Abstract：
: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 Escherichia coli and may be involved in the survival of susceptible strains of E. coli in the presence of antibiotics, through the hydrolysis of the β-lactam antibiotic. In this study, OMVs isolated from β-lactam-resistant E. coli 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 E. coli 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 E. coli. 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.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Kim SW,Lee JS,Park SB,Lee AR,Jung JW,Chun JH,Lazarte JMS,Kim J,Seo JS,Kim JH,Song JW,Ha MW,Thompson KD,Lee CR,Jung M,Jung TSdoi
10.3390/ijms21082822subject
Has Abstractpub_date
2020-04-17 00:00:00issue
8issn
1422-0067pii
ijms21082822journal_volume
21pub_type
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