Immobilized betulinic acid column and its interactions with phospholipase A2 and snake venom proteins

2004 ◽  
Vol 27 (14) ◽  
pp. 1215-1220 ◽  
Author(s):  
Hsiao-Chun Tseng ◽  
Yin-Chang Liu
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Betulinic Acid ◽  
Venom Proteins

Characterization of inflamin, the first member of a new family of snake venom proteins that induces inflammation

2013 ◽  
Vol 455 (2) ◽  
pp. 239-250 ◽  
Author(s):  
Bhaskar Barnwal ◽  
R. Manjunatha Kini
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Calcium Dependent ◽  
Venom Toxin ◽  
New Family ◽  
Snake Venom Toxin ◽  
Venom Proteins

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.

scholarly journals In vitro Kinetics Study of Cerastes Cerastes Phospholipase A2 using Olive Leaf Extract: A Fluorescence Approach

2018 ◽  
Vol 3 (2) ◽  
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Risk Evaluation ◽  
Therapeutic Drug ◽  
Additional Information ◽  
Zero Order Kinetics ◽  
Evaluation Strategies ◽  
In Vitro Kinetics ◽  
Venom Proteins

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.

scholarly journals A Neurotoxic Snake Venom without Phospholipase A2: Proteomics and Cross-Neutralization of the Venom from Senegalese Cobra, Naja senegalensis (Subgenus: Uraeus)

Toxins ◽  
2021 ◽  
Vol 13 (1) ◽  
pp. 60
Author(s):  
Kin Ying Wong ◽  
Kae Yi Tan ◽  
Nget Hong Tan ◽  
Choo Hock Tan
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Lethal Effect ◽  
High Abundance ◽  
Western Africa ◽  
Venom Composition ◽  
Proteomic Approach ◽  
Cross Neutralization ◽  
Naja Haje ◽  
Venom Proteins

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.

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

2006 ◽  
Vol 142 (3-4) ◽  
pp. 371-381 ◽  
Author(s):  
Rodrigo G. Stábeli ◽  
Saulo F. Amui ◽  
Carolina D. Sant'Ana ◽  
Matheus G. Pires ◽  
Auro Nomizo ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Bothrops Moojeni ◽  
Venom Proteins

Characterization of Venoms of Deinagkistrodon acutus and Bungarus multicinctus Using Proteomics and Peptidomics

2020 ◽  
Vol 17 (3) ◽  
pp. 241-254
Author(s):  
Yaqiong Zhang ◽  
Zhiping Jia ◽  
Yunyang Liu ◽  
Xinwen Zhou ◽  
Yi Kong
Keyword(s):  
Snake Venom ◽  
Protein Families ◽  
Traditional Medicines ◽  
Phospholipases A2 ◽  
Inhibitory Peptides ◽  
Sds Page ◽  
Deinagkistrodon Acutus ◽  
Venom Proteins ◽  
Proteins And Peptides

Background: Deinagkistrodon acutus (D. acutus) and Bungarus multicinctus (B. multicinctus) as traditional medicines have been used for hundreds of years in China. The venoms of these two species have strong toxicity on the victims. Objective: The objective of this study is to reveal the profile of venom proteins and peptides of D. acutus and B. multicinctus. Method: Ultrafiltration, SDS-PAGE coupled with in-gel tryptic digestion and Liquid Chromatography- Electrospray Ionization-Tandem Mass Spectrometry (LC-ESI-MS/MS) were used to characterize proteins and peptides of venoms of D. acutus and B. multicinctus. Results: In the D. acutus venom, 67 proteins (16 protein families) were identified, and snake venom metalloproteinases (SVMPs, 38.0%) and snake venom C-type lectins (snaclecs, 36.7%) were dominated proteins. In the B. multicinctus venom, 47 proteins (15 protein families) were identified, and three-finger toxins (3FTxs, 36.3%) and Kunitz-type Serine Protease Inhibitors (KSPIs, 32.8%) were major components. In addition, both venoms contained small amounts of other proteins, such as Snake Venom Serine Proteinases (SVSPs), Phospholipases A2 (PLA2s), Cysteine-Rich Secreted Proteins (CRISPs), 5'nucleotidases (5'NUCs), Phospholipases B (PLBs), Phosphodiesterases (PDEs), Phospholipase A2 Inhibitors (PLIs), Dipeptidyl Peptidases IV (DPP IVs), L-amino Acid Oxidases (LAAOs) and Angiotensin-Converting Enzymes (ACEs). Each venom also had its unique proteins, Nerve Growth Factors (NGFs) and Hyaluronidases (HYs) in D. acutus, and Cobra Venom Factors (CVFs) in B. multicinctus. In the peptidomics, 1543 and 250 peptides were identified in the venoms of D. acutus and B. multicinctus, respectively. Some peptides showed high similarity with neuropeptides, ACE inhibitory peptides, Bradykinin- Potentiating Peptides (BPPs), LAAOs and movement related peptides. Conclusion: Characterization of venom proteins and peptides of D. acutus and B. multicinctus will be helpful for the treatment of envenomation and drug discovery.

Antiangiogenic effects of phospholipase A2 Lys49 BnSP-7 from Bothrops pauloensis snake venom on endothelial cells: An in vitro and ex vivo approach

2021 ◽  
Vol 72 ◽  
pp. 105099
Author(s):  
Lorena Polloni ◽  
Fernanda Van Petten Vasconcelos Azevedo ◽  
Samuel Cota Teixeira ◽  
Eloá Moura ◽  
Tassia Rafaela Costa ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Phospholipase A2 ◽  
Snake Venom ◽  
Ex Vivo ◽  
Ex Vivo Approach

Snake Venom Proteins: Development into Antimicrobial and Wound Healing Agents

2014 ◽  
Vol 11 (1) ◽  
pp. 4-14 ◽  
Author(s):  
Ramar Samy ◽  
Jayapal Manikandan ◽  
Gautam Sethi ◽  
Octavio Franco ◽  
Josiah C. Okonkwo ◽  
...  
Keyword(s):  
Wound Healing ◽  
Snake Venom ◽  
Venom Proteins
Sign in / Sign up

Export Citation Format

Share Document