Proteomic analysis of summer and winter Apis mellifera workers shows reduced protein abundance in winter samples

Ward, Rachel; Coffey, Mary F.; Kavanagh, Kevin

doi:10.1016/j.jinsphys.2022.104397

Cited by 7 publications

(8 citation statements)

References 56 publications

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“…Proteins represent more than 50% of dry matter [ 13 , 14 , 15 , 16 ] and have a specific physiological role in queen bee development. MRJPs include numerous essential amino acids, like ovalbumin and casein [ 17 , 18 , 19 , 20 , 21 , 22 ]. Proteins from the MRJP family, from MRP1 to MRP9, are the main soluble proteins (31%) of RJ [ 17 , 18 , 19 ].…”

Section: Chemical Composition Of Royal Jellymentioning

confidence: 99%

“…Proteins from the MRJP family, from MRP1 to MRP9, are the main soluble proteins (31%) of RJ [ 17 , 18 , 19 ]. MRJP 1 is a weakly acidic glycoprotein (55 kDa) that forms oligomers of 350 or 420 kDa [ 19 , 20 ]. MRJP 2, MRJP3, MRJP4, and MRJP 5 are glycoproteins of 49 kDa, 60–70 kDa, 60 kDa, and 80 kDa, respectively) [ 22 ].…”

Section: Chemical Composition Of Royal Jellymentioning

confidence: 99%

“…In one study that investigated the protein composition of RJ, 134 proteins were identified by gel-based and gel-free proteomics [ 20 , 22 , 23 , 24 ]. MRJPs were the main protein components of RJ, together with some proteins participating in the carbohydrate metabolism, such as glucose oxidase, predecessor-glucosidase, and glucose dehydrogenase.…”

Section: Chemical Composition Of Royal Jellymentioning

confidence: 99%

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Royal Jelly: Biological Action and Health Benefits

Oršolić,

Jazvinšćak Jembrek

2024

IJMS

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Royal jelly (RJ) is a highly nutritious natural product with great potential for use in medicine, cosmetics, and as a health-promoting food. This bee product is a mixture of important compounds, such as proteins, vitamins, lipids, minerals, hormones, neurotransmitters, flavonoids, and polyphenols, that underlie the remarkable biological and therapeutic activities of RJ. Various bioactive molecules like 10-hydroxy-2-decenoic acid (10-HDA), antibacterial protein, apisin, the major royal jelly proteins, and specific peptides such as apisimin, royalisin, royalactin, apidaecin, defensin-1, and jelleins are characteristic ingredients of RJ. RJ shows numerous physiological and pharmacological properties, including vasodilatory, hypotensive, antihypercholesterolaemic, antidiabetic, immunomodulatory, anti-inflammatory, antioxidant, anti-aging, neuroprotective, antimicrobial, estrogenic, anti-allergic, anti-osteoporotic, and anti-tumor effects. Moreover, RJ may reduce menopause symptoms and improve the health of the reproductive system, liver, and kidneys, and promote wound healing. This article provides an overview of the molecular mechanisms underlying the beneficial effects of RJ in various diseases, aging, and aging-related complications, with special emphasis on the bioactive components of RJ and their health-promoting properties. The data presented should be an incentive for future clinical studies that hopefully will advance our knowledge about the therapeutic potential of RJ and facilitate the development of novel RJ-based therapeutic opportunities for improving human health and well-being.

