Relevant bibliographies by topics / Lysostaphin resistance

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Academic literature on the topic 'Lysostaphin resistance'

Author: Grafiati
Published: 4 June 2021
Last updated: 27 April 2022

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Journal articles on the topic "Lysostaphin resistance"

1

Climo, Michael W., Kerstin Ehlert, and Gordon L. Archer. "Mechanism and Suppression of Lysostaphin Resistance in Oxacillin-Resistant Staphylococcus aureus." Antimicrobial Agents and Chemotherapy 45, no. 5 (May 1, 2001): 1431–37. http://dx.doi.org/10.1128/aac.45.5.1431-1437.2001.

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ABSTRACT The potential for the development of resistance in oxacillin-resistant Staphylococcus aureus (ORSA) to lysostaphin, a glycylglycine endopeptidase produced byStaphylococcus simulans biovar staphylolyticus, was examined in vitro and in an in vivo model of infection. Following in vitro exposure of ORSA to subinhibitory concentrations of lysostaphin, lysostaphin-resistant mutants were idenitifed among all isolates examined. Resistance to lysostaphin was associated with a loss of resistance to β-lactams and a change in the muropeptide interpeptide cross bridge from pentaglycine to a single glycine. Mutations in femA, the gene required for incorporation of the second and third glycines into the cross bridge, were found following PCR amplification and nucleotide sequence analysis. Complementation of lysostaphin-resistant mutants with pBBB31, which encodes femA, restored the phenotype of oxacillin resistance and lysostaphin susceptibility. Addition of β-lactam antibiotics to lysostaphin in vitro prevented the development of lysostaphin-resistant mutants. In the rabbit model of experimental endocarditis, administration of a low dose of lysostaphin for 3 days led predictably to the appearance of lysostaphin-resistant ORSA mutants in vegetations. Coadministration of nafcillin with lysostaphin prevented the emergence of lysostaphin-resistant mutants and led to a mean reduction in aortic valve vegetation counts of 7.5 log10 CFU/g compared to those for untreated controls and eliminated the isolation of lysostaphin-resistant mutants from aortic valve vegetations. Treatment with nafcillin and lysostaphin given alone led to mean reductions of 1.35 and 1.65 log10 CFU/g respectively. In ORSA, resistance to lysostaphin was associated with mutations in femA, but resistance could be suppressed by the coadministration of β-lactam antibiotics.
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Gründling, Angelika, Dominique M. Missiakas, and Olaf Schneewind. "Staphylococcus aureus Mutants with Increased Lysostaphin Resistance." Journal of Bacteriology 188, no. 17 (September 1, 2006): 6286–97. http://dx.doi.org/10.1128/jb.00457-06.

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ABSTRACT Staphylococcus simulans secretes lysostaphin, a bacteriolytic enzyme that specifically binds to the cell wall envelope of Staphylococcus aureus and cleaves the pentaglycine cross bridges of peptidoglycan, thereby killing staphylococci. The study of S. aureus mutants with resistance to lysostaphin-mediated killing has revealed biosynthetic pathways for cell wall assembly. To identify additional genes involved in cell wall envelope biosynthesis, we have screened a collection of S. aureus strain Newman transposon mutants for lysostaphin resistance. Bursa aurealis insertion in SAV2335, encoding a polytopic membrane protein with predicted protease domain, caused a high degree of lysostaphin resistance, similar to the case for a previously described femAB promoter mutant. In contrast to the case for this femAB mutant, transposon insertion in SAV2335, herein named lyrA (lysostaphin resistance A), did not cause gross alterations of cell wall cross bridges such as truncations of pentaglycine to tri- or monoglycine. Also, inactivation of LyrA in a methicillin-resistant S. aureus strain did not precipitate a decrease in β-lactam resistance as observed for fem (factor essential for methicillin resistance) mutants. Lysostaphin bound to the cell wall envelopes of lyrA mutants in a manner similar to that for wild-type staphylococci. Lysostaphin resistance of lyrA mutants is attributable to altered cell wall envelope properties and may in part be due to increased abundance of altered cross bridges. Other lyr mutants with intermediate lysostaphin resistance carried bursa aurealis insertions in genes specifying GTP pyrophosphokinase or enzymes of the purine biosynthetic pathway.
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Batool, Nayab, Kwan Soo Ko, Akhilesh Kumar Chaurasia, and Kyeong Kyu Kim. "Functional Identification of Serine Hydroxymethyltransferase as a Key Gene Involved in Lysostaphin Resistance and Virulence Potential of Staphylococcus aureus Strains." International Journal of Molecular Sciences 21, no. 23 (November 30, 2020): 9135. http://dx.doi.org/10.3390/ijms21239135.

