesis of a beta-lactamase or a low affinity target. We identified a dipeptide, resulting from the peptidoglycan turnover and present in bacterial cytoplasm, which is able to directly bind to the BlaI/MecI repressor and to destabilize the BlaI/MecI-DNA complex. We propose a general model, in which the acylation of BlaR/MecR receptor and the cellular stress induced by the antibiotic, are both necessary to generate a cell wall-derived coactivator responsible for the expression of an inducible beta-lactam-resistance factor. The new model proposed confirms and emphasizes the role of peptidoglycan degradation fragments in bacterial cell regulation. [less ▲]

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See detailSecond-generation sulfonamide inhibitors of D-glutamic acid-adding enzyme: activity optimisation with conformationally rigid analogues of D-glutamic acid.
Sosic, Izidor; Barreteau, Helene; Simcic, Mihael et al

in European journal of medicinal chemistry (2011), 46(7), 2880-94

D-Glutamic acid-adding enzyme (MurD) catalyses the essential addition of d-glutamic acid to the cytoplasmic peptidoglycan precursor UDP-N-acetylmuramoyl-l-alanine, and as such it represents an important ... [more ▼]

D-Glutamic acid-adding enzyme (MurD) catalyses the essential addition of d-glutamic acid to the cytoplasmic peptidoglycan precursor UDP-N-acetylmuramoyl-l-alanine, and as such it represents an important antibacterial drug-discovery target enzyme. Based on a series of naphthalene-N-sulfonyl-d-Glu derivatives synthesised recently, we synthesised two series of new, optimised sulfonamide inhibitors of MurD that incorporate rigidified mimetics of d-Glu. The compounds that contained either constrained d-Glu or related rigid d-Glu mimetics showed significantly better inhibitory activities than the parent compounds, thereby confirming the advantage of molecular rigidisation in the design of MurD inhibitors. The binding modes of the best inhibitors were examined with high-resolution NMR spectroscopy and X-ray crystallography. We have solved a new crystal structure of the complex of MurD with an inhibitor bearing a 4-aminocyclohexane-1,3-dicarboxyl moiety. These data provide an additional step towards the development of sulfonamide inhibitors with potential antibacterial activities. [less ▲]

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See detailSmall molecule inhibitors of peptidoglycan synthesis targeting the lipid II precursor.
Derouaux, Adeline ULiege; Turk, Samo; Olrichs, Nick K et al

in Biochemical Pharmacology (2011), 81(9), 1098-105

Bacterial peptidoglycan glycosyltransferases (GTs) of family 51 catalyze the polymerization of the lipid II precursor into linear peptidoglycan strands. This activity is essential to bacteria and ... [more ▼]

Bacterial peptidoglycan glycosyltransferases (GTs) of family 51 catalyze the polymerization of the lipid II precursor into linear peptidoglycan strands. This activity is essential to bacteria and represents a validated target for the development of new antibacterials. Application of structure-based virtual screening to the National Cancer Institute library using eHits program and the structure of the glycosyltransferase domain of the Staphylococcus aureus penicillin-binding protein 2 resulted in the identification of two small molecules analogues 5, a 2-[1-[(2-chlorophenyl)methyl]-2-methyl-5-methylsulfanylindol-3-yl]ethanamine and 5b, a 2-[1-[(3,4-dichlorophenyl)methyl]-2-methyl-5-methylsulfanylindol-3-yl]ethanamine that exhibit antibacterial activity against several Gram-positive bacteria but were less active on Gram-negative bacteria. The two compounds inhibit the activity of five GTs in the micromolar range. Investigation of the mechanism of action shows that the compounds specifically target peptidoglycan synthesis. Unexpectedly, despite the fact that the compounds were predicted to bind to the GT active site, compound 5b was found to interact with the lipid II substrate via the pyrophosphate motif. In addition, this compound showed a negatively charged phospholipid-dependent membrane depolarization and disruption activity. These small molecules are promising leads for the development of more active and specific compounds to target the essential GT step in cell wall synthesis. [less ▲]

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See detailStructure-Guided Design of Cell Wall Biosynthesis Inhibitors That Overcome beta-Lactam Resistance in Staphylococcus aureus (MRSA).
Contreras-Martel, Carlos; Amoroso, Ana Maria ULiege; Woon, Esther C.Y. et al

in ACS Chemical Biology (2011)

beta-Lactam antibiotics have long been a treatment of choice for bacterial infections since they bind irreversibly to Penicillin-Binding Proteins (PBPs), enzymes that are vital for cell wall biosynthesis ... [more ▼]

beta-Lactam antibiotics have long been a treatment of choice for bacterial infections since they bind irreversibly to Penicillin-Binding Proteins (PBPs), enzymes that are vital for cell wall biosynthesis. Many pathogens express drug-insensitive PBPs rendering beta-lactams ineffective, revealing a need for new types of PBP inhibitors active against resistant strains. We have identified alkyl boronic acids that are active against pathogens including methicillin-resistant S. aureus (MRSA). The crystal structures of PBP1b complexed to 11 different alkyl boronates demonstrate that in vivo efficacy correlates with the mode of inhibitor side chain binding. Staphylococcal membrane analyses reveal that the most potent alkyl boronate targets PBP1, an autolysis system regulator, and PBP2a, a low beta-lactam affinity enzyme. This work demonstrates the potential of boronate-based PBP inhibitors for circumventing beta-lactam resistance and opens avenues for the development of novel antibiotics that target Gram-positive pathogens. [less ▲]

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See detailNew noncovalent inhibitors of penicillin-binding proteins from penicillin-resistant bacteria.
Turk, Samo; Verlaine, Olivier ULiege; Gerards, Thomas ULiege et al

in PloS one (2011), 6(5), 19418

BACKGROUND: Penicillin-binding proteins (PBPs) are well known and validated targets for antibacterial therapy. The most important clinically used inhibitors of PBPs beta-lactams inhibit transpeptidase ... [more ▼]

BACKGROUND: Penicillin-binding proteins (PBPs) are well known and validated targets for antibacterial therapy. The most important clinically used inhibitors of PBPs beta-lactams inhibit transpeptidase activity of PBPs by forming a covalent penicilloyl-enzyme complex that blocks the normal transpeptidation reaction; this finally results in bacterial death. In some resistant bacteria the resistance is acquired by active-site distortion of PBPs, which lowers their acylation efficiency for beta-lactams. To address this problem we focused our attention to discovery of novel noncovalent inhibitors of PBPs. METHODOLOGY/PRINCIPAL FINDINGS: Our in-house bank of compounds was screened for inhibition of three PBPs from resistant bacteria: PBP2a from Methicillin-resistant Staphylococcus aureus (MRSA), PBP2x from Streptococcus pneumoniae strain 5204, and PBP5fm from Enterococcus faecium strain D63r. Initial hit inhibitor obtained by screening was then used as a starting point for computational similarity searching for structurally related compounds and several new noncovalent inhibitors were discovered. Two compounds had promising inhibitory activities of both PBP2a and PBP2x 5204, and good in-vitro antibacterial activities against a panel of Gram-positive bacterial strains. CONCLUSIONS: We found new noncovalent inhibitors of PBPs which represent important starting points for development of more potent inhibitors of PBPs that can target penicillin-resistant bacteria. [less ▲]

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See detailInteraction of ceftobiprole with the low-affinity PBP 5 of Enterococcus faecium
Henry, X.; Amoroso, Ana Maria ULiege; Coyette, Jacques ULiege et al

in Antimicrobial Agents and Chemotherapy (2010), 54

Detailed reference viewed: 29 (6 ULiège)