Melittin: from honeybees to superbugs

Memariani, Hamed; Memariani, Mojtaba; Shahidi‐Dadras, Mohammad; Nasiri, Soheila; Akhavan, M.; Moravvej, Hamideh

doi:10.1007/s00253-019-09698-y

Cited by 101 publications

(86 citation statements)

References 84 publications

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“…One of the most extensively studied AMPs is a major component in the venom of European honeybee Apis mellifera, melittin [28]. Melittin has demonstrated a wide range of bactericidal activity against both reference and clinical strains [28][29][30], which includes antibiotic-resistant bacteria, such as A. baumannii and Pseudomonas aeruginosa [31][32][33]. It is a small cationic linear peptide composed of 26 amino acid residues (GIGAVLKVLTTGLPALISWIKRKRQQ-CONH 2 ) with a net charge at physiological pH of +6 due to the presence of arginine and lysine residues [22,34].…”

Section: Introductionmentioning

confidence: 99%

“…It is a small cationic linear peptide composed of 26 amino acid residues (GIGAVLKVLTTGLPALISWIKRKRQQ-CONH 2 ) with a net charge at physiological pH of +6 due to the presence of arginine and lysine residues [22,34]. The N-and C-terminal amino acids of melittin are mostly hydrophobic and hydrophilic, respectively [28,35]. Polar and nonpolar amino acid residues are distributed asymmetrically in melittin, suggesting an amphipathic nature when it adopts in an α-helical conformation [36].…”

Section: Introductionmentioning

confidence: 99%

“…Polar and nonpolar amino acid residues are distributed asymmetrically in melittin, suggesting an amphipathic nature when it adopts in an α-helical conformation [36]. This cationic and amphipathic structure is regarded as the most characteristic configuration of AMPs, which makes melittin a representative model peptide for understanding the mechanisms of membrane permeabilization by AMPs [28,37,38].…”

Section: Introductionmentioning

confidence: 99%

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Pan-Drug Resistant Acinetobacter baumannii, but Not Other Strains, Are Resistant to the Bee Venom Peptide Melittin

et al. 2020

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Acinetobacter baumannii is a prevalent pathogen in hospital settings with increasing importance in infections associated with biofilm production. Due to a rapid increase in its drug resistance and the failure of commonly available antibiotics to treat A. baumannii infections, this bacterium has become a critical public health issue. For these multi-drug resistant A. baumannii, polymyxin antibiotics are considered the only option for the treatment of severe infections. Concerning, several polymyxin-resistant A. baumannii strains have been isolated over the last few years. This study utilized pan drug-resistant (PDR) strains of A. baumannii isolated in Brazil, along with susceptible (S) and extreme drug-resistant (XDR) strains in order to evaluate the in vitro activity of melittin, an antimicrobial peptide, in comparison to polymyxin and another antibiotic, imipenem. From a broth microdilution method, the determined minimum inhibitory concentration showed that S and XDR strains were susceptible to melittin. In contrast, PDR A. baumannii was resistant to all treatments. Treatment with the peptide was also observed to inhibit biofilm formation of a susceptible strain and appeared to cause permanent membrane damage. A subpopulation of PDR showed membrane damage, however, it was not sufficient to stop bacterial growth, suggesting that alterations involved with antibiotic resistance could also influence melittin resistance. Presumably, mutations in the PDR that have arisen to confer resistance to widely used therapeutics also confer resistance to melittin. Our results demonstrate the potential of melittin to be used in the control of bacterial infections and suggest that antimicrobial peptides can serve as the basis for the development of new treatments.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Pan-Drug Resistant Acinetobacter baumannii, but Not Other Strains, Are Resistant to the Bee Venom Peptide Melittin

et al. 2020

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“…The peptide melittin is the most abundant toxin in honeybee venom, comprising ~40 to 60% of the dry weight of this venom, consisting of a basic 26-amino-acid polypeptide ( 12 , 15 , 16 ). Melittin monomers bind to lipid membranes producing pores, exerting a cytotoxic effect ( 17 , 18 ). Furthermore, it acts synergistically with the enzyme phospholipase A 2 , promoting damage to the cellular and mitochondrial membranes of various cell types.…”