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Gaining an insight into the mechanism underlying antimicrobial-resistance development in Staphylococcus aureus is crucial for identifying effective antimicrobials. We isolated S. aureus sequence type 72 from a patient in whom the S. aureus infection was highly resistant to various antibiotics and lysostaphin, but no known resistance mechanisms could explain the mechanism of lysostaphin resistance. Genome-sequencing followed by subtractive and functional genomics revealed that serine hydroxymethyltransferase (glyA or shmT gene) plays a key role in lysostaphin resistance. Serine hydroxymethyltransferase (SHMT) is indispensable for the one-carbon metabolism of serine/glycine interconversion and is linked to folate metabolism. Functional studies revealed the involvement of SHMT in lysostaphin resistance, as ΔshmT was susceptible to the lysostaphin, while complementation of the knockout expressing shmT restored resistance against lysostaphin. In addition, the ΔshmT showed reduced virulence under in vitro (mammalian cell lines infection) and in vivo (wax-worm infection) models. The SHMT inhibitor, serine hydroxymethyltransferase inhibitor 1 (SHIN1), protected the 50% of the wax-worm infected with wild type S. aureus. These results suggest SHMT is relevant to the extreme susceptibility to lysostaphin and the host immune system. Thus, the current study established that SHMT plays a key role in lysostaphin resistance development and in determining the virulence potential of multiple drug-resistant S. aureus.
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Kusuma, Caroline, Anna Jadanova, Tanya Chanturiya, and John F. Kokai-Kun. "Lysostaphin-Resistant Variants of Staphylococcus aureus Demonstrate Reduced Fitness In Vitro and In Vivo." Antimicrobial Agents and Chemotherapy 51, no. 2 (February 2007): 475–82. http://dx.doi.org/10.1128/aac.00786-06.

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ABSTRACT Lysostaphin is under development as a therapy for serious staphylococcal infections. During preclinical development, lysostaphin-resistant Staphylococcus aureus variants have occasionally been reported in vitro and in vivo. The acquisition of resistance to this drug, however, leads to a significant increase in β-lactam antibiotic susceptibility, rendering methicillin-resistant S. aureus (MRSA) strains functionally methicillin susceptible. In this study, we have demonstrated that the development of lysostaphin resistance by two strains of MRSA also led to a loss of fitness in the variants. Consistent with the mutations found in previously reported lysostaphin-resistant S. aureus variants, these two variants had mutations in their femA genes, resulting in nonfunctional FemA proteins and, thus, monoglycine cross bridges in the peptidoglycan. The diminished fitness of the lysostaphin-resistant variants was reflected by (i) a reduced logarithmic growth rate, with the variants being outcompeted in cocultures by their wild-type parental strains; (ii) increased susceptibility to elevated temperatures; and (iii) at least fivefold less virulence of the lysostaphin-resistant variants than their wild-type strains in a mouse kidney infection model, with the lysostaphin-resistant variants being outcompeted in coinfections with their wild-type parental strains. During a 14-day serial passage without selective pressure, the lysostaphin-resistant variants failed to develop compensatory mutations which restored their fitness. These results suggest that should lysostaphin resistance due to an alteration in the FemA function emerge in S. aureus during therapy with lysostaphin, the resistant variants would be less fit and less virulent, and, in addition, infections with these strains would be easily treatable with β-lactam antibiotics.
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Heath Farris, M., Lucie S. Heath, Harry E. Heath, Paul A. LeBlanc, Robin S. Simmonds, and Gary L. Sloan. "Expression of the genes for lysostaphin and lysostaphin resistance in streptococci." FEMS Microbiology Letters 228, no. 1 (November 2003): 115–19. http://dx.doi.org/10.1016/s0378-1097(03)00743-2.

