ARTICLE
pubs.acs.org/jpr
Pseudechis australis Venomics: Adaptation for a Defense against Microbial Pathogens and Recruitment of Body Transferrin †,‡ †,§ € § § || Dessislava Georgieva,^ Jana Seifert, Michaela Ohler, Martin‡ von Bergen, Patrick Spencer, Raghuvir K. Arni, Nicolay Genov,# and Christian Betzel*, ‡ Institute of Biochemistry and Molecular Biology, University of Hamburg, Laboratory of Structural Biology of Infection and Inflammation, c/o DESY, Notkestrasse 85, Build. 22a, 22603 Hamburg, Germany § Department of Proteomics, Helmholtz Centre for Environmental Research-UFZ, Permoser Strasse 15, 04318 Leipzig, Germany Centro) de Biotecnologia, Instituto de Pesquisas Energ eticas e Nucleares, Av. Lineeu Prestes 2242, 05508-000 S~ao Paulo, Brazil ^ Department of Physics, IBILCE/UNESP, Crist ov~ao Colombo 2265, CEP 15054-000, S~ao Jos e do Rio Preto, SP Brazil #Institute of Organic Chemistry, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria
ABSTRACT: The venom composition of Pseudechis australis,a widely distributed in Australia reptile, was analyzed by 2-DE and mass spectrometric analysis. In total, 102 protein spots were identified as venom toxins. The gel is dominated by horizontal trains of spots with identical or very similar molecular masses but differing in the pI values. This suggests possible post- translational modifications of toxins, changing their electrostatic charge. The results demonstrate a highly specialized biosynth- esis of toxins destroying the hemostasis (P III metallopro- teases, SVMPs), antimicrobial proteins (L-amino acid oxidases, LAAOs, and transferrin-like proteins, TFLPs), and myotoxins (phospholipase A2s, PLA2s). The three transferrin isoforms of the Australian P. australis (Elapidae snake) venom are highly homologous to the body transferrin of the African Lamprophis fuliginosus (Colubridae), an indication for the recruitment of body transferrin. The venomic composition suggests an adaptation for a defense against microbial pathogens from the prey. Transferrins have not previously been reported as components of elapid or other snake venoms. Ecto-50-nucleotidases (50-NTDs), nerve growth factors (VNGFs), and a serine proteinase inhibitor (SPI) were also identified. The venom composition and enzymatic activities explain the clinical manifestation of the king brown snakebite. The results can be used for medical, scientific, and biotechnological purposes. KEYWORDS: snake venomics, Pseudechis australis, 2-D electrophoresis, electrospray mass spectrometry, venom transferrin, enzyme activity