scholarly journals Bothrops moojeni myotoxin-II, a Lys49-phospholipase A2 homologue: An example of function versatility of snake venom proteins

Author(s):  
Rodrigo G. Stábeli ◽  
Saulo F. Amui ◽  
Carolina D. Sant'Ana ◽  
Matheus G. Pires ◽  
Auro Nomizo ◽  
...  
2018 ◽  
Vol 99 (5) ◽  
pp. 226-235 ◽  
Author(s):  
Kellen Cristina Torres Costa ◽  
Bruna Barbosa de Sousa ◽  
Edigar Henrique Vaz Dias ◽  
Déborah Fernanda da Cunha Pereira ◽  
Mariana Santos Matias ◽  
...  

2013 ◽  
Vol 455 (2) ◽  
pp. 239-250 ◽  
Author(s):  
Bhaskar Barnwal ◽  
R. Manjunatha Kini

Inflamin, a novel snake venom toxin from Aipysurus eydouxii, leads to the activation of calcium-dependent phospholipase A2 by phosphorylation at Ser505, resulting in inflammation and pain.


2000 ◽  
Vol 373 (1) ◽  
pp. 7-15 ◽  
Author(s):  
Andreimar M Soares ◽  
Sı́lvia H Andrião-Escarso ◽  
Yamileth Angulo ◽  
Bruno Lomonte ◽  
José M Gutiérrez ◽  
...  

2018 ◽  
Vol 3 (2) ◽  

Understanding snake venom kinetics is crucial for developing risk evaluation strategies and determining the best dose and timing of antivenom required to bind all venom in snakebite patients. Polyphenolic compounds have shown to inhibit toxic effects induced by snake venom proteins. The interaction of polyphenols with Phospholipase A2 of Cerastes cerastes snake venom was investigated by fluorescence spectroscopy. The decrease in the fluorescence versus time was conducted at room temperature in 0.01 M Tris, 0.1 M NaCl at pH 7.4. The decrease in fluorescence was following a pattern of zero-order kinetics rate in which the fluorescence is decreasing linearly with time. This study is expected to offer additional information about the interactions of PLA2 with natural product that might lead to therapeutic drug.


Toxicon ◽  
2008 ◽  
Vol 52 (8) ◽  
pp. 908-917 ◽  
Author(s):  
Norival A. Santos-Filho ◽  
Lucas B. Silveira ◽  
Clayton Z. Oliveira ◽  
Carolina P. Bernardes ◽  
Danilo L. Menaldo ◽  
...  

Author(s):  
Rogério Bodini Benati ◽  
Tássia Rafaela Costa ◽  
Maira da Costa Cacemiro ◽  
Suely Vilela Sampaio ◽  
Fabíola Attié de Castro ◽  
...  

Toxins ◽  
2021 ◽  
Vol 13 (1) ◽  
pp. 60
Author(s):  
Kin Ying Wong ◽  
Kae Yi Tan ◽  
Nget Hong Tan ◽  
Choo Hock Tan

The Senegalese cobra, Naja senegalensis, is a non-spitting cobra species newly erected from the Naja haje complex. Naja senegalensis causes neurotoxic envenomation in Western Africa but its venom properties remain underexplored. Applying a protein decomplexation proteomic approach, this study unveiled the unique complexity of the venom composition. Three-finger toxins constituted the major component, accounting for 75.91% of total venom proteins. Of these, cardiotoxin/cytotoxin (~53%) and alpha-neurotoxins (~23%) predominated in the venom proteome. Phospholipase A2, however, was not present in the venom, suggesting a unique snake venom phenotype found in this species. The venom, despite the absence of PLA2, is highly lethal with an intravenous LD50 of 0.39 µg/g in mice, consistent with the high abundance of alpha-neurotoxins (predominating long neurotoxins) in the venom. The hetero-specific VINS African Polyvalent Antivenom (VAPAV) was immunoreactive to the venom, implying conserved protein antigenicity in the venoms of N. senegalensis and N. haje. Furthermore, VAPAV was able to cross-neutralize the lethal effect of N. senegalensis venom but the potency was limited (0.59 mg venom completely neutralized per mL antivenom, or ~82 LD50 per ml of antivenom). The efficacy of antivenom should be further improved to optimize the treatment of cobra bite envenomation in Africa.


2013 ◽  
Vol 73 ◽  
pp. 35-43 ◽  
Author(s):  
Lucas B. Silveira ◽  
Daniela P. Marchi-Salvador ◽  
Norival A. Santos-Filho ◽  
Floriano P. Silva ◽  
Silvana Marcussi ◽  
...  

Toxicon ◽  
2008 ◽  
Vol 51 (8) ◽  
pp. 1509-1519 ◽  
Author(s):  
Andrana K. Calgarotto ◽  
Daniela C.S. Damico ◽  
L.A. Ponce-Soto ◽  
Paulo A. Baldasso ◽  
Saulo L. Da Silva ◽  
...  

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