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6

Gargis, Shaw R., Harry E. Heath, Paul A. LeBlanc, Linda Dekker, Robin S. Simmonds, and Gary L. Sloan. "Inhibition of the Activity of Both Domains of Lysostaphin through Peptidoglycan Modification by the Lysostaphin Immunity Protein." Applied and Environmental Microbiology 76, no. 20 (August 20, 2010): 6944–46. http://dx.doi.org/10.1128/aem.01066-10.

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ABSTRACT Resistance to lysostaphin, a staphylolytic glycylglycine endopeptidase, is due to a FemABX-like immunity protein that inserts serines in place of some glycines in peptidoglycan cross bridges. These modifications inhibit both binding of the recombinant cell wall targeting domain and catalysis by the recombinant catalytic domain of lysostaphin.
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7

Hertlein, Tobias, Volker Sturm, Udo Lorenz, K. Sumathy, Peter Jakob, and Knut Ohlsen. "Bioluminescence and19F Magnetic Resonance Imaging Visualize the Efficacy of Lysostaphin Alone and in Combination with Oxacillin against Staphylococcus aureus in Murine Thigh and Catheter-Associated Infection Models." Antimicrobial Agents and Chemotherapy 58, no. 3 (December 23, 2013): 1630–38. http://dx.doi.org/10.1128/aac.01422-13.

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ABSTRACTStaphylococci are the leading cause of hospital-acquired infections worldwide. Increasingly, they resist antibiotic treatment owing to the development of multiple antibiotic resistance mechanisms in most strains. Therefore, the activity and efficacy of recombinant lysostaphin as a drug against this pathogen have been evaluated. Lysostaphin exerts high levels of activity against antibiotic-resistant strains ofStaphylococcus aureus, including methicillin-resistantS. aureus(MRSA). The therapeutic value of lysostaphin has been analyzed in two different clinically relevantin vivomodels, a catheter-associated infection model and a thigh infection model. We infected mice with luciferase-expressingS. aureusXen 29, and the efficacies of lysostaphin, vancomycin, oxacillin, and combined lysostaphin-oxacillin were investigated by determining numbers of CFU, detecting bioluminescent signals, and measuring the accumulation of perfluorocarbon emulsion at the site of infection by19F magnetic resonance imaging. Lysostaphin treatment significantly reduced the bacterial burden in infected thigh muscles and, after systemic spreading from the catheter, in inner organs. The efficiency of lysostaphin treatment was even more pronounced in combinatorial therapy with oxacillin. These results suggest that recombinant lysostaphin may have potential as an anti-S. aureusdrug worthy of further clinical development. In addition, both imaging technologies demonstrated efficacy patterns similar to that of CFU determination, although they proved to be less sensitive. Nonetheless, they served as powerful tools to provide additional information about the course and gravity of infection in a noninvasive manner, possibly allowing a reduction in the number of animals needed for research evaluation of new antibiotics in future studies.
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8

Wu, Julie A., Caroline Kusuma, James J. Mond, and John F. Kokai-Kun. "Lysostaphin Disrupts Staphylococcus aureus and Staphylococcus epidermidis Biofilms on Artificial Surfaces." Antimicrobial Agents and Chemotherapy 47, no. 11 (November 2003): 3407–14. http://dx.doi.org/10.1128/aac.47.11.3407-3414.2003.

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ABSTRACT Staphylococci often form biofilms, sessile communities of microcolonies encased in an extracellular matrix that adhere to biomedical implants or damaged tissue. Infections associated with biofilms are difficult to treat, and it is estimated that sessile bacteria in biofilms are 1,000 to 1,500 times more resistant to antibiotics than their planktonic counterparts. This antibiotic resistance of biofilms often leads to the failure of conventional antibiotic therapy and necessitates the removal of infected devices. Lysostaphin is a glycylglycine endopeptidase which specifically cleaves the pentaglycine cross bridges found in the staphylococcal peptidoglycan. Lysostaphin kills Staphylococcus aureus within minutes (MIC at which 90% of the strains are inhibited [MIC90], 0.001 to 0.064 μg/ml) and is also effective against Staphylococcus epidermidis at higher concentrations (MIC90, 12.5 to 64 μg/ml). The activity of lysostaphin against staphylococci present in biofilms compared to those of other antibiotics was, however, never explored. Surprisingly, lysostaphin not only killed S. aureus in biofilms but also disrupted the extracellular matrix of S. aureus biofilms in vitro on plastic and glass surfaces at concentrations as low as 1 μg/ml. Scanning electron microscopy confirmed that lysostaphin eradicated both the sessile cells and the extracellular matrix of the biofilm. This disruption of S. aureus biofilms was specific for lysostaphin-sensitive S. aureus, as biofilms of lysostaphin-resistant S. aureus were not affected. High concentrations of oxacillin (400 μg/ml), vancomycin (800 μg/ml), and clindamycin (800 μg/ml) had no effect on the established S. aureus biofilms in this system, even after 24 h. Higher concentrations of lysostaphin also disrupted S. epidermidis biofilms.
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9

