The protein composition of honeybee venom reconsidered by a proteomic approach

Peiren, Nico; Vanrobaeys, Frank; Graaf, Dirk C. de; Devreese, Bart; Beeumen, Jozef Van; Jacobs, Franciscus

doi:10.1016/j.bbapap.2005.07.017

Cited by 152 publications

(178 citation statements)

References 11 publications

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“…Its composition, isolation, characterization, and the cloning of its bioactive species induced physiological damages and use in therapeutic treatments, are some of the aspects so far investigated [9,22,38,39].…”

Section: Resultsmentioning

confidence: 99%

“…The disclosure of this information would have considerable impact on current venom immunotherapy (VIT) by allowing tailoring of the therapeutic treatment of an individual's allergic reaction. In 2005, Peiren and coworkers reported that VIT with recombinant HBV allergens, assayed in stage I clinical trials, was more specific and safer than treatments employing bee-derived venom [9]. A full venom characterization would also help to possibly improve current HBV based therapeutics, reported in particular for arthritic and rheumatic conditions [12].…”

mentioning

confidence: 99%

“…Api m 3 is a glycoprotein accounting for 1% to 2% of the venom dry weight [3,13]. In 2005, this protein was reported by Peiren and coworkers [9] to have been removed from the list of allergens because of incomplete IgE binding and lack of satisfactory sequence data. Nonetheless, the IUIS has re-introduced this enzyme into the allergen list.…”

mentioning

confidence: 99%

“…It was then detected by other laboratories [23][24][25][26], and shown to contain a typical tryptic protease domain with a serine protease catalytic triad. Despite not being reported in the official allergen list, the newly discovered HBV Icarapin (MW 19.6 kDa) [9] is a glycoprotein worth mentioning along with the other allergens, as it has been cloned, expressed and found to bind IgE [10].…”

mentioning

confidence: 99%

“…The study, isolation and characterization of allergenic proteins and peptides are being performed using much more sophisticated analytical techniques including: gene cloning, mass spectrometry, X-ray and genomic techniques [21]. In this context, MALDI mass spectrometry has proven to be a powerful tool, especially when used in a typical bottom up proteomic approach [9].…”

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confidence: 99%

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Detection of honeybee venom in envenomed tissues by direct MALDI MSI

Francese

Lambardi

Mastrobuoni

et al. 2009

J. Am. Soc. Mass Spectrom.

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A new analytical approach using matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI MSI) for the study of honeybee venom is shown. In vitro and in vivo models simulating the bee sting have been developed using live honeybees and, as the envenomation sites, pig ears and rat legs; MALDI MSI has been used to map, over time, the diffusion and distribution of three venom allergens (Api m 1, Api m 4, and Api m 6) and two venom toxins (apamine and mast cell degranulating peptide). In conjunction with other classical biochemical techniques and high resolution mass spectrometry (HRMS), structural data have been obtained that contribute to current understanding of honeybee venom composition. Initial data have also been obtained demonstrating the feasibility of mapping the organism's response to the sting. The opportunity to monitor venom diffusion and the organism's response at the same time might open new pathways for in vivo preclinical studies in designing and testing new venom immunotherapy (VIT). (J Am Soc Mass Spectrom 2009, 20, 112-123)

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Detection of honeybee venom in envenomed tissues by direct MALDI MSI

Francese

Lambardi

Mastrobuoni

et al. 2009

J. Am. Soc. Mass Spectrom.

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The rise and fall of major royal jelly proteins during a honeybee (Apis mellifera) workers' life

Dobritzsch

Aumer

Fuszard

et al. 2019

Ecology and Evolution

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The genome of the western honeybee ( Apis mellifera ) harbors nine transcribed major royal jelly protein genes ( mrjp1‐9 ) which originate from a single‐copy precursor via gene duplication. The first MRJP was identified in royal jelly, a secretion of the bees' hypopharyngeal glands that is used by young worker bees, called nurses, to feed developing larvae. Thus, MRJPs are frequently assumed to mainly have functions for developing bee larvae and to be expressed in the food glands of nurse bees. In‐depth knowledge on caste‐ and age‐specific role and abundance of MRJPs is missing. We here show, using combined quantitative real‐time PCR with quantitative mass spectrometry, that expression and protein amount of mrjp1‐5 and mrjp7 show an age‐dependent pattern in worker's hypopharyngeal glands as well as in brains, albeit lower relative abundance in brains than in glands. Expression increases after hatching until the nurse bee period and is followed by a decrease in older workers that forage for plant products. Mrjp6 expression deviates considerably from the expression profiles of the other mrjps , does not significantly vary in the brain, and shows its highest expression in the hypopharyngeal glands during the forager period. Furthermore, it is the only mrjp of which transcript abundance does not correlate with protein amount. Mrjp8 and mrjp9 show, compared to the other mrjps, a very low expression in both tissues. Albeit mrjp8 mRNA was detected via qPCR, the protein was not quantified in any of the tissues. Due to the occurrence of MRJP8 and MRJP9 in other body parts of the bees, for example, the venom gland, they might not have a hypopharyngeal gland‐ or brain‐specific function but rather functions in other tissues. Thus, mrjp1‐7 but not mrjp8 and mrjp9 might be involved in the regulation of phenotypic plasticity and age polyethism in worker honeybees.

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The hemolymph proteome of the honeybee: Gel‐based or gel‐free?

et al. 2009

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The honeybee has an invaluable economic impact and is a model for studying immunity, development and social behavior. The recent sequencing and annotation of the honeybee genome facilitates the study of its hemolymph, which reflects the physiological condition and mediates immune responses. We aimed at making a proteomic reference map of honeybee hemolymph and compared gel-free and gel-based techniques. One hundred and four 2-DE spots corresponding to 62 different proteins were identified. Eight identical 2-DLC experiments resulted in the identification of 32 unique proteins. One repeat was clearly not representative for the potential of the given 2-DLC setup. Only 27% of the identified hemolymph proteins were found by both techniques. In addition, we found proteins of three different viruses which creates possibilities for biomarker design. Future hemolymph studies will benefit from this work.

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The protein composition of honeybee venom reconsidered by a proteomic approach

Cited by 152 publications

References 11 publications

Detection of honeybee venom in envenomed tissues by direct MALDI MSI

Detection of honeybee venom in envenomed tissues by direct MALDI MSI

The rise and fall of major royal jelly proteins during a honeybee (Apis mellifera) workers' life

The hemolymph proteome of the honeybee: Gel‐based or gel‐free?

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