Molecular cloning and expression of icarapin, a novel IgE‐binding bee venom protein

Peiren, Nico; Graaf, Dirk C. de; Brunain, Marleen; Bridts, Chris H.; Ebo, Didier G.; Stevens, W. J.; Jacobs, Franciscus

doi:10.1016/j.febslet.2006.08.005

Cited by 49 publications

(44 citation statements)

References 12 publications

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“…The protein composition of HBV is highly complex, with at least 113 identified proteins and peptides (Van Vaerenbergh et al, 2014). The complexity is even increased by different glycosylation patterns and protein heterogeneity [phospholipase A 2 (Peiren et al, 2005;Blank et al, 2011a); Api m 6 (Peiren et al, 2006;Kettner et al, 2001)]. Currently, 12 different HBV proteins have been recognized as allergens (http://www.allergen.org/).…”

Section: Introductionmentioning

confidence: 98%

“…Interestingly, while present in unprocessed HBV, Api m 10 seemed to be absent or underrepresented in therapeutic HBV preparations used for venom-specific immunotherapy . Until now two alternatively spliced Api m 10 transcripts have been identified [variant 1 (Peiren et al, 2006) and variant 2 (Peiren et al, 2006;Blank et al, 2011b)], both of which display IgE reactivity that is independent of cross-reactive carbohydrate determinants (CCDs) (Peiren et al, 2006;Blank et al, 2011b).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

IgE recognition of chimeric isoforms of the honeybee (Apis mellifera) venom allergen Api m 10 evaluated by protein array technology

Vaerenbergh

Smet

Rafei-Shamsabadi

et al. 2015

Molecular Immunology

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Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

IgE recognition of chimeric isoforms of the honeybee (Apis mellifera) venom allergen Api m 10 evaluated by protein array technology

Vaerenbergh

Smet

Rafei-Shamsabadi

et al. 2015

Molecular Immunology

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“…Based on 2DGE/MALDI experiments, three previously unknown proteins were found (Peiren et al, 2005). The presence of each one has, however, been difficult to rationalize: Venom protein 2 (later named icarapin (Peiren et al, 2006)) is a carbohydrate-rich protein with unknown function, a platelet-derived growth factor/vascular endothelial growth factor-like protein, the human homologue of which promotes blood vessel growth, and finally MRJP8. MRJP8 transcript was observed in a brain expressed sequence tag (EST) library (Albert et al, 2004) but the protein itself has not yet found in RJ, except as a single-peptide hit in the hypopharyngeal gland (Santos et al, 2005), implying that it has roles other than just food.…”

Section: Venommentioning

confidence: 97%

Apis mellifera Proteomics: Where Will the Future Bee?

Chan¹,

Foster

2009

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Honey bees play a crucial role in pollinating wild and cultivated vegetation, with substantial implications on our economy and food supply. Our scientific knowledge of bees consists largely of behavioral or macroscopic-level biological studies. Although in the past several decades there have been some advances in our knowledge of specific hormones, genes, and proteins, molecular biology of bees remain poorly understood relative to the depth to which we understand humans, and typical model organisms such as the mouse or fruit fly. This is due in part to the lack of available reagents for interrogating protein-specific information in standard assays such as Western blot, immunolocalization, and immunoaffinity purification, as well as a relatively difficult system for introducing small, interfering RNAs. Given the available genome sequence then, mass spectrometry-based proteomics techniques are ideally suited to studies in bees; starting from so little knowledge, the discovery-based nature of proteomics should allow for a very steep learning curve relative to better-studied systems such as fruit fly. To this end, twenty-two honey bee proteomics papers have been published since 2005. Here we present a brief summary of biochemical/molecular biological research in bees, including some of the challenges; we focus on the proteomics work to date, and relate these findings to recent transcriptomic work and proteomic studies in other social insects. We end with some speculation on where proteomics is most likely able to provide insight into bee biology where other methods would fail. As the general population and scientific community become increasingly aware of the value of honey bees to both our economy and ecosystem, proteomics will play an important role in improving our understanding of this beneficial insect.

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“…Sera from 37% of bee venom sensitive patients had IgE reacting with the recombinant protein. A protein, previously called carbohydrate rich protein [15], was cloned and a recombinant produced in bacteria [16]. IgE from four of five allergic beekeepers bound to the carbohydratefree recombinant protein, named icarapin.…”

Section: Bee Allergensmentioning

confidence: 99%