Proteomic analysis of Myremecia pilosula (jack jumper) ant venom

M.D. Wiese, T.K. Chataway, N.W. Davies, R.W. Milne, Simon Brown, W.P. Gai, R.J. Heddle

    Research output: Contribution to journalArticle

    33 Citations (Scopus)

    Abstract

    Ant sting allergy in Australia is predominantly due to the Myrmecia pilosula species complex. Gel separation of M. pilosula venom is necessary so that the allergenic importance of each component can be defined by western blotting. However, previous PAGE methods produced suboptimal resolution and the components of each band were not precisely defined. Venom was resolved in both non-reduced and reduced form by one-dimensional acid urea PAGE, SDS-PAGE and two-dimensional acid urea-SDS PAGE. Resolved peptides were extracted and analysed by HPLC-MS. Acid urea PAGE and acid urea-SDS PAGE proved more effective than SDS-PAGE for resolution of peptides smaller than 10 kDa. All of the major peptides previously observed in M. pilosula venom were observed in gel resolved venom. Venom was found to primarily consist of peptides with molecular weight < 10 kDa, most of which contain disulfide bridges. SDS-PAGE of non-reduced venom clearly defined six higher molecular weight proteins between 26 and 90 kDa. An 8546 Da dimer named pilosulin 5 was observed, but pilosulin 4, a peptide recently proposed to be present in venom was not. A variant of pilosulin 4 here named pilosulin 4.1a, existing as an 8198 Da dimer, was observed and has been characterised. (c) 2005 Elsevier Ltd. All rights reserved.
    Original languageEnglish
    Pages (from-to)208-217
    JournalToxicon
    Volume47
    Issue number2
    DOIs
    Publication statusPublished - 2006

    Fingerprint Dive into the research topics of 'Proteomic analysis of Myremecia pilosula (jack jumper) ant venom'. Together they form a unique fingerprint.

    Cite this