Synthetic Peptidoglycan Substrates for Penicillin-Binding Protein 5 of Gram-Negative Bacteria

2004 ◽  
Vol 69 (3) ◽  
pp. 778-784 ◽  
Author(s):  
Dusan Hesek ◽  
Maxim Suvorov ◽  
Ken-ichiro Morio ◽  
Mijoon Lee ◽  
Stephen Brown ◽  
...  
Keyword(s):  
Binding Protein ◽  
Gram Negative Bacteria ◽  
Penicillin Binding Protein ◽  
Gram Negative

scholarly journals Low-Molecular-Mass Penicillin Binding Protein 6b (DacD) Is Required for Efficient GOB-18 Metallo-β-Lactamase Biogenesis in Salmonella enterica and Escherichia coli

2013 ◽  
Vol 58 (1) ◽  
pp. 205-211 ◽  
Author(s):  
Luciano Brambilla ◽  
Jorgelina Morán-Barrio ◽  
Alejandro M. Viale
Keyword(s):  
Escherichia Coli ◽  
Molecular Mass ◽  
Salmonella Enterica ◽  
Metal Ion ◽  
Binding Protein ◽  
Gram Negative Bacteria ◽  
Penicillin Binding Protein ◽  
Biofilm Growth ◽  
Gram Negative ◽  
Content Type

ABSTRACTMetallo-β-lactamases (MBLs) are Zn2+-containing secretory enzymes of clinical relevance, whose final folding and metal ion assembly steps in Gram-negative bacteria occur after secretion of the apo form to the periplasmic space. In the search of periplasmic factors assisting MBL biogenesis, we found thatdacDnull (ΔdacD) mutants ofSalmonella entericaandEscherichia coliexpressing the pre-GOB-18 MBL gene from plasmids showed significantly reduced resistance to cefotaxime and concomitant lower accumulation of GOB-18 in the periplasm. This reduced accumulation of GOB-18 resulted from increased accessibility to proteolytic attack in the periplasm, suggesting that the lack of DacD negatively affects the stability of secreted apo MBL forms. Moreover, ΔdacDmutants ofS. entericaandE. colishowed an altered ability to develop biofilm growth. DacD is a widely distributed low-molecular-mass (LMM) penicillin binding protein (PBP6b) endowed with lowdd-carboxypeptidase activity whose functions are still obscure. Our results indicate roles for DacD in assisting biogenesis of particular secretory macromolecules in Gram-negative bacteria and represent to our knowledge the first reported phenotypes for bacterial mutants lacking this LMM PBP.

scholarly journals Correction: Freischem et al. Interaction Mode of the Novel Monobactam AIC499 Targeting Penicillin Binding Protein 3 of Gram-Negative Bacteria. Biomolecules 2021, 11, 1057

Biomolecules ◽  
2021 ◽  
Vol 12 (1) ◽  
pp. 5
Author(s):  
Stefan Freischem ◽  
Immanuel Grimm ◽  
Arancha López-Pérez ◽  
Dieter Willbold ◽  
Burkhard Klenke ◽  
...  
Keyword(s):  
Binding Protein ◽  
Gram Negative Bacteria ◽  
The Novel ◽  
Penicillin Binding Protein ◽  
Gram Negative ◽  
Interaction Mode

In the original article [...]

scholarly journals Critical Role of Lipopolysaccharide-Binding Protein and CD14 in Immune Responses against Gram-Negative Bacteria

2001 ◽  
Vol 167 (5) ◽  
pp. 2759-2765 ◽  
Author(s):  
Didier Le Roy ◽  
Franco Di Padova ◽  
Yoshiyuki Adachi ◽  
Michel Pierre Glauser ◽  
Thierry Calandra ◽  
...  
Keyword(s):  
Immune Responses ◽  
Binding Protein ◽  
Critical Role ◽  
Gram Negative Bacteria ◽  
Lipopolysaccharide Binding Protein ◽  
Gram Negative ◽  
Lipopolysaccharide Binding

scholarly journals Phylogenomic insights into distribution and adaptation of Bdellovibrionota in marine waters

2020 ◽  
Author(s):  
Qing-Mei Li ◽  
Ying-Li Zhou ◽  
Zhan-Fei Wei ◽  
Yong Wang
Keyword(s):  
Comparative Genomics ◽  
Marine Environment ◽  
Deep Sea ◽  
Binding Protein ◽  
Glycerol Metabolism ◽  
Metabolic Reconstruction ◽  
Gram Negative Bacteria ◽  
Phylogenetic Groups ◽  
Gram Negative ◽  
Chitin Binding Protein

