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Article

Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation

1
Laboratoire des Venins et Biomolécules Thérapeutiques LR16IPT08, Université de Tunis El Manar, Institut Pasteur de Tunis, Tunis 1002, Tunisia
2
Departamento de Bioquímica e Imunologia, Universida de Federal de Minas Gerais, Belo Horizonte, Minas Gerais 31270-901, Brazil
3
Venom and Biotherapeutic Molecules Lab., Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran 13169-43551, Iran
*
Author to whom correspondence should be addressed.
Equal contribution.
Received: 21 July 2020 / Revised: 19 August 2020 / Accepted: 24 August 2020 / Published: 1 October 2020
(This article belongs to the Section Animal Venoms)
The Hemiscorpius lepturus scorpion and brown spider Loxosceles intermedia represent a public health problem in Asia and America, respectively. Although distinct, these organisms contain similar toxins responsible for the principal clinical signs of envenomation. To better understand the properties of these toxins, we designed a study to compare recombinant Heminecrolysin (rHNC) and rLiD1, the major phospholipase D toxins of scorpion and spider venom, respectively. Using a competitive ELISA and a hemolytic inhibition test, we come to spot a cross reaction between scorpion and spider venoms along with an epitopic similarity between rHNC and rLiD1 associated with neutralizing antibodies. Results show that the ability of the rHNC to hydrolyze lysophosphatidylcholine (LPC) is equivalent to that of rLiD1 to hydrolyze sphingomyelin and vice-versa. rHNC exclusively catalyze transphosphatidylation of LPC producing cyclic phosphatidic acid (cPA). The in-silico analysis of hydrogen bonds between LPC and toxins provides a possible explanation for the higher transphosphatidylase activity of rHNC. Interestingly, for the first time, we reveal that lysophosphatidic acid (LPA) can be a substrate for both enzymes using cellular and enzymatic assays. The finding of the usage of LPA as a substrate as well as the formation of cPA as an end product could shed more light on the molecular basis of Hemiscorpius lepturus envenomation as well as on loxoscelism. View Full-Text
Keywords: Hemiscorpius; Loxosceles; phospholipase D; transphosphatidylase activity; cyclic phosphatidic acid Hemiscorpius; Loxosceles; phospholipase D; transphosphatidylase activity; cyclic phosphatidic acid
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MDPI and ACS Style

Ben Yekhlef, R.; Felicori, L.; Santos, L.H.; F. B. Oliveira, C.; Fadhloun, R.; Torabi, E.; Shahbazzadeh, D.; Pooshang Bagheri, K.; Salgado Ferreira, R.; Borchani, L. Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation. Toxins 2020, 12, 631. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12100631

AMA Style

Ben Yekhlef R, Felicori L, Santos LH, F. B. Oliveira C, Fadhloun R, Torabi E, Shahbazzadeh D, Pooshang Bagheri K, Salgado Ferreira R, Borchani L. Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation. Toxins. 2020; 12(10):631. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12100631

Chicago/Turabian Style

Ben Yekhlef, Ramla, Liza Felicori, Lucianna H. Santos, Camila F. B. Oliveira, Raoudha Fadhloun, Elham Torabi, Delavar Shahbazzadeh, Kamran Pooshang Bagheri, Rafaela Salgado Ferreira, and Lamia Borchani. 2020. "Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation" Toxins 12, no. 10: 631. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12100631

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