The affinity of β-lactamase inhibitory protein (BLIP) for TEM-1 β-lactamase has raised hopes in the challenge of proteinbased inhibitor discovery for β-lactamase-mediated antibiotic resistance. Currently, the effect of the formation of the β-lactamase:BLIP complex in vivo in β-lactam resistant bacteria is an open question. The scarcity of information to the extent to which BLIP can impair β-lactamase activity inside cells has urged us to assess the in vivo efficacy of BLIP as a potent β-lactamase inhibitor. To this end, β-lactamase and BLIP were coexpressed in Escherichia coli. Simultaneous expression of β-lactamase and BLIP and the formation of the TEM-1 β-lactamase:BLIP complex in the periplasmic space of E. coli were verified by electrophoretic and Western blot techniques. Growth profiles of the cells expressing both β-lactamase and its protein inhibitor, complemented with β-lactamase activity measurements, suggested that BLIP synthesis retarded cell growth and reduced β-lactamase activity. Although co-expression of β-lactamase and its protein inhibitor did not completely impair cell growth, the specificity of BLIP enabled it to bind β-lactamase in the bacterial periplasm, regardless of the crowding components.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.