Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria

Lugtenberg, Ben; Alphen, Loek van

doi:10.1016/0304-4157(83)90014-x

Cited by 730 publications

(509 citation statements)

References 536 publications

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“…In this model, the peptide specificity to eukaryotic or prokaryotic cells depends upon the compositional difference in the lipids of membranes (Abraham et al, 2005). As mentioned above, eukaryotic cell membranes are characterized by the zwitterionic phospholipids that contain a relatively large amount of cholesterol and sphingomyelin, while prokaryotic membranes are distinguished by the negative transmembrane potential inside (Zilberstein et al, 1979;Lugtenberg and Van Alphen, 1983). For eukaryotic cells, peptides form pores/channels in the hydrophobic core of the bilayer membranes and cause the hemolysis of erythrocytes.…”

Section: Mechanism Of Actionmentioning

confidence: 99%

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

2010

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Antimicrobial peptides (AMPs), with their extraordinary properties, such as broad-spectrum activity, rapid action and difficult development of resistance, have become promising molecules as new antibiotics. Despite their various mechanisms of action, the interaction of AMPs with the bacterial cell membrane is the key step for their mode of action. Moreover, it is generally accepted that the membrane is the primary target of most AMPs, and the interaction between AMPs and eukaryotic cell membranes (causing toxicity to host cells) limits their clinical application. Therefore, researchers are engaged in reforming or de novo designing AMPs as a 'singleedged sword' that contains high antimicrobial activity yet low cytotoxicity against eukaryotic cells. To improve the antimicrobial activity of AMPs, the relationship between the structure and function of AMPs has been rigorously pursued. In this review, we focus on the current knowledge of α-helical cationic antimicrobial peptides, one of the most common types of AMPs in nature.

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Section: Mechanism Of Actionmentioning

confidence: 99%

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

2010

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“…1D); the convex OMF contained only small IMPs. The convex OMFs of the spirochetes contained low IMP concentrations, typical of the OM of gram-negative organisms (5,19).…”

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confidence: 99%

“…Extensive OM cleavage occurs in Escherichia coli K-12 mutants deficient in OmpA and in mutants with a rough lipopolysaccharide chemotype (19). No associations have been made between specific spirochetal components and preferred fracture plane; it is interesting that these spirochetes appear to lack a typical gram-negative lipopolysaccharide (1,3,13,27,36).…”

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confidence: 99%

Analysis of outer membrane ultrastructure of pathogenic Treponema and Borrelia species by freeze-fracture electron microscopy

et al. 1991

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We analyzed the outer membrane (OM) ultrastructure of four pathogenic members of the family Spirochaetaceae by freeze fracture. The OM of Treponema pallidum subsp. pertenue contained a low intramembranous particle concentration, indicating that it contains few OM transmembrane proteins. The concave OM fracture faces of Treponema hyodysenteriae and Borrelia burgdorferi contained dense populations of particles, typical of gram-negative organisms. A relatively low concentration of particles which were evenly divided between a small and a large species was present in the concave OM fracture face of Borrelia hermsii; the convex OM fracture face contained only small particles. As for gram-negative bacteria, the convex OM fracture face particle concentrations of these pathogens were low. These spirochetes cleaved preferentially within the OM, in contrast to typical gram-negative bacteria, which tend to fracture within the inner membrane. The OM ultrastructure of T. palldum subsp. pertenue provides an explanation for the lack of antigenicity of the treponemal surface and may reflect a mechanism by which this pathogen evades the host immune response.Treponema pallidum subsp. pertenue, Treponema hyodysenteriae, Borrelia burgdorferi, and Borrelia hermsii are the etiologic agents of yaws, swine dysentery, Lyme borreliosis, and relapsing fever, respectively. Although the diseases caused by these spirochetes (family Spirochaetaceae) have been well described, research on the biology of these pathogens has been hampered by several factors. Rich, serum-containing media are required to cultivate the agents of Lyme borreliosis, relapsing fever, and swine dysentery; none of the treponemes responsible for disease in humans can be cultivated continuously in vitro. No systems for introducing DNA into members of the family Spirochaetaceae have been developed. The spirochetal outer membrane (OM) tends to be easily damaged by mild physical and chemical manipulations (3,12,14,15,27,28,32). Work with spirochetes such as Treponema pallidum subsp. pallidum, the etiologic agent of syphilis, has indicated that this fragility has not been adequately addressed by the techniques used to define the OM constituents of gram-negative bacteria (12, 26-28, 30, 38).Freeze-fracture electron microscopy has allowed examination of the ultrastructure of the OM of T. pallidum subsp. pallidum (30,38). The OM of this spirochete was shown to be unusual in that it contains a low intramembranous particle (IMP) concentration in both the concave and convex fracture faces, indicating that the OM of T. pallidum subsp. pallidum contains few transmembrane proteins (30,38). In this study, we used the techniques of freeze-fracture and freeze-etch electron microscopy to examine the OM of T. pallidum subsp. pertenue provided by Paul H. Hardy, Jr., The Johns Hopkins University School of Medicine, Baltimore, Md. The strain was cultivated by passage in New Zealand White male rabbits and harvested as previously described for T. pallidum subsp. pallidum (23). T. hyodysenteriae ...

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“…So, in vivo studies on the influence of lipopolysaccharide on the pore function of the pore proteins are mainly limited to variations in the core sugar chain of lipopolysaccharide. A structural role of lipoprotein for the assembly and/or integrity of the outer membrane has been reported [22,41] and evidence for an interaction between lipoprotein and pore protein has been presented [1,42].…”

Section: Discussionmentioning

confidence: 99%

“…Both membranes contain phospholipid and protein and in addition, the outer membrane contains lipopolysaccharide (for a review see Ref. 1).…”

Section: Introductionmentioning

confidence: 99%

Increased efficiency of the outer membrane PhoE protein pore in escherichia coli K-12 mutants with heptose-deficient lipopolysaccharide

Korteland

Lugtenberg

1984

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The pore properties of PhoE protein channels in the outer membrane of a lipoprotein-deficient mutant and in a mutant with heptose-deficient lipopolysaecharide were investigated. The absence of lipoprotein neither affects the rate of permeation of glucose 6-phosphate or of the/~-lactam antibiotic eephsulodin through the PhoE pore nor the inhibition of cephsulodin permeation by polyphosphate. In contrast, heptose deficiency results in a 6-to 8-fold increase in the rates of permeation of glucose 6-phosphate and cephsulodin. Possible explanations for these data are discussed. It is argued that the lipopolysaecharide structure synthesized under phosphate limitation may be similar to that of the heptoseless mutant and hence that not only the structure of the PhoE protein pore but also the structure of the lipopolysaecharide may promote the uptake of Pi and Pi-containing solutes under phosphate limitation.

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Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria

Cited by 730 publications

References 536 publications

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

Analysis of outer membrane ultrastructure of pathogenic Treponema and Borrelia species by freeze-fracture electron microscopy

Increased efficiency of the outer membrane PhoE protein pore in escherichia coli K-12 mutants with heptose-deficient lipopolysaccharide

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