Comparative proteomic analysis of the venom of the taipan snake, Oxyuranus scutellatus, from Papua New Guinea and Australia: Role of neurotoxic and procoagulant effects in venom toxicity María Herrera a , Julián Fernández a , Mariángela Vargas a , Mauren Villalta a , Álvaro Segura a , Guillermo León a , Yamileth Angulo a , Owen Paiva b , Teatulohi Matainaho b , Simon D. Jensen b, c , Kenneth D. Winkel c , Juan J. Calvete d , David J. Williams b, c , e , José María Gutiérrez a, ⁎ a Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica b School of Medicine & Health Sciences, University of Papua New Guinea, Port Moresby, Papua New Guinea c Australian Venom Research Unit, Department of Pharmacology, University of Melbourne, Parkville, VIC, Australia d Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas (CSIC), Jaume Roig 11, 46010 Valencia, Spain e Nossal Institute for Global Health, University of Melbourne, Parkville, VIC, Australia ARTICLE INFO ABSTRACT Article history: Received 14 December 2011 Accepted 8 January 2012 Available online 14 January 2012 The venom proteomes of populations of the highly venomous taipan snake, Oxyuranus scutellatus, from Australia and Papua New Guinea (PNG), were characterized by reverse- phase HPLC fractionation, followed by analysis of chromatographic fractions by SDS- PAGE, N-terminal sequencing, MALDI-TOF mass fingerprinting, and collision-induced dis- sociation tandem mass spectrometry of tryptic peptides. Proteins belonging to the following seven protein families were identified in the two venoms: phospholipase A 2 (PLA 2 ), Kunitz- type inhibitor, metalloproteinase (SVMP), three-finger toxin (3FTx), serine proteinase, cysteine-rich secretory proteins (CRISP), and coagulation factor V-like protein. In addition, C-type lectin/lectin-like protein and venom natriuretic peptide were identified in the venom of specimens from PNG. PLA 2 s comprised more than 65% of the venoms of these two populations. Antivenoms generated against the venoms of these populations showed a pattern of cross-neutralization, corroborating the immunological kinship of these venoms. Toxicity experiments performed in mice suggest that, at low venom doses, neuro- toxicity leading to respiratory paralysis represents the predominant mechanism of prey im- mobilization and death. However, at high doses, such as those injected in natural bites, intravascular thrombosis due to the action of the prothrombin activator may constitute a potent and very rapid mechanism for killing prey. © 2012 Elsevier B.V. All rights reserved. Keywords: Taipan Oxyuranus scutellatus Venom Taipoxin Proteome Antivenom JOURNAL OF PROTEOMICS 75 (2012) 2128 – 2140 ⁎ Corresponding author. Tel.: +506 2229 3135; fax: +506 2292 0485. E-mail address: jose.gutierrez@ucr.ac.cr (J.M. Gutiérrez). 1874-3919/$ – see front matter © 2012 Elsevier B.V. All rights reserved. doi:10.1016/j.jprot.2012.01.006 Available online at www.sciencedirect.com www.elsevier.com/locate/jprot