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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/22038
Title: 
Pseudechis australis Venomics: Adaptation for a Defense against Microbial Pathogens and Recruitment of Body Transferrin
Author(s): 
Institution: 
  • Univ Hamburg
  • UFZ Helmholtz Ctr Environm Res
  • Instituto de Pesquisas Energéticas e Nucleares (IPEN)
  • Universidade Estadual Paulista (UNESP)
  • Bulgarian Acad Sci
ISSN: 
1535-3893
Sponsorship: 
  • Deutsche Forschungsgemeinschaft (DFG)
  • Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Sponsorship Process Number: 
  • DFG: BE 1443-18-1
  • DFG: BE1443
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 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.
Issue Date: 
1-May-2011
Citation: 
Journal of Proteome Research. Washington: Amer Chemical Soc, v. 10, n. 5, p. 2440-2464, 2011.
Time Duration: 
2440-2464
Publisher: 
Amer Chemical Soc
Keywords: 
  • Snake venomic
  • Pseudechis australis
  • 2-D electrophoresis
  • electrospray mass spectrometry
  • venom transferrin
  • Enzymatic activity
Source: 
http://dx.doi.org/10.1021/pr101248e
URI: 
Access Rights: 
Acesso restrito
Type: 
outro
Source:
http://repositorio.unesp.br/handle/11449/22038
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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