Comparison of activities of β-lactam antibiotics against Streptococcus pneumoniae with recombinant penicillin-binding protein genes from a penicillin-resistant strain

Maeda, Kumiko; Ida, Takashi; Sanbongi, Yumiko; Suzuki, Takahisa; Fukushima, Toshirou; Kurazono, Mizuyo; Yonezawa, Minoru; Ubukata, Kimiko; Inoue, Matsuhisa

doi:10.1007/s10156-005-0374-2

Cited by 5 publications

(2 citation statements)

References 13 publications

(22 reference statements)

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“…29 The role of PBP1a in drug resistance has been investigated by the sequencing effort of several laboratories, which have identified mutations in clinical isolates from South Africa, Hungary, Japan, USA, France, and Canada. 16,[29][30][31][32][33][34][35] Figure 5 relates positions of all mutations within the TP and C-terminal regions of PBP1a from highly drug-resistant clinical isolates identified in France (73311), South Africa (8303), and Japan (5/H31). Interestingly, most mutations detected among PBP1a sequences from isolates coming from different continents are shared amongst all of the isolates, suggesting that there is a unique PBP1a-derived b-lactam resistance mechanism.…”

Section: Bifunctional and Monofunctional Pbpsmentioning

confidence: 99%

Crystal Structure of Penicillin-binding Protein 1a (PBP1a) Reveals a Mutational Hotspot Implicated in β-Lactam Resistance in Streptococcus pneumoniae

Contreras‐Martel

Job

Guilmi

et al. 2006

Journal of Molecular Biology

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Section: Bifunctional and Monofunctional Pbpsmentioning

confidence: 99%

Crystal Structure of Penicillin-binding Protein 1a (PBP1a) Reveals a Mutational Hotspot Implicated in β-Lactam Resistance in Streptococcus pneumoniae

Contreras‐Martel

Job

Guilmi

et al. 2006

Journal of Molecular Biology

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“…This compound has also shown potent in vitro activities against penicillin-resistant S. pneumoniae, H. influenzae, and Enterococcus faecalis. When tested against members of the Enterobacteriaceae, ME1036 is more active than ceftriaxone and other broad-spectrum cephalosporins (including ceftaroline) due to a higher level of resistance to hydrolysis by ESBLs and AmpC ␤-lactamases produced by these organisms (8,9,12).…”

mentioning

confidence: 99%

Antimicrobial Activities of Ceftaroline and ME1036 Tested against Clinical Strains of Community-Acquired Methicillin-Resistant Staphylococcus aureus

Sader

Fritsche

Jones

2008

Antimicrob Agents Chemother

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Two investigational anti-methicillin-resistant Staphylococcus aureus (anti-MRSA) ␤-lactams, ceftaroline (a cephalosporin) and ME1036 (a carbapenem), were subjected to susceptibility testing by reference broth microdilution methods using 152 strains of community-acquired MRSA from the United States (47 medical centers). Ceftaroline and ME1036 were 64-and >128-fold more potent than ceftriaxone, respectively. All isolates had the Panton-Valentine leukocidin genes and staphylococcal cassette chromosome mec type IV, while 67.8% of isolates displayed pulsed-field gel electrophoresis clonal type USA300-0114.

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β‐Lactam Antibiotics

Testero

Fisher

Mobashery

2010

Burger's Medicinal Chemistry and Drug Discovery

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The β‐lactam classes of antibacterials are preeminent in the treatment of bacterial infection due to their unparalleled clinical efficacy and clinical safety. Following the discovery of the penicillins, successive β‐lactam drug discovery has added the cephalosporin, penem cephamycin, clavulanate, monobactam, nocardicin, and carbapenem subclasses. The driving force behind much of this era of discovery is the staggering ability of pathogenic bacteria to adapt previous generations of the β‐lactam by the acquisition and expression of resistance mechanisms. Although many factors contribute to β‐lactam resistance, alterations to the molecular targets of the β‐lactams (the penicillin binding proteins) and the use of enzymes (the β‐lactamases) capable of the hydrolytic deactivation of the β‐lactams are paramount. This review traces the historical development of β‐lactam drug discovery, with emphasis on the most recent progress in the medicinal chemistry, biochemistry, and microbiology of the β‐lactams leading to the discovery of new generation β‐lactam antibacterials effective against the Gram‐negative and ‐positive bacterial pathogens of current medical concern.

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Comparison of activities of β-lactam antibiotics against Streptococcus pneumoniae with recombinant penicillin-binding protein genes from a penicillin-resistant strain

Cited by 5 publications

References 13 publications

Crystal Structure of Penicillin-binding Protein 1a (PBP1a) Reveals a Mutational Hotspot Implicated in β-Lactam Resistance in Streptococcus pneumoniae

Crystal Structure of Penicillin-binding Protein 1a (PBP1a) Reveals a Mutational Hotspot Implicated in β-Lactam Resistance in Streptococcus pneumoniae

Antimicrobial Activities of Ceftaroline and ME1036 Tested against Clinical Strains of Community-Acquired Methicillin-Resistant Staphylococcus aureus

β‐Lactam Antibiotics

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