The use of valinomycin, nigericin and trichlorocarbanilide in control of the protonmotive force in <i>Escherichia coli</i> cells

Ahmed, Sohail; Booth, Ian R.

doi:10.1042/bj2120105

Cited by 61 publications

(46 citation statements)

References 25 publications

(27 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…(B) Same as in panel A except that DCCD (5 ,ug/ml) was added at 10 min and daptomycin (100 ,ug/ml) was added 10 min after the addition of DCCD. (17); a potassium ionophore, valinomycin (1); and nisin, a peptide antibiotic which causes nonselective ion efflux (20). The effect of daptomycin, i.e., loss of accumulated TPP+, was not seen when nigericin, an ionophore which collapses ApH (1), was tested under identical conditions.…”

mentioning

confidence: 96%

Daptomycin disrupts membrane potential in growing Staphylococcus aureus

Alborn

Allen

Preston

1991

Antimicrob Agents Chemother

190

119

View full text Add to dashboard Cite

Daptomycin (LY146032) caused a calcium-dependent dissipation of the membrane potential (At) in Staphylococcus aureus without noticeably affecting the chemical gradient (ApH) across the membrane. The effect of daptomycin on membrane energization may account for many of the inhibitory effects on macromolecular biosyntheses and membrane function reported for this antibiotic. Our evidence indicates that the bactericidal activity of daptomycin is dependent on an available At.Previous studies have demonstrated effects of daptomycin (LY146032), a calcium-requiring cyclic lipopeptide antibiotic, on both peptidoglycan synthesis and membrane integrity in gram-positive bacteria (4,7,11,12). No specific step in cell wall formation sensitive to inhibition by daptomycin has been identified, but membrane disruption as evidenced by leakage of intracellular potassium (6, 7) activity against an L form of Staphylococcus aureus (4), and the calciumdependent interaction between daptomycin analogs and phospholipid vesicles (14, 15) suggests a membrane-associated target for this antibiotic.In the present study, we examined the effects of daptomycin on membrane energetics (i.e., the electrochemical proton gradient) in S. aureus under conditions where daptomycin is bactericidal. The results of this study and a preliminary report (3) indicate that daptomycin can dissipate membrane potential (At) without affecting the chemical gradient (ApH). These findings provide, for the first time, a coherent explanation for the multiplicity of antibacterial effects attributed to this antibiotic, including inhibition of peptidoglycan biosynthesis (6 added to the upper chamber after an additional 15 min of incubation. The total volume of the reaction mix in the upper chamber was 0.5 ml; the volume of the lower chamber was 1.0 ml. Two-milliliter fractions were collected during the course of the experiment from the lower chamber at a flow rate of 2 ml/min. Radioactivity was determined from 1-ml aliquots mixed with 9 ml of Aquassure (DuPont) counted in a Beckman model LS3811 liquid scintillation counter.In some experiments, steady-state distribution data from the

show abstract

mentioning

confidence: 96%

Daptomycin disrupts membrane potential in growing Staphylococcus aureus

Alborn

Allen

Preston

1991

Antimicrob Agents Chemother

190

119

View full text Add to dashboard Cite

show abstract

“…The essential nature of the hydrophobic tail for antimicrobial activity and the overall amphiphilic structure of TriA 1 support an interaction with the bacterial membrane; therefore we examined the function of the inner membrane in detail. Bacteria use both protons and potassium ions to generate adenosine triphosphate (ATP) via the proton motive force, a process that is essential for cell growth (22,23). Other antibiotics are known to affect this vital cellular process.…”

Section: Significancementioning

confidence: 99%

Antimicrobial lipopeptide tridecaptin A₁selectively binds to Gram-negative lipid II

Cochrane

Findlay

Bakhtiary

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

109

122

View full text Add to dashboard Cite

Tridecaptin A 1 (TriA 1 ) is a nonribosomal lipopeptide with selective antimicrobial activity against Gram-negative bacteria. Here we show that TriA 1 exerts its bactericidal effect by binding to the bacterial cellwall precursor lipid II on the inner membrane, disrupting the proton motive force. Biochemical and biophysical assays show that binding to the Gram-negative variant of lipid II is required for membrane disruption and that only the proton gradient is dispersed. The NMR solution structure of TriA 1 in dodecylphosphocholine micelles with lipid II has been determined, and molecular modeling was used to provide a structural model of the TriA 1 -lipid II complex. These results suggest that TriA 1 kills Gram-negative bacteria by a mechanism of action using a lipid-II-binding motif.antibiotic | peptide | lipid II | peptidoglycan | membrane pore

show abstract

“…This organism uses both ATP (4,5,32) and Ap (4,32) to drive protein export. The proton motive force in E. coli is typically -175 to -200 mV under aerobic conditions (1,16 (25), and gramicidin inhibits the export of a glycosyltransferase in Streptococcus sanguis (18,31 (19,21,23). Proton influx in motile streptococci was directly coupled to rotation of the flagellar filament (19).…”

