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Versatility of aminoglycosides and prospects for their future. Clin Microbiol Rev. A common mechanism of cellular death induced by bactericidal antibiotics. Reveals that treatment of Gram-positive and Gram-negative bacteria with lethal levels of bactericidal antibiotics induces the formation of hydroxyl radicals via a common mechanism involving drug-induced changes in NADH consumption and central metabolism, notably the tricarboxylic acid cycle.
Gyrase inhibitors induce an oxidative damage cellular death pathway in Escherichia coli. Mol Syst Biol. Describes the physiological responses of E. Ultimately, these physiological changes are shown to result in hydroxyl radical production, which contribute to cell death. Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death. Demonstrates that systems which facilitate membrane protein traffic are central to aminoglycoside-induced oxidative stress and cell death.
This occurs by signaling through the redox- and the envelope stress-responsive two-component systems. These two-component systems are also shown to have a general role in bactericidal antibiotic-mediated oxidative stress and cell death, expanding our understanding of the common mechanism of killing induced by bactericidal antibiotics.
Espeli O, Marians KJ. Untangling intracellular DNA topology. Mol Microbiol. Drlica K, Snyder M. Superhelical Escherichia coli DNA: relaxation by coumermycin. J Mol Biol. Mechanism of action of nalidixic acid: purification of Escherichia coli nalA gene product and its relationship to DNA gyrase and a novel nicking-closing enzyme.
References 14 and 15 discuss the results of complementary in vivo and in vitro studies that characterized the genetic locus nalA , later gyrA and the basic mechanism of quinolone antibiotic action prevention of DNA duplex strand rejoining yielding double-stranded DNA breaks , while postulating on the composition and energetic requirements of DNA gyrase activity.
Nalidixic acid resistance: a second genetic character involved in DNA gyrase activity. Hooper DC, Rubinstein E. Quinolone antimicrobial agents. Rubinstein E. History of quinolones and their side effects. Lu T, et al. Enhancement of fluoroquinolone activity by C-8 halogen and methoxy moieties: action against a gyrase resistance mutant of Mycobacterium smegmatis and a gyrase-topoisomerase IV double mutant of Staphylococcus aureus. Identifies topoisomerase IV as a second target of fluoroquinolone antibiotics in Gram-negative bacteria, while characterizing subtle yet critical differences in the mechanism of killing by various quinolone drugs.
Drlica K, Zhao X. DNA gyrase, topoisomerase IV, and the 4-quinolones. Microbiol Mol Biol Rev. Neisseria gonorrhoeae acquires mutations in analogous regions of gyrA and parC in fluoroquinolone-resistant isolates. Critchlow SE, Maxwell A. Marians KJ, Hiasa H. Mechanism of quinolone action. J Biol Chem.
Kampranis SC, Maxwell A. The DNA gyrase-quinolone complex. Morais Cabral JH, et al. Crystal structure of the breakage-reunion domain of DNA gyrase.
Heddle J, Maxwell A. Inhibition of Deoxyribonucleic Acid Synthesis. J Bacteriol. Snyder M, Drlica K. Cox MM, et al. The importance of repairing stalled replication forks. Courcelle J, Hanawalt PC. RecA-dependent recovery of arrested DNA replication forks. Annu Rev Genet. J Pharm Pharmacol. Cirz RT, et al. Inhibition of mutation and combating the evolution of antibiotic resistance. PLoS Biol. Guerin E, et al. The SOS response controls integron recombination.
SOS response promotes horizontal dissemination of antibiotic resistance genes. J Med Microbiol. Contribution of reactive oxygen species to pathways of quinolone-mediated bacterial cell death.
J Antimicrob Chemother. The communication factor EDF and the toxin-antitoxin module mazEF determine the mode of action of antibiotics. Dukan S, et al. Protein oxidation in response to increased transcriptional or translational errors. Biochim Biophys Acta. Campbell EA, et al. Structural mechanism for rifampicin inhibition of bacterial rna polymerase.
Describes the intricacies of binding between the rifamycin antibiotic, rifampicin, and a DNA-engaged RNA polymerase, while providing a detailed mechanism for rifamycin action blockage of the nacent RNA transcript exit channel based primarially on the results of x-ray crystallography studies.
The beta subunit of Escherichia coli RNA polymerase is not required for interaction with initiating nucleotide but is necessary for interaction with rifampicin. RNA polymerase. Y: On the mechanism of rifampicin inhibition of RNA synthesis. A new class of bacterial RNA polymerase inhibitor affects nucleotide addition. Rifomycin, a new antibiotic; preliminary report. Farmaco Sci. Sensi P. History of the development of rifampin. Rev Infect Dis. Wehrli W. Rifampin: mechanisms of action and resistance.
Comparative pharmacokinetics and pharmacodynamics of the rifamycin antibacterials. Clin Pharmacokinet. The action of rifampin alone and in combination with other antituberculous drugs. Am Rev Respir Dis. Kono Y. Oxygen Enhancement of bactericidal activity of rifamycin SV on Escherichia coli and aerobic oxidation of rifamycin SV to rifamycin S catalyzed by manganous ions: the role of superoxide. J Biochem Tokyo ; 91 — Reveals that redox cycling of rifamycin drug molecules results in the formation of reactive oxygen species, and that reactive oxygen species generation contributes to the bactericidal activity of the antibiotic.
