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Kim, Si Won; Lee, Jung Seok; Park, Seong Bin; Lee, Ae Rin; Jung, Jae Wook; Chun, Jin Hong; Lazarte, Jassy Mary S; Kim, Jaesung; Seo, Jong-Su; Kim, Jong-Hwan; Song, Jong-Wook; Ha, Min Woo; Thompson, Kim D; Lee, Chang-Ro; Jung, Myunghwan; Jung, Tae Sung
International journal of molecular sciences, 04/2020, Letnik: 21, Številka: 8Journal Article
Gram-negative bacteria have an outer membrane inhibiting the entry of antibiotics. Porins, found within the outer membrane, are involved in regulating the permeability of β-lactam antibiotics. β-lactamases are enzymes that are able to inactivate the antibacterial properties of β-lactam antibiotics. Interestingly, porins and β-lactamase are found in outer membrane vesicles (OMVs) of β-lactam-resistant and may be involved in the survival of susceptible strains of in the presence of antibiotics, through the hydrolysis of the β-lactam antibiotic. In this study, OMVs isolated from β-lactam-resistant and from mutants, lacking porin or β-lactamase, were evaluated to establish if the porins or β-lactamase in OMVs were involved in the degradation of β-lactam antibiotics. OMVs isolated from deficient in β-lactamase did not show any degradation ability against β-lactam antibiotics, while OMVs lacking OmpC or OmpF showed significantly lower levels of hydrolyzing activity than OMVs from parent . These data reveal an important role of OMVs in bacterial defense mechanisms demonstrating that the OmpC and OmpF proteins allow permeation of β-lactam antibiotics into the lumen of OMVs, and antibiotics that enter the OMVs can be degraded by β-lactamase.
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in: SICRIS
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