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Section: Chemical Composition Of Royal Jellymentioning

confidence: 99%

Section: Chemical Composition Of Royal Jellymentioning

confidence: 99%

Section: Chemical Composition Of Royal Jellymentioning

confidence: 99%

See 1 more Smart Citation

Royal Jelly: Biological Action and Health Benefits

Oršolić,

Jazvinšćak Jembrek

2024

IJMS

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“…Bees are insects found on all continents, many of these species have yet to be described and are an exciting source for the study and search for new molecules with antimicrobial properties. There are experimental and clinical reports on Apis mellifera venom and its anti-inflammatory, antimicrobial, and anticancer effects; the components present in the venom, such as proteins, vary from a summer season compared to a winter season [ 36 , 37 , 38 ], in addition, have shown different therapeutic properties against oxidative stress induced by beta-amyloid [ 39 , 40 , 41 ]. For Parkinson’s disease, the neuroprotective potential of bee venom against oxidative stress induced by rotenone (pesticide) has been demonstrated in a mouse model, including preventing the decrease in dopamine and also restoring locomotor activity in mice [ 42 , 43 ].…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial Activity of Apis mellifera Bee Venom Collected in Northern Peru

2023

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Due to the emergence of microorganisms resistant to antibiotics and the failure of antibiotic therapies, there is an urgent need to search for new therapeutic options, as well as new molecules with antimicrobial potential. The objective of the present study was to evaluate the in vitro antibacterial activity of Apis mellifera venom collected in the beekeeping areas of the city of Lambayeque in northern Peru against Escherichia coli, Pseudomonas aeruginosa, and Staphylococcus aureus. Bee venom extraction was performed by electrical impulses and separated using the Amicon ultra centrifugal filter. Subsequently, the fractions were quantified by spectrometric 280 nm and evaluated under denaturant conditions in SDS-PAGE. The fractions were pitted against Escherichia coli ATCC 25922, Staphylococcus aureus ATCC 29213, and Pseudomonas aeruginosa ATCC 27853. A purified fraction (PF) of the venom of A. mellifera and three low molecular weight bands of 7 KDa, 6 KDa, and 5 KDa were identified that showed activity against E. coli with a MIC of 6.88 µg/mL, while for P. aeruginosa and S. aureus, it did not present a MIC. No hemolytic activity at a concentration lower than 15.6 µg/mL and no antioxidant activity. The venom of A. mellifera contains a potential presence of peptides and a predilection of antibacterial activity against E. coli.

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“…Specifically, APD 2 is a component of internal flexible cuticles [ 4 ], and proteomic analyses have demonstrated that APD 2 is also detected in the fat body of A. mellifera worker bees [ 7 ] and is an exoskeletal component [ 8 ]. Cuticular proteins, including APD 2, showed an increased abundance in summer A. mellifera worker bees in comparison to winter worker bees [ 9 ]. In addition, APD genes have been analyzed through genome-wide identification in wasps [ 2 , 10 , 11 ] and bumblebees [ 12 ].…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial Activity of Apidermin 2 from the Honeybee Apis mellifera

Kim

Choi

et al. 2022

Insects

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Apidermins (APDs) are known as structural cuticular proteins in insects, but their additional roles are poorly understood. In this study, we characterized the honeybee, Apis mellifera, APD 2 (AmAPD 2), which displays activity suggesting antimicrobial properties. In A. mellifera worker bees, the AmAPD 2 gene is transcribed in the epidermis, hypopharyngeal glands, and fat body, and induced upon microbial ingestion. Particularly in the epidermis of A. mellifera worker bees, the AmAPD 2 gene showed high expression and responded strongly to microbial challenge. Using a recombinant AmAPD 2 peptide, which was produced in baculovirus-infected insect cells, we showed that AmAPD 2 is heat-stable and binds to live bacteria and fungi as well as carbohydrates of microbial cell wall molecules. This binding action ultimately induced structural damage to microbial cell walls, which resulted in microbicidal activity. These findings demonstrate the antimicrobial role of AmAPD 2 in honeybees.

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Proteomic analysis of summer and winter Apis mellifera workers shows reduced protein abundance in winter samples

Cited by 7 publications

References 56 publications

Royal Jelly: Biological Action and Health Benefits

Royal Jelly: Biological Action and Health Benefits

Antimicrobial Activity of Apis mellifera Bee Venom Collected in Northern Peru

Antimicrobial Activity of Apidermin 2 from the Honeybee Apis mellifera

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