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Volume 26, Number 4—April 2020
Research Letter

Novel Rapid Test for Detecting Carbapenemase

Yanfang Feng1, Akilan Palanisami1, Jerrin Kuriakose, Michael Pigula, Shoaib Ashraf, and Tayyaba HasanComments to Author 
Author affiliations: Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, USA (Y. Feng, A. Palanisami, J. Kuriakose, M. Pigula, S. Ashraf, T. Hasan); Harvard-MIT Health Sciences and Technology, Cambridge, Massachusetts, USA (T. Hasan)

Main Article

Figure

Schematic illustration of the principle of fluorescence identification of β-lactamase activity. A). The β-lactamase–activated fluorophore probe comprises a cleavable β-lactam core conjugated to 2 fluorophores (circled) that are quenched because of close proximity. This construct was designed to mimic the enzymatic degradation properties of easily cleavable β-lactam antimicrobial drugs. When this probe is attacked by β-lactamase, the probe core is cleaved, leading to the separation of the fluorop

Figure. Schematic illustration of the principle of fluorescence identification of β-lactamase activity. A). The β-lactamase–activated fluorophore probe comprises a cleavable β-lactam core conjugated to 2 fluorophores (circled) that are quenched because of close proximity. This construct was designed to mimic the enzymatic degradation properties of easily cleavable β-lactam antimicrobial drugs. When this probe is attacked by β-lactamase, the probe core is cleaved, leading to the separation of the fluorophores and the recovery of their fluorescent properties (fluorescent state). B) Assay profile for carbapenemase-producing bacteria. C) Assay profile for non–carbapenemase-producing bacteria. Black, quenched fluorophore; blue, unquenched fluorophore turning fluorescent; green, β-lactam core; red, imipenem; purple, β-lactamase. β-LEAF, β-lactamase enzyme–activated fluorophore.

Main Article

1These authors contributed equally to this article.

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