Section: Methodsmentioning

confidence: 99%

“…Most studies on the energetic requirements of protein secretion in bacteria have focused on Escherichia coli. This organism maintains a Ap of approximately -200 mV when grown under aerobic conditions (1,2,16). Secretion of ,B-lactamase by this organism was inhibited by 50% when the Ap was lowered to -150 mV (2).…”

mentioning

confidence: 99%

Dextransucrase secretion in Leuconostoc mesenteroides depends on the presence of a transmembrane proton gradient

Otts

Day

1988

J Bacteriol

View full text Add to dashboard Cite

The relationship between proton motive force and the secretion of dextransucrase in Leuconostoc mesenteroides was investigated. L. mesenteroides was able to maintain a constant proton motive force of -130 mV when grown in batch fermentors at pH values 5.8 to 7.0. The contribution of the membrane potential and the transmembrane pH gradient varied depending on the pH of the growth medium. The differential rate of dextransucrase secretion was relatively constant at 1,040 AmU/Amg (dry weight) when cells were grown at pH 6.0 to 6.7. Over this pH range, the internal pH was alkaline with respect to the external pH. When cells were grown at alkaline pH values, dextransucrase secretion was severely inhibited. This inhibition was accompanied by an inversion of the pH gradient as the internal pH became more acidic than the external pH. Addition of nigericin to cells at alkaline pH partially dissipated the inverted pH gradient and produced a fourfold stimulation of dextransucrase secretion. Treatment of cells with the lipophilic cation methyltriphenylphosphonium had no effect on the rate of dextransucrase secretion at pH 5.5 but inhibited secretion by 95% at pH 7.0. The reduced rate of secretion correlated with the dissipation of the proton motive force by this compound. Values of proton motive force greater than -90 mV were required for maximal rates of dextransucrase secretion. The results of this study indicate that dextransucrase secretion in L. mesenteroides is dependent on the presence of a proton gradient across the cytoplasmic membrane that is directed into the cell.Over the past 7 years, evidence has accumulated indicating a role for proton motive force (Ap) in the process of protein secretion in bacteria (2,(5)(6)(7)(8)(9)32). This requirement has been demonstrated as obligatory for the export of several proteins (2, 25) but nonessential for others (4,5). Most studies on the energetic requirements of protein secretion in bacteria have focused on Escherichia coli. This organism maintains a Ap of approximately -200 mV when grown under aerobic conditions (1, 2, 16). Secretion of ,B-lactamase by this organism was inhibited by 50% when the Ap was lowered to -150 mV (2). This level of Ap is typical for bacteria that derive their cellular energy through strictly fermentative pathways. Examples include Ap values of -120 mV for Streptococcus cremoris (29), -143 mV for Streptococcus lactis (16), and -120 mV for Clostridium thermoaceticum (3). The involvement of Ap in protein secretion in strictly fermentative bacteria has not been thoroughly examined. Do bacteria that generate relatively low levels of Ap require Ap for efficient protein secretion?To answer this question, we studied the role of Ap in dextransucrase secretion in the strictly fermentative, grampositive bacterium Leuconostoc mesenteroides. Earlier work demonstrated the inhibition of secretion of this enzyme upon treatment of cells with various ionophores (10,26). In this study, we correlated the secretion of dextransucrase with the level of Ap generated by the ...

show abstract

The use of valinomycin, nigericin and trichlorocarbanilide in control of the protonmotive force in Escherichia coli cells

Cited by 61 publications

References 25 publications

Daptomycin disrupts membrane potential in growing Staphylococcus aureus

Daptomycin disrupts membrane potential in growing Staphylococcus aureus

Antimicrobial lipopeptide tridecaptin A₁selectively binds to Gram-negative lipid II

Dextransucrase secretion in Leuconostoc mesenteroides depends on the presence of a transmembrane proton gradient

Contact Info

Product

Resources

About

The use of valinomycin, nigericin and trichlorocarbanilide in control of the protonmotive force in Escherichia coli cells

Cited by 61 publications

References 25 publications

Daptomycin disrupts membrane potential in growing Staphylococcus aureus

Daptomycin disrupts membrane potential in growing Staphylococcus aureus

Antimicrobial lipopeptide tridecaptin A1selectively binds to Gram-negative lipid II

Dextransucrase secretion in Leuconostoc mesenteroides depends on the presence of a transmembrane proton gradient

Contact Info

Product

Resources

About

Antimicrobial lipopeptide tridecaptin A₁selectively binds to Gram-negative lipid II