Scratching the Surface of an Itch: Molecular Evolution of Aculeata Venom Allergens
- 738 Downloads
Hymenopteran insects are infamous for their sting, and their ability to cause severe anaphylaxis and in some cases death. This allergic reaction is a result of allergens present in the venom. Hymenopterans have many common venom allergens, the most widespread of which include phospholipase A1, phospholipase A2, acid phosphatase, hyaluronidase, serine protease and antigen 5. While there have been studies that look at the phylogenetic histories of allergens within closely related species, to our knowledge, this is the first study using evolutionary analyses to compare across Hymenoptera the types of selection that are occurring on allergens. This research examined the publicly available sequences of six different groups of allergens and found that allergens had diverged and formed closely related clades which share greater sequence similarities. We also analysed the patterns of selection and found that they are predominately under the influence of negative selection.
KeywordsVenom evolution Toxin Hymenoptera Allergen
KB and DB were supported by University of Queensland PhD scholarships. This work was also supported by the Department of Science and Technology (DST) INSPIRE Faculty Award (DST/INSPIRE/04/2017/000071) to KS and the DBT-IISc Partnership Program.
- Bateman A, O’Donovan C, Magrane M, Alpi E, Antunes R, Bely B et al (2018) UniProt: the universal protein knowledgebase. Nucleic Acids Res 45:D1Google Scholar
- Grimaldi DA, Engel MS (2005) Evolution of the insects. Cambridge University Press, CambridgeGoogle Scholar
- Mirza O, Henriksen A, Ipsen H, Larsen JN, Wissenbach M, Spangfort MD, Gajhede M (2000) Dominant epitopes and allergic cross-reactivity: complex formation between a Fab fragment of a monoclonal murine IgG antibody and the major allergen from birch pollen Bet v 1. J Immunol (Baltimore Md: 1950) 165(1):331–338CrossRefGoogle Scholar
- Murayama N, Saguchi Ki, Mentele R, Assakura MT, Ohi H, Fujita Y et al (2003) The unusual high molecular mass of Bothrops protease A, a trypsin-like serine peptidase from the venom of Bothrops jararaca, is due to its high carbohydrate content. Biochimica et biophysica acta 1652(1):1–6CrossRefPubMedGoogle Scholar
- Palma MS (2013) Handbook of biologically active peptides, 2nd edn. Elsevier, New YorkGoogle Scholar
- Schmidt JO (2009) Defensive behavior, Elsevier, New York, pp 252–257Google Scholar
- Suzuki N, Yamazaki Y, Fujimoto Z, Morita T, Mizuno H (2005) Crystallization and preliminary X-ray diffraction analyses of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels. Acta Crystallogr F 61(Pt 8):750–752CrossRefGoogle Scholar