Molecular biology of development

Neyfakh, Alexander A.; Timofeeva, M. Ya.

doi:10.1007/978-1-4899-5370-4

Cited by 3 publications

(3 citation statements)

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“…Altogether, these results indicate that the antibiotic specificity of LmrP includes lincosamides, 14-and 15-membered macrolides, streptogramins and the tetracycline class of antibiotics. Unlike other secondary multidrug transporters, such as AcrAB, Bmr, MdfA, MexAB, NorA, NorM and Tap, LmrP did not confer resistance to aminoglycosides, β-lactam antibiotics, quinolones or chloramphenicol (Yoshida et al, 1990 ;Neyfakh, 1992 ;Li et al, 1995 ;Edgar & Bibi, 1997 ;Aı! nsa et al, 1998 ;Morita et al, 1998 ;.…”

Section: Discussionmentioning

confidence: 98%

The lactococcal secondary multidrug transporter LmrP confers resistance to lincosamides, macrolides, streptogramins and tetracyclines

et al. 2001

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The active efflux of toxic compounds by (multi)drug transporters is one of the mechanisms that bacteria have developed to resist cytotoxic drugs. The authors describe the role of the lactococcal secondary multidrug transporter LmrP in the resistance to a broad range of clinically important antibiotics. Cells expressing LmrP display an increased resistance to the lincosamide, streptogramin, tetracycline and 14-and 15-membered macrolide antibiotics. The streptogramin antibiotic quinupristin, present in the fourth-generation antibiotic RP 59500, can inhibit LmrP-mediated Hoechst 33342 transport, but is not transported by LmrP, indicating that quinupristin acts as a modulator of LmrP activity. LmrP-expressing Lactococcus lactis cells in which a protonmotive force is generated accumulate significantly less tetracycline than control cells without LmrP expression. In contrast, LmrP-expressing and control cells accumulate equal amounts of tetracycline in the absence of metabolic energy. These findings demonstrate that the increased antibiotic resistance in LmrP-expressing cells is a result of the active extrusion of antibiotics from the cell.

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Section: Discussionmentioning

confidence: 98%

The lactococcal secondary multidrug transporter LmrP confers resistance to lincosamides, macrolides, streptogramins and tetracyclines

et al. 2001

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“…Since these mutations did not affect the sensitivity of Bmr to rescinnamine, a close structural analog of reserpine, it seems likely that Val-286 does not play a direct role in inhibitor recognition but may instead form part of a reserpine-binding "pocket" (2). Further mutational analysis of Bmr has indicated that mutations in TMS 4, 7, 9, 10, and 11 affect the spectrum of cross-resistance to various drugs (186).…”

Section: Bmr Blt and Nora 12-tms Multidrug Efflux Proteinsmentioning

confidence: 99%

“…In particular exporters, mutagenesis has identified specific residues implicated in substrate specificity. In most cases, the residues potentially involved in substrate binding are located within predicted transmembrane regions; for instance, in the MFS proteins, substitutions at Asp-323 (TMS 10) in QacA (205), Val-286 (TMS 9) (2) and within TMS 4, 7, and 9 to 11 (186) in Bmr, and Ala-362 (TMS 12) in NorA (126,201) all alter substrate specificity (see above for details and discussion of roles of specific residues). Such studies have yet to provide a clear picture of the molecular basis of the broad substrate specificity of such multidrug efflux proteins.…”

Section: Molecular Basis Of Broad Substrate Specificitymentioning

confidence: 99%