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Bacteriolysis
The Experts below are selected from a list of 201 Experts worldwide ranked by ideXlab platform
Edward E. Ishiguro – 1st expert on this subject based on the ideXlab platform
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temperature sensitivity of Bacteriolysis induced by β lactam antibiotics in amino acid deprived escherichia coli
Journal of Bacteriology, 1998Co-Authors: Dmitrii G. Rodionov, Edward E. IshiguroAbstract:The temperature-sensitive penicillin tolerance response previously reported in amino acid-deprived Escherichia coli (W. Kusser and E. E. Ishiguro, J. Bacteriol. 169:2310–2312, 1987) was not due to the induction of the heat shock response resulting from a temperature upshift and was therefore unrelated to the findings of another report (J. K. Powell and K. D. Young, J. Bacteriol. 173:4021–4026, 1991) indicating a positive correlation between the expression of heat shock proteins and penicillin tolerance. The thermosensitive event occurred in the lysis induction stage.
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Ampicillin-induced Bacteriolysis of Escherichia coli is not affected by reduction in levels of anionic phospholipids
Fems Microbiology Letters, 1997Co-Authors: Dmitrii G. Rodionov, Edward E. IshiguroAbstract:Anionic phospholipids have been shown to interact with both membrane-associated proteins and integral membrane proteins. The objective of this work was to determine whether Bacteriolysis induced by treatment with ampicillin was influenced by the levels of anionic membrane phospholipids in Escherichia coli strain HDL11. The pgsA gene, encoding phosphatidylglycerophosphate synthase, in HDL11 is under the control of lacOP, and the levels of anionic membrane phospholipids are consequently dependent on IPTG. The results indicate that limiting the amounts of phosphatidylglycerol and cardiolipin did not affect the lysis process in both growing and nongrowing bacteria.
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beta lactam induced Bacteriolysis of amino acid deprived escherichia coli is dependent on phospholipid synthesis
Journal of Bacteriology, 1995Co-Authors: Dmitrii G. Rodionov, A G Pisabarro, M A De Pedro, W Kusser, Edward E. IshiguroAbstract:The penicillin tolerance of amino acid-deprived relA+ Escherichia coli is attributed to the stringent response; i.e., relaxation of the stringent response suppresses penicillin tolerance. The beta-lactam-induced lysis of amino acid-deprived bacteria resulting from relaxation of the stringent response was inhibited by cerulenin, or by glycerol deprivation in the case of a gpsA mutant (defective in the biosynthetic sn-glycerol 3-phosphate dehydrogenase). Therefore, beta-lactam-induced lysis of amino acid-deprived cells was dependent on phospholipid synthesis. The lysis process during amino acid deprivation can be experimentally dissociated into two stages designated the priming stage (during which the interaction between the beta-lactam and the penicillin-binding proteins occurs) and the beta-lactam-independent lysis induction stage. Both stages were shown to require phospholipid synthesis. It has been known for some time that the inhibition of phospholipid synthesis is among the plethora of physiological changes resulting from the stringent response. These results indicate that the inhibition of peptidoglycan synthesis and the penicillin tolerance associated with the stringent response are both secondary consequences of the inhibition of phospholipid synthesis.
Isaac Ginsburg – 2nd expert on this subject based on the ideXlab platform
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Are cationic antimicrobial peptides also ‘double-edged swords’?
Expert Review of Anti-infective Therapy, 2020Co-Authors: Isaac Ginsburg, Erez KorenAbstract:The present view focuses on the possibility that cationic antimicrobial peptides (CAMPs) might, in addition to their killing effects due to permeabilization of microbial membranes, also function similarly to β-lactam antibiotics to activate nascent autolytic wall enzymes, leading to Bacteriolysis. Since the massive release of microbial cell wall components is a major cause of postinfectious sequelae, the in vivo process of Bacteriolysis must be controlled. Due to the emergence of antibiotic resistance in pathogenic bacteria, CAMPs might be useful as an alternative to antibiotics. However, they should be used with caution, since they might also function as a ‘double-edged sword’ by injuring both the bacteria and host.
