Transport across the outer membrane porin of mycolic acid containing actinomycetales: Nocardia farcinica

Singh, Pratik Raj; Bajaj, Harsha; Benz, Roland; Winterhalter, Mathias; Mahendran, Kozhinjampara R.

doi:10.1016/j.bbamem.2014.11.020

Cited by 6 publications

(5 citation statements)

References 56 publications

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“…Moreover, Gram-positive bacteria ( Nocardia farcinica) has a complex cell wall and bind to a variety of lipids and pore-forming proteins and form a hydrophilic pathway across the cell wall and exhibited in interaction with the antibiotics. The role of mycobacterial resistance to antibiotics in outer-membrane is indispensable [62]. Certain antibiotic-resistant bacteria strain either lack or over express outer membrane proteins.…”

Section: Resistance Mechanisms Of Biofilmmentioning

confidence: 99%

Understanding the Mechanism of Bacterial Biofilms Resistance to Antimicrobial Agents

et al. 2017

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A biofilm is a group of microorganisms, that causes health problems for the patients with indwelling medical devices via attachment of cells to the surface matrix. It increases the resistance of a microorganism for antimicrobial agents and developed the human infection. Current strategies are removed or prevent the microbial colonies from the medical devices, which are attached to the surfaces. This will improve the clinical outcomes in favor of the patients suffering from serious infectious diseases. Moreover, the identification and inhibition of genes, which have the major role in biofilm formation, could be the effective approach for health care systems. In a current review article, we are highlighting the biofilm matrix and molecular mechanism of antimicrobial resistance in bacterial biofilms.

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Section: Resistance Mechanisms Of Biofilmmentioning

confidence: 99%

Understanding the Mechanism of Bacterial Biofilms Resistance to Antimicrobial Agents

et al. 2017

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“…The outer cell membrane of all Gram-negative and a few Gram-positive bacteria contains a pore protein called porin, which is the mediators for the diffusion of hydrophilic molecules inside a cell and can initiate the host–guest interaction. On solubilizing the Zn(II)-complexes, the departure of the metal coordinated halide (Br < I) makes it a positively charged entity, which gets attracted toward the negatively charged porins , through electrostatic interaction. As the phosphatase-like activity of such Zn(II) complexes is much more pronounced, as evident from previous works of our group, it can be assumed that the complexes can also break down the phospholipid chain of the cell membrane by the hydrolysis of the phosphoester bond.…”

Section: Resultsmentioning

confidence: 99%

Biochemical Resistivity against Free Radicals and Microbes: Cooperative Action of Zn(II)/Imidazole in Phosphoesterase-Mediated Cell Death

Biswas

Chowdhury

Dutta

et al. 2023

ACS Appl. Bio Mater.

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This work delivers a targeted synthesis of four isostructural O-substituted imidazole-based zinc(II) complexes, namely, [Zn 2 (L 1 ) 2 (I) 2 ](DMF) (1), [Zn 2 (L 2 ) 2 (I) 2 ](DMF) (2), [Zn 2 (L 1 ) 2 (Br) 2 ] (3), and [Zn 2 (L 2 ) 2 (Br) 2 ] (4), derived from homologous Schiff-base ligands HL 1 and HL 2 to explore their impact on free radicals, microbes, and dephosphorylation of phosphoesters. The antioxidant activity of all complexes was checked by various radical scavenging assays (ABTS +• , DPPH • , and H 2 O 2 radical quenching). Among them, complex 2 showed superior radical quenching activity, as indicated by its lowest EC50 value and thus maximum antioxidative capability. Again, antibacterial assays against several Gram-positive and Gramnegative bacteria were conducted to evaluate the zone of inhibition. The minimum bactericidal concentration and minimum inhibitory concentration values from the microdilution method for all complexes revealed complex 3 to have maximum potency against Gram-positive bacteria. The P−O bond hydrolysis in the phospholipid chain caused by the hydrolytic phosphoesterase activity of the Zn(II)-complexes plays a crucial role in cell membrane rupture. A model substrate 4-PNPP was used to explain the potency of monomeric Zn(II) complex (3) for cell penetration over dimeric one (2) with a proper mechanism. Furthermore, a heme model substrate, Fe(TPP)Cl, has been introduced with the most potent complex 3 and has spectrophotometric evidence for covalent interaction with imidazole and Fe(III) that can disrupt the nitric oxide dioxygenase function of flavohemoglobin, leading to bacterial cell death. To our knowledge, this is the first case to report a novel mechanism of antimicrobial action where both the metal and the ligand are cooperatively involved in bacterial cell death. The main goal of this work is to invent multifunctional therapeutics as well as the proper chemical rationalization of biological processes using mechanistic approaches, which includes investigating the roles of halides, imidazoles, and solution-phase structural variations of complexes..

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“…After a renaturation procedure, these subunits formed oligomers. Examples are the MspA monomer of M. smegmatis and the NfpA and NfpB monomers of N. farcinica (Niederweis et al 1999 ; Kläckta et al 2011 ; Singh et al 2015 ) that formed channels in lipid bilayer membranes. Genes porARc , porARr and porBRr were cloned by inserting in pET19b, resulting in the vectors pET19b_ porARC , pET19b_ porARr* , and pET19b_ porBRr* .…”

Section: Methodsmentioning

confidence: 99%

Cell wall channels of Rhodococcus species: identification and characterization of the cell wall channels of Rhodococcus corynebacteroides and Rhodococcus ruber

et al. 2022

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The cell wall of Rhodococcus corynebacteroides formerly known as Nocardia corynebacteroides contains cell wall channels that are responsible for the cell wall permeability of this bacterium. Based on partial sequencing of the polypeptide subunits and a BLAST search, we identified one polypeptide of R. corynebacteroides (PorARc) and two polypeptides (PorARr and PorBRr) from the closely related bacterium Rhodococcus ruber. The corresponding genes, porARc (606 bp), porARr (702 bp), and porBRr (540 bp) are constituents of the known genome of R. corynebacteroides DSM-20151 and R. ruber DSM-43338, respectively. porARr and porBRr of R. ruber are possibly forming a common operon coding for the polypeptide subunits of the cell wall channel. The genes coding for PorARc and for PorARr and PorBRr without signal peptide were separately expressed in the porin-deficient Escherichia coli BL21DE3Omp8 strain and the proteins were purified to homogeneity. All proteins were checked for channel formation in lipid bilayers. PorARc formed channels with characteristics that were very similar to those of a previous study. The proteins PorARr and PorBRr expressed in E. coli could alone create channels in lipid bilayer membranes, despite the possibility that the two corresponding genes form a porin operon and that both subunits possibly form the cell wall channels in vivo. Based on amino acid sequence comparison of a variety of proteins forming cell wall channels in bacteria of the suborder Corynebacterineae, it seems very likely that PorARc, PorARr, and PorBRr are members of a huge family of proteins (PF09203) that form MspA-like cell wall channels.

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Transport across the outer membrane porin of mycolic acid containing actinomycetales: Nocardia farcinica

Cited by 6 publications

References 56 publications

Understanding the Mechanism of Bacterial Biofilms Resistance to Antimicrobial Agents

Understanding the Mechanism of Bacterial Biofilms Resistance to Antimicrobial Agents

Biochemical Resistivity against Free Radicals and Microbes: Cooperative Action of Zn(II)/Imidazole in Phosphoesterase-Mediated Cell Death

Cell wall channels of Rhodococcus species: identification and characterization of the cell wall channels of Rhodococcus corynebacteroides and Rhodococcus ruber

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