Section: The Honeybee Venommentioning

confidence: 99%

“…This peptide is probably the major responsible for the bee venom-induced pain through direct and indirect activation of primary nociceptor cells ( 16 ). As melittin has various pharmacological activities, including antitumoral ( 15 , 19 ), anti-viral ( 18 , 18 , 20 ), antibacterial ( 15 , 17 ), antifungal ( 15 ), anti-arthritis, anti-inflammatory, anti-atherosclerotic, anti-diabetic, and neuro-protective ( 12 ) effects, several studies have been conducted to evaluate the safety of the compound when administered orally. The results of these studies indicate that oral ingestion of this peptide results in low toxicity ( 21 – 23 ).…”

Section: The Honeybee Venommentioning

confidence: 99%

Toxicological Risk Assessment of the Accidental Ingestion of a Honeybee (Apis mellifera L.) Present in Food

Marinho

Soto-Blanco

2020

Front. Vet. Sci.

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The aim of the present work was to evaluate the possible risk of toxic effects due to the ingestion of a honeybee ( Apis mellifera L.) accidentally present in food. The methodology used in this study was a bibliographic survey of studies on the toxic effects related to honeybees, with a critical analysis of the possible risks of accidental ingestion of these insects. The amount of venom present in a bee is considered insufficient to induce detectable toxic effects in a person who ingests it by accident, and various components of the venom are destroyed by gastric secretions. However, despite the rare frequency, there is a risk of the ingestion of a bee, causing an allergic reaction to some components of the venom in sensitized individuals. In addition, pollen carried by a bee may cause an allergic reaction in a sensitive individual. Thus, the accidental ingestion of a bee present in a food does not pose the risk of toxic effects for the majority of the population but may promote allergic reactions in susceptible individuals.

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Microfluidic Giant Polymer Vesicles Equipped with Biopores for High‐Throughput Screening of Bacteria

Heuberger,

Messmer,

dos Santos

et al. 2023

Advanced Science

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Understanding the mechanisms of antibiotic resistance is critical for the development of new therapeutics. Traditional methods for testing bacteria are often limited in their efficiency and reusability. Single bacterial cells can be studied at high throughput using double emulsions, although the lack of control over the oil shell permeability and limited access to the droplet interior present serious drawbacks. Here, a straightforward strategy for studying bacteria‐encapsulating double emulsion‐templated giant unilamellar vesicles (GUVs) is introduced. This microfluidic approach serves to simultaneously load bacteria inside synthetic GUVs and to permeabilize their membrane with the pore‐forming peptide melittin. This enables antibiotic delivery or the influx of fresh medium into the GUV lumen for highly parallel cultivation and antimicrobial efficacy testing. Polymer‐based GUVs proved to be efficient culture and analysis microvessels, as microfluidics allow easy selection and encapsulation of bacteria and rapid modification of culture conditions for antibiotic development. Further, a method for in situ profiling of biofilms within GUVs for high‐throughput screening is demonstrated. Conceivably, synthetic GUVs equipped with biopores can serve as a foundation for the high‐throughput screening of bacterial colony interactions during biofilm formation and for investigating the effect of antibiotics on biofilms.

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Melittin: from honeybees to superbugs

Cited by 101 publications

References 84 publications

Pan-Drug Resistant Acinetobacter baumannii, but Not Other Strains, Are Resistant to the Bee Venom Peptide Melittin

Pan-Drug Resistant Acinetobacter baumannii, but Not Other Strains, Are Resistant to the Bee Venom Peptide Melittin

Toxicological Risk Assessment of the Accidental Ingestion of a Honeybee (Apis mellifera L.) Present in Food

Microfluidic Giant Polymer Vesicles Equipped with Biopores for High‐Throughput Screening of Bacteria

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