scholarly journals A New Group II Phospholipase A2 from Walterinnesia aegyptia Venom with Antimicrobial, Antifungal, and Cytotoxic Potential

Processes ◽  
2020 ◽  
Vol 8 (12) ◽  
pp. 1560
Author(s):  
Islem Abid ◽  
Ikram Jemel ◽  
Mona Alonazi ◽  
Abir Ben Bacha
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Specific Activity ◽  
Industrial Effluents ◽  
Phospholipases A2 ◽  
Microbial Infections ◽  
Snake Venom Phospholipase ◽  
Terminal Amino ◽  
Group Ii ◽  
Cancerous Cells

Many venomous species, especially snakes, contain a variety of secreted phospholipases A2 that contribute to venom toxicity and prey digestion. We characterized a novel highly toxic phospholipase A2 of group II, WaPLA2-II, from the snake venom of Saudi Walterinnesia aegyptia (W. aegyptia). The enzyme was purified using a reverse phase C18 column. It is a monomeric protein with a molecular weight of approximately 14 kDa and an NH2-terminal amino acid sequence exhibiting similarity to the PLA2 group II enzymes. WaPLA2-II, which contains 2.5% (w/w) glycosylation, reached a maximal specific activity of 1250 U/mg at pH 9.5 and 55 °C in the presence of Ca2+ and bile salts. WaPLA2-II was also highly stable over a large pH and temperature range. A strong correlation between antimicrobial and indirect hemolytic activities of WaPLA2 was observed. Additionally, WaPLA2-II was found to be significantly cytotoxic only on cancerous cells. However, chemical modification with para-Bromophenacyl bromide (p-BPB) inhibited WaPLA2-II enzymatic activity without affecting its antitumor effect, suggesting the presence of a separate ‘pharmacological site’ in snake venom phospholipase A2 via its receptor binding affinity. This enzyme is a candidate for applications including the treatment of phospholipid-rich industrial effluents and for the food production industry. Furthermore, it may represent a new therapeutic lead molecule for treating cancer and microbial infections.

scholarly journals Two phospholipase A2 inhibitors from the plasma of Cerrophidion (Bothrops) godmani which selectively inhibit two different group-II phospholipase A2 myotoxins from its own venom: isolation, molecular cloning and biological properties

2000 ◽  
Vol 346 (3) ◽  
pp. 631-639 ◽  
Author(s):  
Sergio LIZANO ◽  
Yamileth ANGULO ◽  
Bruno LOMONTE ◽  
Jay W. FOX ◽  
Gérard LAMBEAU ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Biological Properties ◽  
Amino Acid Sequence Analysis ◽  
Terminal Amino Acid ◽  
Phospholipases A2 ◽  
Terminal Amino ◽  
Group Ii ◽  
Inhibition Studies ◽  
Phospholipase A2 Inhibitors ◽  
Insight Into

Myotoxic phospholipases A2 (PLA2s; group II) account for most of the muscle-tissue damage that results from envenomation by viperid snakes. In the venom of the Godman's viper (Cerrophidion godmani, formerly Bothrops godmani), an enzymically active PLA2 (myotoxin I) and an inactive, Lys-49 variant (myotoxin II) induce extensive muscle damage and oedema. In this study, two distinct myotoxin inhibitor proteins of C. godmani, CgMIP-I and CgMIP-II, were purified directly from blood plasma by selective binding to affinity columns containing either myotoxin I or myotoxin II, respectively. Both proteins are glycosylated, acidic (pI = 4) and composed of 20-25-kDa subunits that form oligomers of 110 kDa (CgMIP-I) or 180 kDa (CgMIP-II). In inhibition studies, CgMIP-I specifically neutralized the PLA2 and the myotoxic, oedema-forming and cytolytic activities of myotoxins I, whereas CgMIP-II selectively inhibited the toxic properties of myotoxin II. N-terminal amino acid sequence analysis and sequencing of cDNAs encoding the two inhibitors revealed that CgMIP-I is similar to γ-type inhibitors, which share a pattern of cysteine residues present in the Ly-6 superfamily of proteins, whereas CgMIP-II shares sequence identity with α-type inhibitors that contain carbohydrate-recognition-like domains, also found in C-type lectins and mammalian PLA2 receptors. N-terminal sequencing of myotoxin I revealed a different primary structure from myotoxin II [De Sousa, Morhy, Arni, Ward, Díaz and Gutiérrez (1998) Biochim. Biophys. Acta 1384, 204-208], which provides insight into the nature of such pharmacological specificity.

Snake Venom Phospholipase A2 Enzymes

2009 ◽  
pp. 173-205 ◽  
Author(s):  
Xingding Zhou ◽  
R Manjunatha Kini ◽  
Robin Doley
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Snake Venom Phospholipase

Systemic and local myotoxicity induced by snake venom group II phospholipases A2: Comparison between crotoxin, crotoxin B and a Lys49 PLA2 homologue

Toxicon ◽  
2008 ◽  
Vol 51 (1) ◽  
pp. 80-92 ◽  
Author(s):  
José María Gutiérrez ◽  
Luis Alberto Ponce-Soto ◽  
Sergio Marangoni ◽  
Bruno Lomonte
Keyword(s):  
Snake Venom ◽  
Phospholipases A2 ◽  
Group Ii
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