English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

The ceftazidime-avibactam antibiotic combination was recently shown to be at risk for the emergence of resistance under treatment. To gain insight into the underlying mechanism, we have analyzed the catalytic properties of aKlebsiella pneumoniae carbapenemase type 2 (KPC-2) β-lactamase harboring the D179 Y substitution. We show that impaired inhibition by avibactam combined with significant residual activity for ceftazidime hydrolysis accounts for the resistance. In contrast, the D179 Y substitution abolished the hydrolysis of aztreonam and imipenem, indicating that these drugs might provide therapeutic alternatives.

antimicrobial agents and chemotherapy

Impaired Inhibition by Avibactam and Resistance to the Ceftazidime-Avibactam Combination Due to the D <sup>179</sup> Y Substitution in the KPC-2 β-Lactamase

Impaired Inhibition by Avibactam and Resistance to the Ceftazidime-Avibactam Combination Due to the D 179 Y Substitution in the KPC-2 β-Lactamase

Impaired Inhibition by Avibactam and Resistance to the Ceftazidime-Avibactam Combination Due to the D ¹⁷⁹ Y Substitution in the KPC-2 β-Lactamase