Interaction of antimicrobial peptide s-thanatin with lipopolysaccharide in vitro and in an experimental mouse model of septic shock caused by a multidrug-resistant clinical isolate of Escherichia coli

Wu, Guoqiu; Fan, Xuetong; Li, Linxian; Wang, Hailiang; Ding, Jinfeng; Wu, Hongbin; Zhao, Rui; Gou, Lantu; Shen, Zancong; Xi, Tao

doi:10.1016/j.ijantimicag.2009.11.009

Cited by 37 publications

(34 citation statements)

References 27 publications

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“…Both steps are necessary for this interaction [4]. Beside the LPS-binding capacity, the cytokine decrease may be partly explained by better bacterial clearance in blood and organ tissue after administration of AMP as demonstrated previously [17,18]. …”

Section: Discussionmentioning

confidence: 81%

The anti-inflammatory effect of the synthetic antimicrobial peptide 19-2.5 in a murine sepsis model: a prospective randomized study

et al. 2013

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IntroductionIncreasing rates of multi-resistant bacteria are a major problem in the treatment of critically ill patients. Furthermore, conventional antibiotics lead to the release of bacterial derived membrane parts initiating pro-inflammatory cascades with potential harm to the patient. Antimicrobial peptides (AMP) may kill bacteria without releasing pro-inflammatory factors. Thus, we compared three newly developed synthetic anti-lipopolysaccharide peptides (SALPs) with a broader range of efficacy to suppress cytokine release in plasma and CD14 mRNA expression in organ tissue in a murine, polymicrobial sepsis model.MethodsA randomized, experimental trial was conducted in an animal research facility. Male NMRI mice (n = 90; 8- to 12-weeks old) were randomized to the following six groups: (i) sham operation and parenteral vehicle (NaCl 0.9%) administration (sham); (ii) cecal ligation and puncture (CLP) and vehicle infusion (sepsis-control), (iii) CLP and polymyxin B infusion (polyB), or (iv to vi) CLP and infusion of three different synthetic antimicrobial peptides Peptide 19-2.5 (Pep2.5), Peptide 19-4 (Pep4) or Peptide 19-8 (Pep8). All animals underwent arterial and venous catheterization for hemodynamic monitoring 48 hours prior to CLP or sham-operation. Physical appearance and behavior (activity), plasma cytokine levels, and CD14 mRNA expression in heart, lung, liver, spleen and kidney tissue were determined 24 hours after CLP or sham operation.ResultsOnly Pep2.5 significantly enhanced the activity after CLP, whereas none of the therapeutic regimens elevated the mean arterial pressure or heart rate. The strongly elevated IL-6, IL-10 and monocyte chemoattractant protein serum levels in septic animals were significantly reduced after Pep2.5 administration (P < 0.001, P < 0.001, and P < 0.001, respectively). Similarly, Pep2.5 significantly reduced the sepsis-induced CD14 mRNA expression in heart (P = 0.003), lung (P = 0.008), and spleen tissue (P = 0.009) but not in kidney and liver.ConclusionsStructurally variable SALPs exhibit major differences in their anti-inflammatory effect in vivo. Continuous parenteral administration of Pep2.5 is able to reduce sepsis-induced cytokine release and tissue inflammation.

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Section: Discussionmentioning

confidence: 81%

The anti-inflammatory effect of the synthetic antimicrobial peptide 19-2.5 in a murine sepsis model: a prospective randomized study

et al. 2013

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“…15 reported that LL-37 and β-sheet peptide hBD-3 displayed anti-inflammatory activities when applied individually and synergistically to a three-dimensional co-culture model of gingival epithelial cells and fibroblasts 15 . Due to their small sizes (<30 amino acid residues) and excellent binding ability to the lipid bilayer of bacterial membranes, β-sheet AMPs such as s-thanatin are also well-established as promising candidates for the treatment of multidrug-resistant bacterial infections and neutralization of LPS 16, 17 .…”

Section: Introductionmentioning

confidence: 99%

Antibacterial and detoxifying activity of NZ17074 analogues with multi-layers of selective antimicrobial actions against Escherichia coli and Salmonella enteritidis

