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J Proteomics. 2009 Mar 6;72(2):145-54. doi: 10.1016/j.jprot.2009.01.017. Epub 2009 Jan 21.

Bee, wasp and ant venomics pave the way for a component-resolved diagnosis of sting allergy.

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Laboratory of Zoophysiology, Ghent University, B-9000 Ghent, Belgium.


With the complete sequencing of its genome, the honey bee is now a preferred model organism for Hymenoptera species, also with respect to venomic studies. Major pitfalls in proteomic profiling are: i) highly abundant proteins masking low-copy number proteins; ii) high heterogeneity in proteomes due to isoforms, protease activity and PTMs; iii) the inability for protein function assignment. If genomic information is not available, proteins still might be identified through cross-species protein identifications or MS/MS data-based de novo sequencing techniques. Venomic approaches discovered several new proteins and peptides from honey bees, bumble bees, ants and different wasp species, and some of these constituents were proven to be of immunological significance. Further digging in the proteome/peptidome will yield more so-called "venom trace elements" with only a local function in the venom duct or reservoir or released by leakage of the gland tissue. An impressive list of recombinants venom proteins has become available from a diverse range of Hymenopterans. Protein microarray allows the determination and monitoring of allergic patients' IgE reactivity profiles to disease-causing allergens using single measurements and minute amounts of serum. The information the physician will get from such a single run will largely exceed the output from current IgE capturing tools using whole venom preparations.

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