Kokai-Kun, John F., Scott M. Walsh, Tanya Chanturiya, and James J. Mond. "Lysostaphin Cream Eradicates Staphylococcus aureus Nasal Colonization in a Cotton Rat Model." Antimicrobial Agents and Chemotherapy 47, no. 5 (May 2003): 1589–97. http://dx.doi.org/10.1128/aac.47.5.1589-1597.2003.

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ABSTRACT The anterior nares are a primary ecologic niche for Staphylococcus aureus, and nasal colonization by this opportunistic pathogen increases the risk of development of S. aureus infection. Clearance of S. aureus nasal colonization greatly reduces this risk. Mupirocin ointment is the current standard of care for clearance of S. aureus nasal colonization, but resistance to this antibiotic is emerging. Lysostaphin is a glycylglycine endopeptidase which specifically cleaves the cross-linking pentaglycine bridges in the cell walls of staphylococci. Lysostaphin is extremely staphylocidal (MIC at which 90% of isolates are inhibited, 0.001 to 0.064 μg/ml) and rapidly lyses both actively growing and quiescent S. aureus. This study demonstrates that a single application of 0.5% lysostaphin (actual dose, ∼150 μg of lysostaphin), formulated in a petrolatum-based cream, dramatically reduces S. aureus nasal colonization in 100% of animals tested and eradicates S. aureus nasal colonization in 93% of animals in a cotton rat model. A single dose of lysostaphin cream is more effective than a single dose of mupirocin ointment in eradicating S. aureus nasal colonization in this animal model. The lantibiotic peptide nisin, which has potent in vitro antistaphylococcal activity, was ineffective in reducing staphylococcal nasal carriage in this model. Nasal colonization was not reduced after three treatments with 5% nisin (∼1,500 μg/dose) in any of the treated animals. Lysostaphin formulated in cream may prove to be a superior alternative to mupirocin ointment for clearance of S. aureus nasal colonization.
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10

Heath, H. E., Lucie S. Heath, James D. Nitterauer, Karen E. Rose, and Gary L. Sloan. "Plasmid-encoded lysostaphin endopeptidase resistance of staphylococcussimulans biovar staphylolyticus." Biochemical and Biophysical Research Communications 160, no. 3 (May 1989): 1106–9. http://dx.doi.org/10.1016/s0006-291x(89)80117-2.

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Dissertations / Theses on the topic "Lysostaphin resistance"

1

Stumpf, Katrina S. "IS256 mediated alteration of femAB expression in Staphylococcus epidermidis and its effect on lysostaphin resistance." VCU Scholars Compass, 2007. http://scholarscompass.vcu.edu/etd_retro/59.

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Mechanisms responsible for the development of acquired resistance to lysostaphin, a glycylglycine endopeptidase, among isolates of Staphylococcus epidermidis were examined. Following overnight exposure to sub-inhibitory concentrations of lysostaphin, lysostaphin-resistant, oxacillin-susceptible mutants were isolated and characterized. Lysostaphin resistance was associated with mutations within the promoter region of the femAB operon. Four of the six characterized mutants contained an IS256 insertion within the femAB promoter and the remaining two mutants had an 18bp deletion within this region. IS256 insertion and the 18-bp deletions were associated with a reduction in femAB transcription and led to the production of an altered peptidoglycan muropeptide with interpeptide crossbridges consisting of a single glycine. The transcriptional start site of femAB was mapped to a 43-bp region of high homology between staphylococcal species, with five out of the six mutations occurring within this putative consensus region. We identified the femAB promoter region as the primary location of mutations associated with lysostaphin resistance.
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Stumpf, Katrina Sue. "IS256 mediated alteration of femAB expression in staphylococcus epidermidis and its effect of lysostaphin resistance /." 2007. http://hdl.handle.net/10156/1183.

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