On the Mechanism of Action of Vancomycin: Inhibition of Peptidoglycan Synthesis in
            <i>Gaffkya homari</i>

Hammes, Walter P.; Neuhaus, Francis C.

doi:10.1128/aac.6.6.722

Cited by 98 publications

(67 citation statements)

References 28 publications

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“…Vancomycin, a narrow spectrum antibiotic, is a glycopeptide that acts by inhibiting cell-wall peptidoglycan synthesis (Hammes & Neuhaus, 1974). It is active against rapidly dividing cells, and in general, has a slower rate of killing than the fluoroquinolones (Kang-Birken, 2000).…”

Section: Persisters In S Epidermidismentioning

confidence: 99%

Evidence for persisters in Staphylococcus epidermidis RP62a planktonic cultures and biofilms

Shapiro

Nguyen

Chamberlain

2011

Journal of Medical Microbiology

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The pathogenesis of Staphylococcus epidermidis in foreign device-related infections is attributed primarily to its ability to form biofilms on a polymer surface. One mechanism proposed for the survival of organisms in a biofilm is the presence of persister cells. Persister cells survive antibiotic treatment without acquiring heritable antibiotic resistance. This study was conducted to determine if S. epidermidis RP62a growing in planktonic cultures and biofilms could survive as persister cells following treatment with levofloxacin and vancomycin. S. epidermidis RP62a produced a small percentage of persisters (levofloxacin, 3.09¾10 "7 %; vancomycin, 8.21¾10 "5 %) when grown to exponential phase, whereas biofilms contained 28 and 94 % persisters, following exposure to levofloxacin and vancomycin, respectively. The highest percentages of persisters were obtained during stationary phase in planktonic cultures and the lowest percentages of persisters were obtained during mid-exponential phase. An increase in persister number was not due to activation of quorum-sensing regulons. Confocal laser scanning microscopy images of biofilms exposed to levofloxacin demonstrated that the antibiotic was able to kill bacteria throughout the biofilm. Our results suggest that antibiotic tolerance in biofilms and in planktonic cultures of S. epidermidis RP62a is due in part to the presence of persister cells.

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Section: Persisters In S Epidermidismentioning

confidence: 99%

Evidence for persisters in Staphylococcus epidermidis RP62a planktonic cultures and biofilms

Shapiro

Nguyen

Chamberlain

2011

Journal of Medical Microbiology

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“…bacteria bound or accumulated approximately 5 x 104 molecules of ramoplanin per cell, only 1/100th of the amount of vancomycin which binds to groups within peptidoglycan conforming to the pattern L-aa (amino acid)-D-aa-D-aa, suggesting that ramoplanin has a different target site. This was confirmed by in vitro studies involving a wall-membrane particulate fraction from Gaffy homari in which peptidoglycan synthesis from UDP-MurNAc-tetrapeptide was inhibited by ramoplanin but not by vancomycin.…”

mentioning

confidence: 99%

Inhibition of peptidoglycan biosynthesis by ramoplanin

Somner

Reynolds

1990

Antimicrob Agents Chemother

137

100

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“…To probe the effect of antibiotics targeting other cellular systems, we assessed the sensitivities of all strains to rifampin (inhibits RNA polymerase activity) (67) and vancomycin (inhibits cell wall synthesis) (68). Interestingly, both strains exhibited increased sensitivity to rifampin, with the ⌬rnj strain in particular being 2.7-fold more sensitive than the wild type (Fig.…”

Section: Resultsmentioning

confidence: 99%

Development, Antibiotic Production, and Ribosome Assembly in Streptomyces venezuelae Are Impacted by RNase J and RNase III Deletion

2014

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b RNA metabolism is a critical but frequently overlooked control element affecting virtually every cellular process in bacteria. RNA processing and degradation is mediated by a suite of ribonucleases having distinct cleavage and substrate specificity. Here, we probe the role of two ribonucleases (RNase III and RNase J) in the emerging model system Streptomyces venezuelae. We show that each enzyme makes a unique contribution to the growth and development of S. venezuelae and further affects the secondary metabolism and antibiotic production of this bacterium. We demonstrate a connection between the action of these ribonucleases and translation, with both enzymes being required for the formation of functional ribosomes. RNase III mutants in particular fail to properly process 23S rRNA, form fewer 70S ribosomes, and show reduced translational processivity. The loss of either RNase III or RNase J additionally led to the appearance of a new ribosomal species (the 100S ribosome dimer) during exponential growth and dramatically sensitized these mutants to a range of antibiotics. R ibonucleases (RNases) are enzymes that process and degrade RNA molecules; consequently, they are critical for RNA maturation, RNA stability, and posttranscriptional regulation (1). In bacterial cells, the finely tuned balance between RNA synthesis and RNA degradation allows for rapid adaptation to changing environments, proper processing of noncoding RNAs, and efficient recycling of ribonucleotides (2).Our understanding of RNA metabolism to date is based largely on studies of Escherichia coli and Bacillus subtilis, which employ distinct enzymes for RNA processing and degradation. In E. coli, RNase E is the central component of the RNA degradosome; as such, it is responsible for much of the RNA decay in this organism. B. subtilis lacks this enzyme, and acting in its place are three other nucleases: RNase J1/J2 and RNase Y (3, 4). Virtually all bacteria contain at least one of RNase E (or its paralog, RNase G), RNase J, or RNase Y (5). These RNases are unrelated in primary sequence and mechanism of catalysis but have similar substrate specificity: they all have single-strand-specific endonuclease activity and preferentially cleave AU-rich regions (4, 6, 7). Unlike RNase E and Y, however, RNase J has the capacity to act both as an endonuclease and as a 5= exonuclease (8, 9). The analysis of available genome sequences suggests that more than half of all bacteria, and over two-thirds of Archaea, possess an RNase J homologue (6,8). In addition to these diverse single-strand-specific RNases, most bacteria also encode the double-strand-specific RNase III (10). This enzyme is highly conserved in bacteria and eukaryotes and has a critical role in posttranscriptional regulation, where it cleaves double-stranded substrates, such as those resulting from the base pairing of an mRNA and noncoding RNA (11), or those associated with highly structured RNAs, such as ribosomal RNAs (rRNAs) (12, 13). There can be considerable functional interplay between RNases, ...

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On the Mechanism of Action of Vancomycin: Inhibition of Peptidoglycan Synthesis in Gaffkya homari

Cited by 98 publications

References 28 publications

Evidence for persisters in Staphylococcus epidermidis RP62a planktonic cultures and biofilms

Evidence for persisters in Staphylococcus epidermidis RP62a planktonic cultures and biofilms

Inhibition of peptidoglycan biosynthesis by ramoplanin

Development, Antibiotic Production, and Ribosome Assembly in Streptomyces venezuelae Are Impacted by RNase J and RNase III Deletion

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