Yang

Liu

Teng

et al. 2017

Sci Rep

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NZ17074 (N1), an arenicin-3 derivative isolated from the lugworm, has potent antibacterial activity and is cytotoxic. To reduce its cytotoxicity, seven N1 analogues with different structures were designed by changing their disulfide bonds, hydrophobicity, or charge. The “rocket” analogue-N2 and the “kite” analogue-N6 have potent activity and showed lower cytotoxicity in RAW264.7 cells than N1. The NMR spectra revealed that N1, N2, and N6 adopt β-sheet structures stabilized by one or two disulfide bonds. N2 and N6 permeabilized the outer/inner membranes of E. coli, but did not permeabilize the inner membranes of S. enteritidis. N2 and N6 induced E. coli and S. enteritidis cell cycle arrest in the I-phase and R-phase, respectively. In E. coli and in S. enteritidis, 18.7–43.8% of DNA/RNA/cell wall synthesis and 5.7–61.8% of DNA/RNA/protein synthesis were inhibited by the two peptides, respectively. Collapsed and filamentous E. coli cells and intact morphologies of S. enteritidis cells were observed after treatment with the two peptides. Body weight doses from 2.5–7.5 mg/kg of N2 and N6 enhanced the survival rate of peritonitis- and endotoxemia-induced mice; reduced the serum IL-6, IL-1β and TNF-α levels; and protected mice from lipopolysaccharide-induced lung injury. These data indicate that N2 and N6, through multiple selective actions, may be promising dual-function candidates as novel antimicrobial and anti-endotoxin peptides.

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“…The Pichia pastoris expression system has been an efficient and economical way to get heterologous protein [Lv et al, 2013;Tang et al, 2012], and effects of different AMPs on animals have been previously reported [Ohh et al, 2010;Wu et al, 2010;Yang et al, 2006]. In the present study, the antiparallel dimer of PMAP-36 was expressed in the P. pastoris system.…”

Section: Introductionmentioning

confidence: 80%

In vitro and in vivo Activity of the Dimer of PMAP-36 Expressed in <b><i>Pichia pastoris</i></b>

Wang¹,

Zhang²,

Jia³

et al. 2014

Microb Physiol

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The antimicrobial peptide PMAP-36 exists as a homodimer stabilized by an intermolecular disulfide bridge. The dimer of PMAP-36 exhibits a potent and rapid microbicidal activity against a wide spectrum of microorganisms. The gene encoding the antiparallel dimer (PMAP-36)₂ was designed and codon-optimized according to bias of Pichia pastoris. The gene was then expressed in the P. pastoris strain GS115. The concentration of the recombinant product reached 106 mg/l. In vitro activity assays indicated that the recombinant peptide showed antimicrobial activities against Gram-positive and Gram-negative bacteria but did not cause hemolysis of chicken erythrocytes. Subsequently, 120 7-day-old male Arbor Acres broilers were used to evaluate the in vivo activities of the peptide. A prophylactic dose of ciprofloxacin lactate was supplemented as the control. The results showed that recombinant (PMAP-36)₂ significantly increased the serum IgM content of the birds (p < 0.05). The recombinant peptide significantly increased the amounts of Bifidobacterium and decreased the amount of Escherichia coli cells in the ceca of the experimental birds (p < 0.05). The results obtained in the present study indicate that the recombinant (PMAP-36)₂ has a potent in vitro and in vivo activity and can be used as an alternative to antibiotic treatment.

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Interaction of antimicrobial peptide s-thanatin with lipopolysaccharide in vitro and in an experimental mouse model of septic shock caused by a multidrug-resistant clinical isolate of Escherichia coli

Cited by 37 publications

References 27 publications

The anti-inflammatory effect of the synthetic antimicrobial peptide 19-2.5 in a murine sepsis model: a prospective randomized study

The anti-inflammatory effect of the synthetic antimicrobial peptide 19-2.5 in a murine sepsis model: a prospective randomized study

Antibacterial and detoxifying activity of NZ17074 analogues with multi-layers of selective antimicrobial actions against Escherichia coli and Salmonella enteritidis

In vitro and in vivo Activity of the Dimer of PMAP-36 Expressed in <b><i>Pichia pastoris</i></b>

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