A proteomic study of the major allergens from yellow jacket venoms

Daniel Kolarich*, Andreas Loos, Renaud Léonard, Lukas Mach, Gorji Marzban, Wolfgang Hemmer, Friedrich Altmann

*Corresponding author for this work

    Research output: Contribution to journalConference paperpeer-review

    25 Citations (Scopus)


    The venoms of stinging insects belong to the most dangerous allergen sources and can cause fatal anaphylactic reactions. Reliable prediction of a patient's risk to anaphylactic reactions is vital, and diagnosis requires the knowledge of the relevant allergens. Recently, a new hyaluronidase -like glycoprotein from Vespula vulgaris (Ves v 2b) was identified. This led us to investigate hyaluronidases and also other major allergens from V. germanica and four additional Vespula species. By MALDI-Q-TOF-MS, the new hyaluronidase-like protein was shown to be the major component of the 43-kDa band in all Vespula species studied. LC-ESI-Q-TOF-MS/MS sequencing of Ves g 2a and Ves g 2b facilitated the cloning of their cDNA. Ves v 2b and Ves g 2b turned out to be essentially identical on protein level. Whereas the less abundant "a" form displayed enzymatic activity, the new "b" homologue did not. This is probably caused by amino acid exchanges in the active site, and it raises questions about the physiological role of this protein. Sequence comparisons by MS/MS of antigen 5 and phospholipases from V. vulgaris, germanica, maculifrons, pensylvanica, flavopilosa and squamosa revealed the latter as a taxonomic outlier and led to the discovery of several not previously reported amino acid differences.

    Original languageEnglish
    Pages (from-to)1615-1623
    Number of pages9
    Issue number10
    Publication statusPublished - May 2007
    EventSiena Meeting : From Genome to Proteome (7th : 2006) - Siena, Italy
    Duration: 3 Sep 20067 Sep 2006


    • Allergens
    • De novo sequencing
    • Hyaluronidase
    • Vespula


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