Molecular characterization of a novel secretory phospholipase A2 as coding gene from venom glands of Iranian Scorpio maurus (Arachnida: Scorpionidae)

Abstract

Background Scorpions as a venomous arthropod can defend and capture the prey by secretion of venom into their venomic sacs. The venom is a mixture of a variety of compounds with specific biological activities, such as phospholipase A2 (PLA2) enzyme to be present in scorpion venom. This study is the first investigation of structural and molecular characterization of PLA2 from Iranian scorpion, S. maurus that can be added to the literature when targeting molecular characterization of PLA2 coding gene from venom glands of Iranian S. maurus. Results S. maurus PLA2 with 432 base pair (bp) nucleotide length encoded a protein of 144 amino acid residues and 16.34 kilodaltons (kDa). According to DiANNA 1.1 web server prediction, this protein had 5 disulfide bridges. The deposited PLA2 in GenBank (MW241004) was very similar to S. maurus (MF347455.1) with 95.14% identity. The phylogenetic analysis indicated that our PLA2 had a close relationship with insect PLA2. Our PLA2 had 38.83% identity with bee venom PLA2 according to SWISS-MODEL prediction and 100% confidence and 39% identity with insect phospholipase A2 family, which was predicted by Phyre2. Our PLA2 was similar to chain A of bee venom PLA2. Conserved domains on target PLA2 contained 17–118 amino acid in length and 45–52 amino acids in the active site. There was no signal peptide. Conclusions In the light of our results, the coding sequence of characterized PLA2 was a member of the PLA2 superfamily. According to the three-dimensional structure prediction, the target PLA2 with five disulfide bonds has a very high similarity to the structure of phospholipase A2 belonged to the group III subfamily. Interestingly, the active site residue of target PLA2 also has the His-Asp acid pair and the effective amino acid in catalytic domain of it was\({\text{H}\text{i}\text{s}}^{49}\).

Whole transcriptome sequencing reveals the activity of the PLA2 family members in Androctonus crassicauda (Scorpionida: Buthidae) venom gland

“…Consistent with this study, scorpion venom sPLA2s are among the venom proteins that have already been well studied and characterized in various scorpion species, including Pandinus imperator (IpTxi 15 kDa) , Hemiscorpius lepturus (Hemilipin 1, 2 ~ 15 kDa) , Anuroctonus phaiodactylus (Phaiodactylipin 19.1 kDa) , Heterometrus fulvipes (HfPLA2 16 kDa), Heterometrus laoticus (HmTx 14 kDa) , Scorpio maurus (Phospholipin 14.8 kDa, Sm‐PLGV 15 kDa) 10,17,19 …”

“…[13][14][15][16] The catalytic activity of the PLA2s triggers a cascade of inflammatory events including release of a complex network of inflammatory mediators. 17,19 The existing literature demonstrates that the sPLA2 subfamily catalyzes the hydrolysis of the sn-2 fatty acid bond of phospholipids, releasing free fatty acids and lysophospholipids. 11,17,19 Free fatty acids can be converted into bioactive metabolites eicosanoids, which act as potent mediators of inflammation.…”

“…17,19 The existing literature demonstrates that the sPLA2 subfamily catalyzes the hydrolysis of the sn-2 fatty acid bond of phospholipids, releasing free fatty acids and lysophospholipids. 11,17,19 Free fatty acids can be converted into bioactive metabolites eicosanoids, which act as potent mediators of inflammation. 11 The cPLA2 and iPLA2 subfamilies by production of the free arachidonic acid from membrane phospholipids, [20][21][22] and lipid hydrolase or transacylase/acyltransferase activities respectively, play essential roles in the generation of inflammatory events.…”

Molecular Characterization and In Silico Analyses of Maurolipin Structure as a Secretory Phospholipase A 2 (

“…(Arachnida: Scorpionidae)" according to the following link https://www.researchsquare.com/article/rs-549530/v1 [56].…”

“…This investigation was funded by Shiraz University of Medical Sciences (SUMS), Shiraz, Iran (Grant No: 98-01-04–20786). This article previously had been located, online, as preprint in the Research Gate entitled “Molecular characterization of a novel secretory phospholipase A 2 as coding gene from venom glands of Iranian Scorpio maurus (Arachnida: Scorpionidae)” according to the following link https://www.researchsquare.com/article/rs-549530/v1 [ 56 ].…”