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. 2020 Feb 7;19(4):2449–2456. doi: 10.3892/etm.2020.8498

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Copyright: © Jiang et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Figure 2. — Biological functions of PBPs in regards to Klebsiella pneumoniae growth. (A) ELISA was used to analyze the affinity between PBPs and β-lactam antibiotic (penicillin) in vitro. (B) PBP efficiently inhibited the growth of NB-K.p and PD-K.p at a concentration of 25 mg/ml. (C) PBP expression was located on the cell surface of Klebsiella pneumonia as determined by confocal fluorescence microscope. (D) PBP treatment downregulated expression of β-lactamases. Data are presented as the mean ± SEM. ^*P<0.05, ^**P<0.01, statistically significant difference. NB-K.p, natural being Klebsiella pneumoniae; PD-K.p, Klebsiella pneumoniae from a patient with pneumonia; ESBL, extended-spectrum β-lactamase; PBPs, penicillin-binding proteins.