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Bacteriolysis a mere laboratory curiosity
Critical Reviews in Microbiology, 2018Co-Authors: Isaac Ginsburg, Erez KorenAbstract:The role of Bacteriolysis in the pathophysiology of microbial infections dates back to 1893 when Buchner and Pfeiffer reported for the first time the lysis of bacteria by immune serum and related this phenomenon to the immune response. Later on, basic anti-microbial peptides and certain beta-lactam antibiotics have been shown not only to kill microorganisms but also to induce Bacteriolysis and the release of cell-wall components.In 2009, a novel paradigm was offered suggesting that the main cause of death in sepsis is due to the exclusive release from activated human phagocytic neutrophils (PMNs) traps adhering upon endothelial cells of highly toxic nuclear histone. Since activated PMNs also release a plethora of pro-inflammatory agonists, it stands to reason that these may act in synergy with histone to damage cells. Since certain beta lactam antibiotics may induce Bacteriolysis, it is questioned whether these may aggravate sepsis patient’s condition. Enigmatically, since the term Bacteriolysis a…
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Bacteriolysis – a mere laboratory curiosity?
Critical Reviews in Microbiology, 2018Co-Authors: Isaac Ginsburg, Erez KorenAbstract:The role of Bacteriolysis in the pathophysiology of microbial infections dates back to 1893 when Buchner and Pfeiffer reported for the first time the lysis of bacteria by immune serum and related this phenomenon to the immune response. Later on, basic anti-microbial peptides and certain beta-lactam antibiotics have been shown not only to kill microorganisms but also to induce Bacteriolysis and the release of cell-wall components.In 2009, a novel paradigm was offered suggesting that the main cause of death in sepsis is due to the exclusive release from activated human phagocytic neutrophils (PMNs) traps adhering upon endothelial cells of highly toxic nuclear histone. Since activated PMNs also release a plethora of pro-inflammatory agonists, it stands to reason that these may act in synergy with histone to damage cells. Since certain beta lactam antibiotics may induce Bacteriolysis, it is questioned whether these may aggravate sepsis patient’s condition. Enigmatically, since the term Bacteriolysis a…
Dmitrii G. Rodionov – 3rd expert on this subject based on the ideXlab platform
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temperature sensitivity of Bacteriolysis induced by β lactam antibiotics in amino acid deprived escherichia coli
Journal of Bacteriology, 1998Co-Authors: Dmitrii G. Rodionov, Edward E. IshiguroAbstract:The temperature-sensitive penicillin tolerance response previously reported in amino acid-deprived Escherichia coli (W. Kusser and E. E. Ishiguro, J. Bacteriol. 169:2310–2312, 1987) was not due to the induction of the heat shock response resulting from a temperature upshift and was therefore unrelated to the findings of another report (J. K. Powell and K. D. Young, J. Bacteriol. 173:4021–4026, 1991) indicating a positive correlation between the expression of heat shock proteins and penicillin tolerance. The thermosensitive event occurred in the lysis induction stage.
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Ampicillin-induced Bacteriolysis of Escherichia coli is not affected by reduction in levels of anionic phospholipids
Fems Microbiology Letters, 1997Co-Authors: Dmitrii G. Rodionov, Edward E. IshiguroAbstract:Anionic phospholipids have been shown to interact with both membrane-associated proteins and integral membrane proteins. The objective of this work was to determine whether Bacteriolysis induced by treatment with ampicillin was influenced by the levels of anionic membrane phospholipids in Escherichia coli strain HDL11. The pgsA gene, encoding phosphatidylglycerophosphate synthase, in HDL11 is under the control of lacOP, and the levels of anionic membrane phospholipids are consequently dependent on IPTG. The results indicate that limiting the amounts of phosphatidylglycerol and cardiolipin did not affect the lysis process in both growing and nongrowing bacteria.
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Ampicillin-induced Bacteriolysis of is not affected by reduction in levels of anionic phospholipids
Fems Microbiology Letters, 1997Co-Authors: Dmitrii G. Rodionov, E IshiguroAbstract:Anionic phospholipids have been shown to interact with both membrane-associated proteins and integral membrane proteins. The objective of this work was to determine whether Bacteriolysis induced by treatment with ampicillin was influenced by the levels of anionic membrane phospholipids in Escherichia coli strain HDL11. The pgsA gene, encoding phosphatidylglycerophosphate synthase, in HDL11 is under the control of lacOP, and the levels of anionic membrane phospholipids are consequently dependent on IPTG. The results indicate that limiting the amounts of phosphatidylglycerol and cardiolipin did not affect the lysis process in both growing and nongrowing bacteria.