AbstractBdellovibrionota is composed of obligate predators that can consume some gram-negative bacteria inhabiting various environments. However, whether genomic traits influence their distribution and marine adaptation remains to be answered. In this study, we performed phylogenomics and comparative genomics studies on 82 Bdellovibrionota genomes along with five metagenome-assembled genomes (MAGs) from deep sea zones. Four phylogenetic groups, Oligoflexia, Bdello-group1, Bdello-group2 and Bacteriovoracia, were revealed by constructing a phylogenetic tree, of which 53.84% of Bdello-group2 and 48.94% of Bacteriovoracia were derived from ocean. Bacteriovoracia was more prevalent in deep sea zones, whereas Bdello-group2 was largely distributed in the epipelagic zone. Metabolic reconstruction indicated that genes involved in chemotaxis, flagellar (mobility), type II secretion system, ABC transporters and penicillin-binding protein were necessary for predatory lifestyle of Bdellovibrionota. Genes involved in glycerol metabolism, hydrogen peroxide (H2O2) degradation, cell wall recycling and peptide utilization were ubiquitously present in Bdellovibrionota genomes. Comparative genomics between marine and non-marine Bdellovibrionota demonstrated that betaine as an osmoprotectant is probably widely used by marine Bdellovibrionota, meanwhile, all the marine genomes have a number of related genes for adapting marine environment. The chitinase and chitin-binding protein encoding genes were identified for the first time in Oligoflexia, which implied that Oligoflexia may prey a wider spectrum of microbes. This study expanded our knowledge on adaption strategies of Bdellovibrionota inhabiting deep sea and their potential usage for biological control.ImportanceBdellovibrionota can prey gram-negative bacteria proposed as biocontrol agent. Available Bdellovibrionota genomes showed that most are from marine environment. However, vertical distribution and adaption of Bdellovibrionota in deep sea has not been reported. Our study of Bdellovibrionota revealed four groups (Oligoflexia, Bdello-group1, Bdello-group2 and Bacteriovoracia) and their distribution pattern in oceans. We also identified the genes for different phases of predation and adaptation in deep-sea environment. Moreover, Oligoflexia genomes contain more genes for carbohydrates utilization and particularly those encoding chitin-binding protein and chitinase. Our analyses of Bdellovibrionota genomes may help understand their special lifestyle and deep-sea adaptation.

scholarly journals LPS-binding protein protects mice from septic shock caused by LPS or gram-negative bacteria.

1998 ◽  
Vol 101 (10) ◽  
pp. 2065-2071 ◽  
Author(s):  
N Lamping ◽  
R Dettmer ◽  
N W Schröder ◽  
D Pfeil ◽  
W Hallatschek ◽  
...  
Keyword(s):  
Septic Shock ◽  
Binding Protein ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Lps Binding

scholarly journals In vitro evaluation of BO-3482, a novel dithiocarbamate carbapenem with activity against methicillin-resistant staphylococci.

1997 ◽  
Vol 41 (10) ◽  
pp. 2282-2285 ◽  
Author(s):  
Y Adachi ◽  
K Nakamura ◽  
Y Kato ◽  
N Hazumi ◽  
T Hashizume ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Clostridium Difficile ◽  
Proteus Mirabilis ◽  
Gram Negative Bacteria ◽  
Penicillin Binding Protein ◽  
Beta Lactam ◽  
Gram Negative ◽  
Methicillin Resistant ◽  
Beta Lactam Antibiotics

BO-3482, a dithiocarbamate carbapenem, inhibited clinical isolates of methicillin-resistant staphylococci (MRS) at 6.25 microg/ml (MIC at which 90% of isolates tested are inhibited [MIC90]), while the MIC90 of imipenem was > 100 microg/ml. BO-3482 was generally less active than imipenem against methicillin-susceptible Staphylococcus aureus, streptococci, enterococci, and gram-negative bacteria, although BO-3482 showed better activity (MIC90) than imipenem against Enterococcus faecium, Haemophilus influenzae, Proteus mirabilis, and Clostridium difficile. The affinities (50% inhibitory concentrations) of BO-3482 for penicillin-binding protein (PBP) PBP 2' of MRS and PBP 5 of E. faecium (both PBPs have low affinities for ordinary beta-lactam antibiotics) were 3.8 and 20 microg/ml, respectively, reflecting the greater activity of BO-3482 against MRS than against E. faecium.

