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penicillin-binding proteins

  • First Penicillin-Binding Protein Occupancy Patterns for 15 β-Lactams and β-Lactamase Inhibitors in <span class="named-content genus-species" id="named-content-1">Mycobacterium abscessus</span>
    Pharmacology
    First Penicillin-Binding Protein Occupancy Patterns for 15 β-Lactams and β-Lactamase Inhibitors in Mycobacterium abscessus

    Mycobacterium abscessus causes serious infections that often require over 18 months of antibiotic combination therapy. There is no standard regimen for the treatment of M. abscessus infections, and the multitude of combinations that have been used clinically have had low success rates and high rates...

    Alaa R. M. Sayed, Nirav R. Shah, Kari B. Basso, Manasi Kamat, Yuanyuan Jiao, Bartolome Moya, Dhruvitkumar S. Sutaria, Yinzhi Lang, Xun Tao, Weiguo Liu, Eunjeong Shin, Jieqiang Zhou, Carolin Werkman, Arnold Louie, George L. Drusano, Jürgen B. Bulitta
  • Multiple Low-Reactivity Class B Penicillin-Binding Proteins Are Required for Cephalosporin Resistance in Enterococci
    Editor's Pick Mechanisms of Resistance
    Multiple Low-Reactivity Class B Penicillin-Binding Proteins Are Required for Cephalosporin Resistance in Enterococci

    Enterococcus faecalis and Enterococcus faecium are commensals of the gastrointestinal tract of most terrestrial organisms, including humans, and are major causes of health care-associated infections. Such infections are difficult or impossible to treat, as the enterococcal strains responsible are...

    Dušanka Djorić, Jaime L. Little, Christopher J. Kristich
  • Open Access
    Susceptibility of Methicillin-Resistant <span class="named-content genus-species" id="named-content-1">Staphylococcus aureus</span> to Five Quinazolinone Antibacterials
    Susceptibility
    Susceptibility of Methicillin-Resistant Staphylococcus aureus to Five Quinazolinone Antibacterials

    The in vitro activities of five quinazolinone antibacterials, compounds Q1 to Q5, were tested against 210 strains of methicillin-resistant Staphylococcus aureus (MRSA). The MIC50/MIC90 values (in μg/ml) were as follows: Q1, 0.5/2; Q2, 1/4; Q3, 2/4; Q4, 0.06/0.25; and Q5, 0.125/0.5.

    Sara Ceballos, Choon Kim, Yuanyuan Qian, Shahriar Mobashery, Mayland Chang, Carmen Torres
  • Influence of the α-Methoxy Group on the Reaction of Temocillin with <span class="named-content genus-species" id="named-content-1">Pseudomonas aeruginosa</span> PBP3 and CTX-M-14 β-Lactamase
    Mechanisms of Action: Physiological Effects
    Influence of the α-Methoxy Group on the Reaction of Temocillin with Pseudomonas aeruginosa PBP3 and CTX-M-14 β-Lactamase

    The prevalence of multidrug-resistant Pseudomonas aeruginosa has led to the reexamination of older “forgotten” drugs, such as temocillin, for their ability to combat resistant microbes. Temocillin is the 6-α-methoxy analogue of ticarcillin, a carboxypenicillin with well-characterized antipseudomonal properties. The α-methoxy modification confers resistance to serine β...

    Michael D. Sacco, Kyle G. Kroeck, M. Trent Kemp, Xiujun Zhang, Logan D. Andrews, Yu Chen
  • Open Access
    Bicarbonate Resensitization of Methicillin-Resistant <em>Staphylococcus aureus</em> to β-Lactam Antibiotics
    Editor's Pick Susceptibility
    Bicarbonate Resensitization of Methicillin-Resistant Staphylococcus aureus to β-Lactam Antibiotics

    Endovascular infections caused by methicillin-resistant Staphylococcus aureus (MRSA) are a major health care concern, especially infective endocarditis (IE). Standard antimicrobial susceptibility testing (AST) defines most MRSA strains as “resistant” to β-lactams, often leading to the use of costly and/or toxic treatment regimens. In this investigation, five prototype...

    Selvi C. Ersoy, Wessam Abdelhady, Liang Li, Henry F. Chambers, Yan Q. Xiong, Arnold S. Bayer
  • <em>In Vitro</em> Activity of Tebipenem (SPR859) against Penicillin-Binding Proteins of Gram-Negative and Gram-Positive Bacteria
    Mechanisms of Action: Physiological Effects
    In Vitro Activity of Tebipenem (SPR859) against Penicillin-Binding Proteins of Gram-Negative and Gram-Positive Bacteria

    Tebipenem (SPR859) is the microbiologically active form of SPR994 (tebipenem-pivoxil), an orally available carbapenem with activity against extended-spectrum β-lactamase (ESBL)-producing Enterobacteriaceae. Measurement of the relative binding of SPR859 to the bacterial cell targets revealed that it is a potent inhibitor of multiple penicillin-binding proteins (PBPs) but primarily a Gram-negative PBP 2 inhibitor, similar to...

    Evelyne Lacasse, Eric Brouillette, Audrey Larose, Thomas R. Parr, Aileen Rubio, François Malouin
  • Genetic Determinants of Penicillin Tolerance in <span class="named-content genus-species" id="named-content-1">Vibrio cholerae</span>
    Mechanisms of Resistance
    Genetic Determinants of Penicillin Tolerance in Vibrio cholerae

    Many bacteria are resistant to killing (tolerant) by typically bactericidal antibiotics due to their ability to counteract drug-induced cell damage. Vibrio cholerae, the cholera agent, displays an unusually high tolerance to diverse inhibitors of cell wall synthesis.

    Anna I. Weaver, Shannon G. Murphy, Benjamin D. Umans, Srikar Tallavajhala, Ikenna Onyekwere, Stephen Wittels, Jung-Ho Shin, Michael VanNieuwenhze, Matthew K. Waldor, Tobias Dörr
  • Epidemiology and Surveillance
    Multiclonal Expansion and High Prevalence of β-Lactamase-Negative Haemophilus influenzae with High-Level Ampicillin Resistance in Japan and Susceptibility to Quinolones

    β-Lactam-resistant Haemophilus influenzae is a clinical concern. A high prevalence (>40%) of β-lactamase-negative high-level ampicillin-resistant H. influenzae (high-BLNAR) isolates in Japan has been reported.

    Hiroyuki Honda, Toyotaka Sato, Masaaki Shinagawa, Yukari Fukushima, Chie Nakajima, Yasuhiko Suzuki, Tsukasa Shiraishi, Koji Kuronuma, Satoshi Takahashi, Hiroki Takahashi, Shin-ichi Yokota
  • Mechanisms of Resistance
    Carbapenem-Nonsusceptible Haemophilus influenzae with Penicillin-Binding Protein 3 Containing an Amino Acid Insertion
    Kazuki Kitaoka, Kouji Kimura, Hiromitsu Kitanaka, Hirotsugu Banno, Wanchun Jin, Jun-ichi Wachino, Yoshichika Arakawa
  • Pharmacology
    First Penicillin-Binding Protein Occupancy Patterns of β-Lactams and β-Lactamase Inhibitors in Klebsiella pneumoniae
    Dhruvitkumar S. Sutaria, Bartolome Moya, Kari B. Green, Tae Hwan Kim, Xun Tao, Yuanyuan Jiao, Arnold Louie, George L. Drusano, Jürgen B. Bulitta

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