Scrutton MC. Divalent metal ion catalysis of the oxidation of rifamycin SV to rifamycin S. FEBS Lett. Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: enzymology, antibiotics, and antibiotic resistance. Nat Prod Rep. Holtje JV. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Park JT, Uehara T. How bacteria consume their own exoskeletons turnover and recycling of cell wall peptidoglycan Microbiol Mol Biol Rev.
Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.
References 56 and 57 describe the results of complementary studies first revealing that inhibition of cell wall biosynthesis by beta-lactam antibiotics is due to catalytic site modification of transpeptidase and carboxypeptidase enzymes later penicillin binding proteins , which misrecognize the drug molecule as a peptidoglycan substrate mimic.
Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Penicillins and cephalosporins are active site-directed acylating agents: evidence in support of the substrate analogue hypothesis.
The perfect penicillin? Inhibition of a bacterial DD-peptidase by peptidoglycan-mimetic beta-lactams. J Am Chem Soc. Glycopeptide and lipoglycopeptide antibiotics. Binding of glycopeptide antibiotics to a model of a vancomycin-resistant bacterium. Chem Biol. Ge M, et al. Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala. Multiple antibiotic resistance in a bacterium with suppressed autolytic system. Demonstrates for the first time that beta-lactam-induced cell lysis is regulated by the activity of murein hydrolases.
Also reveals that wild-type pneumococci and lysis-defective, murein hydrolase activity-deficient pneumococci are equally sensitive to beta-lactam treatment despite starkly different phenotypic effects.
Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli. Reveals that murein hydrolases in E. LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli.
Two bactericidal targets for penicillin in pneumococci: autolysis-dependent and autolysis-independent killing mechanisms. Describes the characterization of the cid system in pneumococci, which contributes to killing by beta-lactams independently of murein hydrolase autolysin activity. Hoch JA. Two-component and phosphorelay signal transduction. Curr Opin Microbiol.
Emergence of vancomycin tolerance in Streptococcus pneumoniae. Signal transduction by a death signal peptide: uncovering the mechanism of bacterial killing by penicillin. Mol Cell. Identification and molecular characterization of a putative regulatory locus that affects autolysis in Staphylococcus aureus.
Identification of LytSR-regulated genes from Staphylococcus aureus. The Staphylococcus aureus lrgAB operon modulates murein hydrolase activity and penicillin tolerance. Rice KC, et al. The Staphylococcus aureus cidAB operon: evaluation of its role in regulation of murein hydrolase activity and penicillin tolerance. Bayles KW. The biological role of death and lysis in biofilm development.
Spratt BG. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K Kitano K, Tomasz A. Triggering of autolytic cell wall degradation in Escherichia coli by beta-lactam antibiotics. Bi E, Lutkenhaus J. Goehring NW, Beckwith J. Diverse paths to midcell: assembly of the bacterial cell division machinery.
Curr Biol. Miller C, et al. SOS response induction by beta-lactams and bacterial defense against antibiotic lethality. Describes observations made in E. Varma A, Young KD. FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli. Lytic effect of two fluoroquinolones, ofloxacin and pefloxacin, on Escherichia coli W7 and its consequences on peptidoglycan composition.
Garrett RA. The ribosome: structure, function, antibiotics, and cellular interactions. The structural basis of ribosome activity in peptide bond synthesis. Katz L, Ashley GW. Translation and protein synthesis: macrolides. Streptogramins, oxazolidinones, and other inhibitors of bacterial protein synthesis. Patel U, et al.
Oxazolidinones mechanism of action: inhibition of the first peptide bond formation. Vannuffel P, Cocito C. Mechanism of action of streptogramins and macrolides. Erythromycin, carbomycin, and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl-tRNA from ribosomes.
The mechanism of action of macrolides, lincosamides and streptogramin B reveals the nascent peptide exit path in the ribosome. If your child receives an antibiotic, be sure to give it exactly as prescribed to decrease the development of resistant bacteria. Have your child finish the entire prescription. Don't stop when the symptoms of infection go away. Never save the left over antibiotics to use "just in case. Do not share your antibiotics with someone else or take an antibiotic that was prescribed for someone else.
Remember that taking antibiotics appropriately and making sure your child receives the proper immunizations will help prevent having to take more dangerous and more costly medicines. Talk with your healthcare provider for more information. Health Home Wellness and Prevention. There are 2 main types of germs that cause most infections. These are viruses and bacteria. Viruses cause: Colds and flu Runny noses Most coughs and bronchitis Most sore throats Antibiotics cannot kill viruses or help you feel better when you have a virus.
Bacteria cause: Most ear infections Some sinus infections Strep throat Urinary tract infections Antibiotics do kill specific bacteria. What are resistant bacteria? Bacteria can develop resistance to certain medicines: Medicine resistance happens when bacteria develop ways to survive the use of medicines meant to kill or weaken them. When are antibiotics needed?
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