Cecropin-like antimicrobial peptide protects mice from lethal E.coli infection

Shrestha, Anishma; Duwadi, Deepesh; Jukosky, James A.; Fiering, Steven

doi:10.1371/journal.pone.0220344

Cited by 12 publications

(10 citation statements)

References 47 publications

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“…However, some studies have shown the potential of these peptides in vivo. For example, single intraperitoneal administrations of H. cecropia Cecs A and B, and Danaus plexipibus DAN2 decreased mortality in acutely E. coli -infected rodent models [114,130]. In addition, mice subjected to DAN2 doses two-fold higher than their most effective antibacterial concentration did not display any behavioral or morphological abnormalities, demonstrating in vivo that these peptides lack toxic effects after acute treatments [130].…”

Section: Health Benefits Of Natural Cecs and Synthetic Cec-analogsmentioning

confidence: 99%

Insect Cecropins, Antimicrobial Peptides with Potential Therapeutic Applications

Brady

Grapputo

Romoli

et al. 2019

IJMS

129

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The alarming escalation of infectious diseases resistant to conventional antibiotics requires urgent global actions, including the development of new therapeutics. Antimicrobial peptides (AMPs) represent potential alternatives in the treatment of multi-drug resistant (MDR) infections. Here, we focus on Cecropins (Cecs), a group of naturally occurring AMPs in insects, and on synthetic Cec-analogs. We describe their action mechanisms and antimicrobial activity against MDR bacteria and other pathogens. We report several data suggesting that Cec and Cec-analog peptides are promising antibacterial therapeutic candidates, including their low toxicity against mammalian cells, and anti-inflammatory activity. We highlight limitations linked to the use of peptides as therapeutics and discuss methods overcoming these constraints, particularly regarding the introduction of nanotechnologies. New formulations based on natural Cecs would allow the development of drugs active against Gram-negative bacteria, and those based on Cec-analogs would give rise to therapeutics effective against both Gram-positive and Gram-negative pathogens. Cecs and Cec-analogs might be also employed to coat biomaterials for medical devices as an approach to prevent biomaterial-associated infections. The cost of large-scale production is discussed in comparison with the economic and social burden resulting from the progressive diffusion of MDR infectious diseases.

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Section: Health Benefits Of Natural Cecs and Synthetic Cec-analogsmentioning

confidence: 99%

Insect Cecropins, Antimicrobial Peptides with Potential Therapeutic Applications

Brady

Grapputo

Romoli

et al. 2019

IJMS

129

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“…Members of the cecropin family typically have peptide chains consisting of 31-39 amino acids and possess broad-spectrum antimicrobial activities (Brady et al, 2019). Several studies have shown that cecropin, when used as a feed additive, can increase the performance of livestock and poultry while also protecting them from lethal pathogen infections (Wen and He, 2012;Wu et al, 2012;Xiao et al, 2015;Shrestha et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Insight Into the Effects of Nisin and Cecropin on the Oral Microbial Community of Rats by High-Throughput Sequencing

Ran

et al. 2020

Front. Microbiol.

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The oral microbiome has major impacts on oral health and disease. Antimicrobial peptides (AMPs), such as nisin and cecropin, have been widely used as food preservatives or feed additives, and are thus inevitably ingested by consumers through their oral cavity. However, as broad-spectrum antimicrobial reagents, the effect of AMPs on the oral microbiome of consumer's remains poorly characterized. In this study, we performed 16S rDNA high-throughput sequencing to investigate the effect of nisin and cecropin on the oral microbiomes of rats. Our results suggest that although nisin and cecropin have different effects on the oral microbiome of rats, both AMPs impact the composition of oral microbial communities at the phylum and genus levels. Cecropin significantly reduced the diversity and richness of rat oral microbial communities. Notably, the relative abundance of the pathogen Acinetobacter baumannii increased in the oral microbial community of rats fed cecropin-containing feed. In addition, nisin significantly reduced the amount of secretory immunoglobulin A in the saliva of rats.

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“…Analyses using the ExPASy ProtParam [30] tool indicate that serrulin is, like other AMPs, a cationic molecule, containing a positive charge (+4) (Figure S3). Generally, cationic antimicrobial peptides act on the membrane of microorganisms by an electrostatic difference [31], but there are AMPs that act internally and can interact on ribosome, internal proteins, or nucleic acids (DNA or RNA) [32,33,34]. Like ctenidins and acanthoscurrins, the mechanism of action of serrulin was not identified in this work, so it is not possible to compare its characteristics with those of similar molecules.…”

Section: Resultsmentioning

confidence: 99%

Serrulin: A Glycine-Rich Bioactive Peptide from the Hemolymph of the Yellow Tityus serrulatus Scorpion

Oliveira

Silva

2019

Toxins

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Antimicrobial peptides (AMPs) are small molecules, which have a potential use as antibiotic or pharmacological tools. In chelicerate organisms, such as scorpions, these molecules constitute an alternative defense system against microorganisms. The aim of this work was to identify AMPs in the hemolymph of the Tityus serrulatus scorpion. Fractions of plasma and hemocytes were subjected to high-performance liquid chromatography (HPLC) and then analyzed to determine their activity in inhibiting microbial growth. One of the fractions from the hemocytes presents antimicrobial activity against microorganisms, such as Gram-negative and Gram-positive bacteria, fungi, and yeast. These fractions were analyzed by mass spectrometry, and a fragment of 3564 Da. was identified. The peptide was called serrulin, because it is derived from the species T. serrulatus. A comparison of the amino acid sequence of serrulin with databases shows that it has a similarity to the glycine-rich peptides described in Cupienius salai and Acanthoscurria gomesiana (spiders). Furthermore, serrulin has no hemolytic activity against human erythrocytes. While the presence of AMPs in T. serrulatus venom has been described in other works, this is the first work to characterize the presence of these molecules in the hemolymph (hemocytes) of this species and show its potential use as an alternative to conventional antibiotics against different species of microorganisms.

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Cecropin-like antimicrobial peptide protects mice from lethal E.coli infection

Cited by 12 publications

References 47 publications

Insect Cecropins, Antimicrobial Peptides with Potential Therapeutic Applications

Insect Cecropins, Antimicrobial Peptides with Potential Therapeutic Applications

Insight Into the Effects of Nisin and Cecropin on the Oral Microbial Community of Rats by High-Throughput Sequencing

Serrulin: A Glycine-Rich Bioactive Peptide from the Hemolymph of the Yellow Tityus serrulatus Scorpion

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