Mechanism of polymyxin B action and selectivity toward biologic membranes

HsuChen, Chuen-Chin; Feingold, David S.

doi:10.1021/bi00735a014

Cited by 120 publications

(63 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This lipid is absent or is present in lower concentrations in the membranes of less sensitive grampositive bacteria and mammalian cells (14,26 10, and (c) 100,ug of polymyxin B/ml 0.1 M Ca2+ containing (d) 0, (e) 10, and polymyxin B/ml. exceeded 60% (11). Increasing the i centration of methyl derivatives of lecithin) decreased PB-induced loss from liposomes.…”

Section: Discussionmentioning

confidence: 94%

See 1 more Smart Citation

Inhibition of Coccidioides immitis In Vitro and Enhancement of Anticoccidioidal Effects of Amphotericin B by Polymyxin B

Collins

Pappagianis

1975

Antimicrob Agents Chemother

View full text Add to dashboard Cite

Growth of the spherule phase of Coccidioides immitis in liquid glucose-mineral salts medium was suppressed for 13 days by 5 to 10 lg of polymyxin B per ml. Inhibition of growth was also noted when filter paper disks containing polymyxin B were placed on the surface of arthrospore-seeded defined medium solidified with refined agar. The antibiotic evidently damaged the cytoplasmic membrane inasmuch as spherules suspended in distilled water containing 10 Ag of polymyxin B per ml rapidly lost nucleotides. Leakage of nucleotides was prevented by 0.1 M Ca2+. The anticoccidioidal activity of amphotericin B (0.02 to 0.08 ,tg/ml) was enhanced by 2.5 Ag of polymyxin B per ml. Colistin (polymyxin E) methanesulfonate did not inhibit spherule growth at concentrations as high as 50 gAg/ml. This may be because colistin, though structurally similar to polymyxin B, is not cationic because its -y-amino groups are masked by methanesulfonate radicals.Depending upon the milieu, basic proteins have been shown by us to kill or inhibit the growth of the spherule phase of Coccidioides immitis in vitro (4-6). Several observations indicated that inhibition of spherule growth was a consequence of interaction between the basic proteins and the spherule surface. For example, lysozyme adsorbed from aqueous solution by formalin-killed spherules was completely eluted by washing cells with 0

show abstract

Section: Discussionmentioning

confidence: 94%

“…Cells sensitive to PB bind the peptide antibiotic to cytoplasmic membrane phospholipids (11,23). Following binding of PB, membrane permeability increases, and cytoplasmic components are lost.…”

mentioning

confidence: 99%

Inhibition of Coccidioides immitis In Vitro and Enhancement of Anticoccidioidal Effects of Amphotericin B by Polymyxin B

Collins

Pappagianis

1975

Antimicrob Agents Chemother

View full text Add to dashboard Cite

show abstract

“…Thus, our experiments reinforce the idea that the Brucella LPS is in itself an efficient shield against polycations. Other Brucella OM molecules, such as phosphatidylcholine and ornithine lipids, whose micelles are not easily disrupted by polymyxin B (11,19), either are limited to reinforcing this property or possess other functions. Similarly, Brucella OM proteins which seem to be similar to those of other proteobacteria (33,34) cannot be excluded, although their direct participation is unlikely.…”

Section: Vol 178 1996mentioning

confidence: 99%

Brucella-Salmonella lipopolysaccharide chimeras are less permeable to hydrophobic probes and more sensitive to cationic peptides and EDTA than are their native Brucella sp. counterparts

et al. 1996

View full text Add to dashboard Cite

A rough (R) Brucella abortus 45/20 mutant was more sensitive to the bactericidal activity of polymyxin B and lactoferricin B than was its smooth (S) counterpart but considerably more resistant than Salmonella montevideo. The outer membrane (OM) and isolated lipopolysaccharide (LPS) of S. montevideo showed a higher affinity for these cationic peptides than did the corresponding B. abortus OM and LPS. We took advantage of the moderate sensitivity of R B. abortus to cationic peptides to construct live R B. abortus-S-LPS chimeras to test the activities of polymyxin B, lactoferricin B, and EDTA. Homogeneous and abundant peripheral distribution of the heterologous S-LPS was observed on the surface of the chimeras, and this coating had no effect on the viability or morphology of the cells. When the heterologous LPS corresponded to the less sensitive bacterium S B. abortus S19, the chimeras were more resistant to cationic peptides; in contrast, when the S-LPS was from the more sensitive bacterium S. montevideo, the chimeras were more susceptible to the action of peptides and EDTA. A direct correlation between the amount of heterologous S-LPS on the surface of chimeric Brucella cells and peptide sensitivity was observed. Whereas the damage produced by polymyxin B in S. montevideo and B. abortus-S. montevideo S-LPS chimeras was manifested mainly as OM blebbing and inner membrane rolling, lactoferricin B caused inner membrane detachment, vacuolization, and the formation of internal electron-dense granules in these cells. Native S and R B. abortus strains were permeable to the hydrophobic probe N-phenyl-1-naphthylamine (NPN). In contrast, only reduced amounts of NPN partitioned into the OMs of the S. montevideo and B. abortus-S. montevideo S-LPS chimeras. Following peptide exposure, accelerated NPN uptake similar to that observed for S. montevideo was detected for the B. abortus-S. montevideo LPS chimeras. The partition of NPN into native or EDTA-, polymyxin B-, or lactoferricin B-treated LPS micelles of S. montevideo or B. abortus mimicked the effects observed with intact cells, and this was confirmed by using micelle hybrids of B. abortus and S. montevideo LPSs. The results showed that LPS is the main cause of B. abortus' resistance to bactericidal cationic peptides, the OM-disturbing action of divalent cationic chelants, and OM permeability to hydrophobic substances. It is proposed that these three features are related to the ability of Brucella bacteria to multiply within phagocytes.The genus Brucella comprises gram-negative, facultative intracellular pathogens that produce disease in a large number of mammals, including humans (8). The outer membrane (OM) of Brucella organisms shares many structural features with the OM of their close relatives in the genera Ochrobactrum, Bartonella, Agrobacterium, Rhizobium, and Phyllobacterium, all of which are eukaryotic-cell-associated ␣-2 proteobacteria (27, 31). However, the Brucella OM differs from that of other pathogenic groups (6,(25)(26)(27), including several facultative in...

show abstract

“…Several investigators have proposed that the mode of action of bactericidal agents derived from granulocytes (5,6), or other sources (7,8), may include effects on permeability. In some instances an effect on phospholipids has been invoked (7,9).…”

Section: Introductionmentioning

confidence: 99%

Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli.

Weiss¹,

Franson²,

Beckerdite³

et al. 1975

J. Clin. Invest.

115

View full text Add to dashboard Cite

Mechanism of polymyxin B action and selectivity toward biologic membranes

Cited by 120 publications

References 23 publications

Inhibition of Coccidioides immitis In Vitro and Enhancement of Anticoccidioidal Effects of Amphotericin B by Polymyxin B

Inhibition of Coccidioides immitis In Vitro and Enhancement of Anticoccidioidal Effects of Amphotericin B by Polymyxin B

Brucella-Salmonella lipopolysaccharide chimeras are less permeable to hydrophobic probes and more sensitive to cationic peptides and EDTA than are their native Brucella sp. counterparts

Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli.

Contact Info

Product

Resources

About