Hemilipin, a novel Hemiscorpius lepturus venom heterodimeric phospholipase A2, which inhibits angiogenesis in vitro and in vivo

Jridi, I.; Catacchio, Ivana; Majdoub, Hafedh; Shahbazeddah, Delavar; Ayeb, Mohamed El; Frassanito, Maria Antonia; Ribatti, Doménico; Vacca, Angelo; Borchani, Lamia

doi:10.1016/j.toxicon.2015.08.022

Cited by 38 publications

(27 citation statements)

References 35 publications

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“…H. lepturus venom is very toxic and some of its peptide and protein components have been completely or partially characterized, such as Hemitoxin [29], Hemicalcin [6], Heminecrolysin [27] and Hemilipin [30]. …”

Section: Discussionmentioning

confidence: 99%

Characteristics and Lethality of a Novel Recombinant Dermonecrotic Venom Phospholipase D from Hemiscorpius lepturus

Torabi

Behdani

Chafi

et al. 2017

Toxins

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Hemoscorpius lepturus is the most medically important scorpion in Iran. The clinical signs of H. lepturus envenomation are remarkably similar to those reported for brown spiders, including dermonecrosis, hematuria, renal failure and even death. The lethality and toxicity of brown spiders’ venom have been attributed to its phospholipase D activity. This study aims to identify a phospholipase D with possible lethality and dermonecrotic activity in H. lepturus venom. In this study, a cDNA library of the venom glands was generated by Illumina RNA sequencing. Phospholipase D (PLD) from H. lepturus was characterized according to its significant similarity with PLDs from brown spiders. The main chain designated as Hl-RecPLD1 (the first recombinant isoform of H. lepturus PLD) was cloned, expressed and purified. Sphingomyelinase, dermonecrotic and lethal activities were examined. Hl-PLD1 showed remarkable sequence similarity and structural homology with PLDs of brown spiders. The conformation of Hl-PLD1 was predicted as a “TIM beta/alpha-barrel”. The lethal dose 50 (LD50) and dermonecrotic activities of Hl-RecPLD1 were determined as 3.1 µg/mouse and 0.7 cm2 at 1 µg respectively. It is the first report indicating that a similar molecular evolutionary mechanism has occurred in both American brown spiders and this Iranian scorpion. In conclusion, Hl-RecPLD1 is a highly active phospholipase D, which would be considered as the lethal dermonecrotic toxin in H. lepturus venom.

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Section: Discussionmentioning

confidence: 99%

Characteristics and Lethality of a Novel Recombinant Dermonecrotic Venom Phospholipase D from Hemiscorpius lepturus

Torabi

Behdani

Chafi

et al. 2017

Toxins

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“…The pathological effects of H.lepturus are different of other scorpions and results in failure of kidney, liver as well as blood cells [1]. Various studies have evaluated the venom component of H.lepturus and various toxic peptides and proteins of H.lepturus have been identi ied like: hemitoxin [2], hemicalcin [3], heminecrolysin [4] and hemilipin [5]. Transcriptome analysis of venom gland of H.lepturus was performed in previous study and whole venom component of this scorpion was identi ied [6].…”

Section: Introductionmentioning

confidence: 99%

Phylogenetic analysis of metalloprotease from transcriptome of venom gland of Hemiscorpius lepturus

Kazemi‐Lomedasht¹,

Shahbazzadeh²,

Behdani³

2019

Arch Biotechnol Biomed

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Hemiscorpius lepturus is a dangerous scorpion and referred to health concern issue in Khuzestan, Iran. The venom of H.lepturus is cytotoxic and its effect is similar to spider Loxosceles reclusa. Metalloproteinases are the important class of enzymes in the venom that has hemorrhagic activity. The early fi nding suggests the existence of metalloproteases in the transcriptome of venom gland of H.lepturus. Phylogenetic analysis was accomplished to reveal the evolutionary relationship of identifi ed metalloproteases. The phylogenetic tree was constructed by Molecular Evolutionary Genetics Analysis software and neighbor-joining method. Results showed among three sequences, two metalloproteinases named HLMP1 and HLMP3 of H.lepturus were most close to spider P. tepidariorum. The third sequence named HLMP2 was different and formed an independent clade in the phylogenetic tree. The results suggest that the sequence of metalloproteases in the venom component of H.lepturus is similar to the spider than the scorpion.

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“…Group III PLA 2 have been identified in many other species [13][14][15] like scorpion [16][17][18][19], gila monster [20], lizards [21] and human [22]. They are involved in inflammation [23,24], apoptosis [25] and cancer [26,27]. Group III sPLA 2 contain ten cysteines and are composed of one or two chains.…”

Section: Introductionmentioning

confidence: 99%

“…Pandinus imperator [30], Phaiodactylipin from Anuroctonus phaiodactylus [17], Heteromtoxin (HmTx) from Heterometrus laoticus [18], Hemilipin from Hemiscorpius lepturus [27] and Sm-PLVG from Scorpio maurus [31].…”

Section: Introductionmentioning

confidence: 99%

Functional characterization and FTIR-based 3D modeling of full length and truncated forms of Scorpio maurus venom phospholipase A 2

Krayem

Parsiegla

Gaussier

et al. 2018

Biochimica et Biophysica Acta (BBA) - General Subjects

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Hemilipin, a novel Hemiscorpius lepturus venom heterodimeric phospholipase A2, which inhibits angiogenesis in vitro and in vivo

Cited by 38 publications

References 35 publications

Characteristics and Lethality of a Novel Recombinant Dermonecrotic Venom Phospholipase D from Hemiscorpius lepturus

Characteristics and Lethality of a Novel Recombinant Dermonecrotic Venom Phospholipase D from Hemiscorpius lepturus

Phylogenetic analysis of metalloprotease from transcriptome of venom gland of Hemiscorpius lepturus

Functional characterization and FTIR-based 3D modeling of full length and truncated forms of Scorpio maurus venom phospholipase A 2

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