Polymyxin B binding sites in Escherichia coli as revealed by polymyxin B-gold labeling.

Morioka, Hiroyljki; Tachibana, Masayoshi; Machino, Mitsuo; Suganuma, A

doi:10.1177/35.2.3025293

Cited by 11 publications

(9 citation statements)

References 11 publications

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“…Polymyxin B is a cationic cyclic lipopeptide known to inhibit LPS activity. This inhibition results from the binding of polymyxin B to the lipid A of LPS (24). As previously shown for B. burgdorferi OspA and OspB (21), polymyxin B treatment had no effect on the spiralin mitogenic effect, which was expected because of the very high purity of spiralin.…”

supporting

confidence: 67%

Spiralin, a mycoplasmal membrane lipoprotein, induces T-cell-independent B-cell blastogenesis and secretion of proinflammatory cytokines

et al. 1997

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Mycoplasmas are bacteria which can cause respiratory, arthritic, and urogenital diseases. During the early phase of infection, mycoplasmas usually induce an inflammatory response and a humoral response preferentially directed against their membrane-bound, surface-exposed lipoproteins. In this report, we describe the effects on immune cells of spiralin, a well-characterized mycoplasmal lipoprotein. Purified spiralin stimulated the in vitro proliferation of human peripheral blood mononuclear cells and murine splenocytes. The stimulation pathway was probably different from that followed by Escherichia coli lipopolysaccharide because the effect of spiralin was not abolished by polymyxin B. Comparison of the effects of whole, native spiralin with those induced by proteinase K-digested spiralin or by the C-terminal half of spiralin (peptide p[13.5] T) revealed that the first half of the protein, which contains the lipoylated N terminus, is responsible for the mitogenic activity. In contrast to whole spiralin, proteinase K-digested spiralin did not trigger murine B-cell differentiation and immunoglobulin G and M secretion. Stimulation of human or murine immune cells led to early secretion of proinflammatory cytokines (human tumor necrosis factor alpha and murine interleukin 1 or 6). Spiralin induced the T-cell-independent blastogenesis of murine B cells but did not stimulate T cells. Altogether, our data demonstrate that spiralin possesses potent immunostimulating activity, similar to that reported for lipoproteins of pathogenic gracilicutes (gram-negative eubacteria; e.g., Borrelia burgdorferi OspA and E. coli Braun lipoprotein), and are consistent with the fact that lipoproteins are major antigens during mycoplasma infections.

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confidence: 67%

Spiralin, a mycoplasmal membrane lipoprotein, induces T-cell-independent B-cell blastogenesis and secretion of proinflammatory cytokines

et al. 1997

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“…As the lipid A moiety is composed of a phosphorylated diglucosamine backbone and fatty acids, we therefore looked for the residues of the lipid A moiety that were implicated in binding of hemoglobin. Incubation of A. pleuropneumoniae lipid A with polymyxin B, which is known to interact with the lipid A-KDO (3-deoxy-D-manno-octulosonic acid) region of LPS (21), completely inhibited pig hemoglobin binding. Fatty acids constituting the lipid A of A. pleuropneumoniae serotype 1, namely, dodecanoic acid, tetradecanoic acid, 3-hydroxytetradecanoic acid, hexadecanoic acid, and octadecanoic acid, were able to bind pig hemoglobin in a dot binding assay.…”

Section: Discussionmentioning

confidence: 99%

Lipopolysaccharides of Actinobacillus pleuropneumoniae bind pig hemoglobin

1995

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A previous study indicated that lipopolysaccharides (LPS) extracted from Actinobacillus pleuropneumoniae bind two low-molecular-mass proteins, of approximately 10 and 11 kDa, present in porcine respiratory tract secretions (M. Bélanger, D. Dubreuil, and M. Jacques, Infect. Immun. 62:868-873, 1994). In the present study, we determined the N-terminal amino acid sequences of these two proteins, which revealed high homology with the ␣ and ␤ chains of pig hemoglobin. Some isolates of A. pleuropneumoniae were able to use hemoglobin from various animal species as well as other heme compounds as sole sources of iron for growth, while other isolates were unable to use them. Immunoelectron microscopy showed binding of pig hemoglobin at the surface of all A. pleuropneumoniae isolates as well as labeling of outer membrane blebs. We observed, using Western blotting (immunoblotting), that the lipid A-core region of LPS of all isolates was binding pig hemoglobin. Furthermore, lipid A obtained after acid hydrolysis of LPS extracted from A. pleuropneumoniae was able to bind pig hemoglobin and this binding was completely abolished by preincubation of lipid A with polymyxin B but was not inhibited by preincubation with glucosamines. Fatty acids constituting the lipid A of A. pleuropneumoniae, namely, dodecanoic acid, tetradecanoic acid, 3-hydroxytetradecanoic acid, hexadecanoic acid, and octadecanoic acid, were also binding pig hemoglobin. Our results indicate that LPS of all A. pleuropneumoniae isolates tested bind pig hemoglobin and that lipid A is involved in this binding. Our results also indicate that some A. pleuropneumoniae isolates are, in addition, able to use hemoglobin for growth. Binding of hemoglobin to LPS might represent an important means by which A. pleuropneumoniae acquires iron in vivo from hemoglobin released from erythrocytes lysed by the action of its hemolysins.

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“…18 ) It is of great interest that the drugs that affect the state of the cell wall or membrane exhibit parallel shifts in the patterns of microbial growth thermograms, as observed in this study, being different from in the cases of cultures with some other drugs like chloramphenicol, streptomycin and tetracycline.! )…”

Section: Methodsmentioning

confidence: 63%

Calorimetric Analysis of the Effects of Penicillin G, Ampicillin and Polymyxin B on the Growth ofEscherichia coli

Katarao

Okuno

Takahashi

1988

Agricultural and Biological Chemistry

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Polymyxin B binding sites in Escherichia coli as revealed by polymyxin B-gold labeling.

Cited by 11 publications

References 11 publications

Spiralin, a mycoplasmal membrane lipoprotein, induces T-cell-independent B-cell blastogenesis and secretion of proinflammatory cytokines

Spiralin, a mycoplasmal membrane lipoprotein, induces T-cell-independent B-cell blastogenesis and secretion of proinflammatory cytokines

Lipopolysaccharides of Actinobacillus pleuropneumoniae bind pig hemoglobin

Calorimetric Analysis of the Effects of Penicillin G, Ampicillin and Polymyxin B on the Growth ofEscherichia coli

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