2. Academic Validation
  3. Pilosulins: a review of the structure and mode of action of venom peptides from an Australian ant Myrmecia pilosula

Pilosulins: a review of the structure and mode of action of venom peptides from an Australian ant Myrmecia pilosula

  • Toxicon. 2015 May:98:54-61. doi: 10.1016/j.toxicon.2015.02.013.
Troy Wanandy 1,  Nuri Gueven 2,  Noel W Davies 3,  Simon G A Brown 4,  Michael D Wiese 5
Affiliations

Affiliations

  • 1 Jack Jumper Allergy Program, Royal Hobart Hospital, GPO Box 1061L, Hobart, Tasmania 7001, Australia; Division of Pharmacy, School of Medicine, University of Tasmania, Private Bag 26, Hobart, Tasmania 7001, Australia; Division of Medicine, School of Medicine, University of Tasmania, Private Bag 68, Hobart, Tasmania 7001, Australia; Department of Pharmacy, Royal Hobart Hospital, GPO Box 1061L, Hobart, Tasmania 7001, Australia. Electronic address: troy.wanandy@dhhs.tas.gov.au.
  • 2 Division of Pharmacy, School of Medicine, University of Tasmania, Private Bag 26, Hobart, Tasmania 7001, Australia.
  • 3 Central Science Laboratory, University of Tasmania, Private Bag 74, Hobart, Tasmania 7001, Australia.
  • 4 Jack Jumper Allergy Program, Royal Hobart Hospital, GPO Box 1061L, Hobart, Tasmania 7001, Australia; Centre for Clinical Research in Emergency Medicine, Harry Perkins Institute of Medical Research and the University of Western Australia, Perth, Australia.
  • 5 Jack Jumper Allergy Program, Royal Hobart Hospital, GPO Box 1061L, Hobart, Tasmania 7001, Australia; School of Pharmacy and Medical Sciences, University of South Australia, GPO Box 2471, Adelaide, South Australia 5001, Australia.
PMID: 25725257 DOI: 10.1016/j.toxicon.2015.02.013
Abstract

Myrmecia pilosula is an endemic Australian ant whose STING is a frequent cause of insect allergy in southeast Australia, and several deaths due to M. pilosula STING envenomation have been documented. In this review, we discuss the composition and bioactivity of M. pilosula venom. In addition to various Enzymes and pharmacologically active constituents, the venom contains four families of highly basic low molecular weight peptides trivially named Pilosulins. These peptides are unique and have low structural homology to Other Hymenoptera venom peptides. Moreover, M. pilosula venom is relatively simple in its composition with 5 predominant peptides making up about 90% by weight. These peptides display cytotoxic, hypotensive, histamine-releasing and antimicrobial activities. Within the M. pilosula venom, Pilosulin 3 has been classified as a major allergen and [Ile(5)]pilosulin 1 and Pilosulin 4.1 are classified as minor allergens. Several uncharacterised higher molecular weight components with allergenic activities have also been identified. The revised naming of M. pilosula venom peptides according to the International Union of Immunological Societies (IUIS) criteria for allergen nomenclature is discussed in this review.

Keywords

Allergens; Ant venom; Myr p; Myrmecia pilosula; Pilosulin.

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