Original article: Myrmecia pilosula (Jack Jumper) ant venom: identification of allergens and revised nomenclature
Article first published online: 12 MAR 2007
Volume 62, Issue 4, pages 437–443, April 2007
How to Cite
Wiese, M. D., Brown, S. G. A., Chataway, T. K., Davies, N. W., Milne, R. W., Aulfrey, S. J. and Heddle, R. J. (2007), Original article: Myrmecia pilosula (Jack Jumper) ant venom: identification of allergens and revised nomenclature. Allergy, 62: 437–443. doi: 10.1111/j.1398-9995.2007.01320.x
- Issue published online: 12 MAR 2007
- Article first published online: 12 MAR 2007
- Accepted for publication 10 December 2006
- Myr p 1;
- Myr p 2;
- Myr p 3;
- Myrmecia pilosula (Jack Jumper) ant venom;
Background: The ‘Jack Jumper Ant’ (JJA; Myrmecia pilosula species complex) is the major cause of ant sting anaphylaxis in Australia. Our aims were to determine the allergenicity of previously described venom peptides in their native forms, identify additional allergens and if necessary, update nomenclature used to describe the allergens according to International Union of Immunological Societies criteria.
Methods: Various polyacrylamide gel electrophoresis methods were used to separate JJA venom. Gel resolved venom was Western-blotted and probed with individual sera taken from patients with a history of JJA sting anaphylaxis and immunoglobulin E radioallergosorbent test (IgE RAST) tracer uptakes of >1% to whole venom.
Results: Of 67 available sera, 54 had RAST uptakes >1%. Thirteen IgE binding bands were identified using these sera. Pilosulin 3, [Ile5]pilosulin 1, and pilosulin 4.1 were recognized by 42 (78%), 18 (33%) and nine (17%) of the 54 sera that were tested. Immunoglobulin E-binding proteins with estimated molecular masses of 6.6, 22.8, 25.6, 30.4, 32.1, 34.4 and 89.8 kDa were each recognized by three or more individual sera. Two of these (25.6 and 89.8 kDa) were recognized by 46% and 37% of sera, respectively.
Conclusion: Nomenclature used to describe JJA venom allergens has been revised. Pilosulin 3 (Myr p 2) is the only major allergen, whilst [Ile5]pilosulin 1 (Myr p 1), and pilosulin 4.1 (Myr p 3) are minor allergens. There are an additional five IgE-binding proteins that require further characterization before they can be named as allergens. These findings provide a framework for standardizing venom extracts for diagnosis and immunotherapy.