| Literature DB >> 33106266 |
Alaa R M Sayed1,2, Nirav R Shah1, Kari B Basso3, Manasi Kamat3, Yuanyuan Jiao1, Bartolome Moya4,5, Dhruvitkumar S Sutaria1, Yinzhi Lang1, Xun Tao1, Weiguo Liu6, Eunjeong Shin1, Jieqiang Zhou1, Carolin Werkman1, Arnold Louie6, George L Drusano6, Jürgen B Bulitta7.
Abstract
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 of toxicities. With β-lactam antibiotics being safe, double β-lactam and β-lactam/β-lactamase inhibitor combinations are of interest for improving the treatment of M. abscessus infections and minimizing toxicity. However, a mechanistic approach for building these combinations is lacking since little is known about which penicillin-binding protein (PBP) target receptors are inactivated by different β-lactams in M. abscessus We determined the preferred PBP targets of 13 β-lactams and 2 β-lactamase inhibitors in two M. abscessus strains and identified PBP sequences by proteomics. The Bocillin FL binding assay was used to determine the β-lactam concentrations that half-maximally inhibited Bocillin binding (50% inhibitory concentrations [IC50s]). Principal component analysis identified four clusters of PBP occupancy patterns. Carbapenems inactivated all PBPs at low concentrations (0.016 to 0.5 mg/liter) (cluster 1). Cephalosporins (cluster 2) inactivated PonA2, PonA1, and PbpA at low (0.031 to 1 mg/liter) (ceftriaxone and cefotaxime) or intermediate (0.35 to 16 mg/liter) (ceftazidime and cefoxitin) concentrations. Sulbactam, aztreonam, carumonam, mecillinam, and avibactam (cluster 3) inactivated the same PBPs as cephalosporins but required higher concentrations. Other penicillins (cluster 4) specifically targeted PbpA at 2 to 16 mg/liter. Carbapenems, ceftriaxone, and cefotaxime were the most promising β-lactams since they inactivated most or all PBPs at clinically relevant concentrations. These first PBP occupancy patterns in M. abscessus provide a mechanistic foundation for selecting and optimizing safe and effective combination therapies with β-lactams.Entities:
Keywords: Mycobacterium abscessuszzm321990; PbpA; PonA1; PonA2; beta-lactams; cell wall biosynthesis; drug-resistant bacteria; penicillin-binding proteins; principal component analysis; receptor binding
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Year: 2020 PMID: 33106266 PMCID: PMC7927833 DOI: 10.1128/AAC.01956-20
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.938