Toxins 2014, 6(3), 850-868; https://doi.org/10.3390/toxins6030850
Elapid Snake Venom Analyses Show the Specificity of the Peptide Composition at the Level of Genera Naja and Notechis
1
Laboratory of Structural Biology of Infection and Inflammation, Institute of Biochemistry and Molecular Biology, University of Hamburg, c/o DESY, Notkestreet 85, Building 22a, Hamburg 22603, Germany
2
Department of Chemistry, University of Engineering & Technology, G.T. Road, Lahore 54890, Pakistan
3
Institute of Organic Chemistry, University of Hamburg, Martin-Luther-King-Platz 6, Hamburg 20146, Germany
4
Institute of Clinical Chemistry, University Medical Centre Hamburg-Eppendorf (UKE), Martinistraße 52, Hamburg 20246, Germany
5
Department of Physics, IBILCE/UNESP, Rua Cristóvão Colombo 2265, São José do Rio Preto CEP 15054-000, SP Brazil
6
Centro de Biotecnologia, Instituto de Pesquisas Energéticas e Nucleares, Avenue Lineu Prestes 2242, São Paulo 05508-000, Brazil
*
Author to whom correspondence should be addressed.
Received: 3 November 2013 / Revised: 24 January 2014 / Accepted: 5 February 2014 / Published: 28 February 2014
(This article belongs to the Collection Evolution of Venom Systems)
Abstract
Elapid snake venom is a highly valuable, but till now mainly unexplored, source of pharmacologically important peptides. We analyzed the peptide fractions with molecular masses up to 10 kDa of two elapid snake venoms—that of the African cobra, N. m. mossambica (genus Naja), and the Peninsula tiger snake, N. scutatus, from Kangaroo Island (genus Notechis). A combination of chromatographic methods was used to isolate the peptides, which were characterized by combining complimentary mass spectrometric techniques. Comparative analysis of the peptide compositions of two venoms showed specificity at the genus level. Three-finger (3-F) cytotoxins, bradykinin-potentiating peptides (BPPs) and a bradykinin inhibitor were isolated from the Naja venom. 3-F neurotoxins, Kunitz/basic pancreatic trypsin inhibitor (BPTI)-type inhibitors and a natriuretic peptide were identified in the N. venom. The inhibiting activity of the peptides was confirmed in vitro with a selected array of proteases. Cytotoxin 1 (P01467) from the Naja venom might be involved in the disturbance of cellular processes by inhibiting the cell 20S-proteasome. A high degree of similarity between BPPs from elapid and viperid snake venoms was observed, suggesting that these molecules play a key role in snake venoms and also indicating that these peptides were recruited into the snake venom prior to the evolutionary divergence of the snakes. View Full-TextKeywords:
Naja mossambica mossambica; Notechis scutatus from Kangaroo Island; pharmacologically active peptides; snake venom; cytotoxin; neurotoxin; natriuretic peptides; Kunitz-type inhibitor; bradykinin-potentiating peptides
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MDPI and ACS Style
Munawar, A.; Trusch, M.; Georgieva, D.; Hildebrand, D.; Kwiatkowski, M.; Behnken, H.; Harder, S.; Arni, R.; Spencer, P.; Schlüter, H.; Betzel, C. Elapid Snake Venom Analyses Show the Specificity of the Peptide Composition at the Level of Genera Naja and Notechis. Toxins 2014, 6, 850-868.