Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A

Srimal, Subita; Surolia, Namita; Balasubramanian, Sathyamangalam V.; Surolia, Avadhesha

doi:10.1042/bj3150679

Cited by 149 publications

(173 citation statements)

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“…Third, Ig production induced by LPS or rHRF showed different patterns: rHRF induced higher levels of IgM than LPS did, but to a lesser extent in the cases of IgG and IgA. Fourth, PMB which neutralizes the biological activity of LPS (26,27), reduced LPS effects on Ig production (Table I) and MHC class II expression (Fig. 5), but did not have any effect on rHRF activity.…”

Section: Discussionmentioning

confidence: 99%

“…The effects of LPS on MHC class II expression were abolished by PMB (Fig. 5AI), a cyclic cationic peptide antibiotic that neutralizes the biological activity of LPS (26,27), but those of rHRF were not affected by PMB (Fig. 5AII), suggesting that the effects of rHRF are different from those of LPS.…”

Section: Effects Of Hrf On the Proliferation And Ig Production Of B Cmentioning

confidence: 99%

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Molecular Identification of IgE-Dependent Histamine-Releasing Factor as a B Cell Growth Factor

Kang

Lee

Song

et al. 2001

The Journal of Immunology

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The culture supernatants of LK1 cells, murine erythroleukemia cells, showed B cell-stimulating activity. Purification and NH2-terminal sequence analysis revealed that one of the candidates was murine IgE-dependent histamine-releasing factor (IgE-HRF), which is known to induce histamine from basophils. Recombinant IgE-HRF (rHRF) obtained from Escherichia coli- or 293-transformed embryonal kidney cells was tested for B cell-stimulating activity. Both rHRFs stimulated B cell proliferation in a dose-dependent manner. However, boiling or anti-HRF Ab abolished the B cell stimulatory effects of rHRF. Recombinant HRF showed strong synergistic effects with IL-2, IL-4, and IL-5 for B cell activation, with maximal activity in the presence of anti-CD40 Ab. Recombinant HRF increased MHC class II expression of B cells. It also increased Ig production from B cells. Treatment with polymyxin B, a neutralizing peptide antibiotic of LPS, did not reduce the activity of rHRF. In addition, FACS analysis using PE-conjugated rHRF showed that HRF bound to B cells. Recombinant HRF up-regulated the expression of IL-1 and IL-6 in B cells. In vivo administration of rHRF or the cDNA for rHRF increased total and Ag-specific Ig synthesis. Taken together, these results indicate that HRF stimulates B cell activation and function.

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Section: Discussionmentioning

confidence: 99%

Section: Effects Of Hrf On the Proliferation And Ig Production Of B Cmentioning

confidence: 99%

Molecular Identification of IgE-Dependent Histamine-Releasing Factor as a B Cell Growth Factor

Kang

Lee

Song

et al. 2001

The Journal of Immunology

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“…The thermodynamics of polymyxin B binding to LPS have been investigated previously using isothermal titration calorimetry by the group of Surolia (34). In these studies, a highly processed LPS preparation from E. coli was used (extensive treatments with proteases, chelating agents, and purifications via dialysis and size exclusion chromatography).…”

Section: Discussionmentioning

confidence: 99%

Isolation, Structural Characterization, and Properties of Mattacin (Polymyxin M), a Cyclic Peptide Antibiotic Produced byPaenibacillus kobensis M

Martin

Moake

et al. 2003

Journal of Biological Chemistry

104

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Mattacin is a nonribosomally synthesized, decapeptide antibiotic produced by Paenibacillus kobensis M. The producing strain was isolated from a soil/manure sample and identified using 16 S rRNA sequence homology along with chemical and morphological characterization. An efficient production and isolation procedure was developed to afford pure mattacin. Structure elucidation using a combination of chemical degradation, multidimensional NMR studies (COSY, HMBC, HMQC, ROESY), and mass spectrometric (MALDI MS/MS) analyses showed that mattacin is identical to polymyxin M, an uncommon antibiotic reported previously in certain Bacillus species by Russian investigators. Mattacin (polymyxin M) is cyclic and possesses an amide linkage between the C-terminal threonine and the side chain amino group of the diaminobutyric acid residue at position 4. It contains an (S)-6-methyloctanoic acid moiety attached as an amide at the N-terminal amino group, one D-leucine, six L-␣,␥-diaminobutyric acid, and three L-threonine residues. Transfer NOE experiments on the conformational preferences of mattacin when bound to lipid A and microcalorimetry studies on binding to lipopolysaccharide showed that its behavior was very similar to that observed in previous studies of polymyxin B (a commercial antibiotic), suggesting an identical mechanism of action. It was capable of inhibiting the growth of a wide variety of Gram-positive and Gramnegative bacteria, including several human and plant pathogens with activity comparable with purified polymyxin B. The biosynthesis of mattacin was also examined briefly using transpositional mutagenesis by which 10 production mutants were obtained, revealing a set of genes involved in production.