scholarly journals A penicillin-binding protein inhibits selection of colistin-resistant, lipooligosaccharide-deficientAcinetobacter baumannii

2016 ◽  
Vol 113 (41) ◽  
pp. E6228-E6237 ◽  
Author(s):  
Joseph M. Boll ◽  
Alexander A. Crofts ◽  
Katharina Peters ◽  
Vincent Cattoir ◽  
Waldemar Vollmer ◽  
...  
Keyword(s):  
Cell Surface ◽  
Outer Membrane ◽  
Lipid A ◽  
Binding Protein ◽  
Resistance Mechanism ◽  
Multidrug Resistant ◽  
Penicillin Binding Protein ◽  
Gram Negative ◽  
Peptidoglycan Cell Wall ◽  
Selection Of

The Gram-negative bacterial outer membrane fortifies the cell against environmental toxins including antibiotics. Unique glycolipids called lipopolysaccharide/lipooligosaccharide (LPS/LOS) are enriched in the cell-surface monolayer of the outer membrane and promote antimicrobial resistance. Colistin, which targets the lipid A domain of LPS/LOS to lyse the cell, is the last-line treatment for multidrug-resistant Gram-negative infections. Lipid A is essential for the survival of most Gram-negative bacteria, but colistin-resistantAcinetobacter baumanniilacking lipid A were isolated after colistin exposure. Previously, strain ATCC 19606 was the onlyA. baumanniistrain demonstrated to subsist without lipid A. Here, we show that otherA. baumanniistrains can also survive without lipid A, but some cannot, affording a unique model to study endotoxin essentiality. We assessed the capacity of 15 clinicalA. baumanniiisolates including 9 recent clinical isolates to develop colistin resistance through inactivation of the lipid A biosynthetic pathway, the products of which assemble the LOS precursor. Our investigation determined that expression of the well-conserved penicillin-binding protein (PBP) 1A, prevented LOS-deficient colony isolation. The glycosyltransferase activity of PBP1A, which aids in the polymerization of the peptidoglycan cell wall, was lethal to LOS-deficientA. baumannii. Global transcriptomic analysis of a PBP1A-deficient mutant and four LOS-deficientA. baumanniistrains showed a concomitant increase in transcription of lipoproteins and their transporters. Examination of the LOS-deficientA. baumanniicell surface demonstrated that specific lipoproteins were overexpressed and decorated the cell surface, potentially compensating for LOS removal. This work expands our knowledge of lipid A essentiality and elucidates a drug resistance mechanism.

scholarly journals Present and future of siderophore-based therapeutic and diagnostic approaches in infectious diseases

2019 ◽  
Vol 11 (2) ◽  
Author(s):  
Gilda Tonziello ◽  
Emanuela Caraffa ◽  
Biagio Pinchera ◽  
Guido Granata ◽  
Nicola Petrosillo
Keyword(s):  
Infectious Diseases ◽  
Iron Uptake ◽  
Protein Complexes ◽  
Specific Binding ◽  
Binding Protein ◽  
Research Progress ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Uptake Pathway ◽  
Diagnostic Approaches

Iron is an essential micronutrient required for the growth of almost all aerobic organisms; the iron uptake pathway in bacteria therefore represents a possible target for novel antimicrobials, including hybrids between antimicrobials and siderophores. Siderophores are low molecular weight iron chelators that bind to iron and are actively transported inside the cell through specific binding protein complexes. These binding protein complexes are present both in Gram negative bacteria, in their outer and inner membrane, and in Gram positive bacteria in their cytoplasmic membrane. Most bacteria have the ability to produce siderophores in order to survive in environments with limited concentrations of free iron, however some bacteria synthetize natural siderophore-antibiotic conjugates that exploit the siderophore-iron uptake pathway to deliver antibiotics into competing bacterial cells and gain a competitive advantage. This approach has been referred to as a Trojan Horse Strategy. To overcome the increasing global problem of antibiotic resistance in Gram negative bacteria, which often have reduced outer membrane permeability, siderophore-antibiotic hybrid conjugates have been synthetized in vitro. Cefiderocol is the first siderophore-antibiotic conjugate that progressed to late stage clinical development so far. In studies on murine models the iron-siderophore uptake pathway has been also exploited for diagnostic imaging of infectious diseases, in which labelled siderophores have been used as specific probes. The aim of this review is to describe the research progress in the field of siderophore-based therapeutic and diagnostic approaches in infectious diseases.

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