Georgieva, DessislavaSeifert, JanaOehler, Michaelavon Bergen, MartinSpencer, PatrickArni, Raghuvir K. [UNESP]Genov, NicolayBetzel, Christian2014-05-202014-05-202011-05-01Journal of Proteome Research. Washington: Amer Chemical Soc, v. 10, n. 5, p. 2440-2464, 2011.1535-3893http://hdl.handle.net/11449/22038The 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 biosynthesis of toxins destroying the hemostasis (P-III metalloproteases, SVMPs), antimicrobial proteins (L-amino acid oxidases, LAAOs, and transferrin-like proteins, TFLPs), and myotoxins (phospholipase A(2)s, PLA(2)s). The three transferrin isoforms of the Australian P. avstralis (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-5'-nucleotidases (5'-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.2440-2464engSnake venomicPseudechis australis2-D electrophoresiselectrospray mass spectrometryvenom transferrinEnzymatic activityArtigo10.1021/pr101248eWOS:000290234800027Acesso restrito91625089789458870000-0003-2460-1145