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“…Concentrations of the peptides were determined by amino acid analysis using Waters Pico-Tag TM systems, whereas that of PMB and PMBN were determined by molar absorbance and weight, respectively (11).…”

Section: Methodsmentioning

confidence: 99%

“…Isothermal Titration Calorimetry-A typical titration involved 15-20 injections at 3-min intervals, 4-l aliquots of peptide solution into the sample cell (volume 1.344 ml) containing lipid A (50 M), conducted on an OMEGA microcalorimeter of MicroCal, Inc. (11). The titration cell was stirred continuously at 400 rpm.…”

Section: Preparation Of Liposomes Monolayer Deposition On Alkanethiomentioning

confidence: 99%

Surface Plasmon Resonance Studies Resolve the Enigmatic Endotoxin Neutralizing Activity of Polymyxin B

Thomas¹,

Surolia²,

Surolia³

1999

Journal of Biological Chemistry

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Polymyxin B (PMB), a cyclic cationic peptide antibiotic, despite its severe side effects continues to occupy a premiere position for treating endotoxicosis. Its mode of neutralization of endotoxin has remained elusive for the last three decades. Several synthetic peptide mimics of PMB, capable of binding endotoxin, have been made. However, the binding ability alone appears to be a deceptive indicator of endotoxin neutralizing activity as molecules with similar binding propensities could either sequester or opsonize the toxin. Hence identification of additional physical parameters which describe adequately the outcome of PMB-endotoxin interaction become imperative. Surface plasmon resonance (SPR) studies reported here show that several mimics of PMB despite exhibiting lipopolysaccharide binding affinities comparable with it but, unlike it, do not sequester the endotoxin. These studies thus provide a striking illustration of the difference in the behavior of PMB, vis a vis its mimics toward the endotoxin lamellae, and define further, in chemical terms, mechanism of the action of PMB and allow us to posit that the design of molecules as effective antidotes for sepsis should incorporate the ability to sequester endotoxin specifically.Release of miniscule (nanomolar) quantities of lipopolysaccharide (LPS), 1 the major structural component of the Gramnegative bacterial outer membrane, in systemic bacterial infections frequently leads to a relatively common but often fatal constellation of symptoms termed as the endotoxic shock (1, 2). The treatment for endotoxic shock which is characterized by deranged hemodynamics, coagulation abnormalities, and multiple system organ failure, continues to remain nonspecific and supportive because of the absence of specific interventional strategies (3). However, the mechanisms by which endotoxin (LPS) acts on the target cells are increasingly being understood, which in turn has led to the development of several experimental approaches for treating endotoxicosis. These include sequestration of LPS by peptides or anti-LPS antibodies (4 -7), use of its antagonistic homologs that prevent its binding to the target cells (8), or the molecules that abrogate signaling to the pathways leading to the production of inflammatory cytokines such as tumor necrosis factor, interleukin-1, etc. (9). Despite these many interventional modalities and the severe side effects associated with the use of polymyxin B (PMB), a cyclic cationic peptide antibiotic, for the treatment of endotoxicosis, it continues to occupy the premiere position in our armamentarium for combating endotoxicosis (3, 4). Only recently have its mode of interaction with LPS and the structural features involved therein been elucidated (6, 10 -12). These and earlier studies have led to the proposal that the asymmetric distribution of the basic and nonpolar groups in polymyxin B impart to it an amphiphilicity that is both necessary and sufficient for its LPS neutralizing activity. That this is indeed the case was proven by a subsequent st...

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Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A

Cited by 149 publications

References 50 publications

Molecular Identification of IgE-Dependent Histamine-Releasing Factor as a B Cell Growth Factor

Molecular Identification of IgE-Dependent Histamine-Releasing Factor as a B Cell Growth Factor

Isolation, Structural Characterization, and Properties of Mattacin (Polymyxin M), a Cyclic Peptide Antibiotic Produced byPaenibacillus kobensis M

Surface Plasmon Resonance Studies Resolve the Enigmatic Endotoxin Neutralizing Activity of Polymyxin B

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