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

The <i>Hemiscorpius lepturus</i> scorpion and brown spider <i>Loxosceles intermedia</i> 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....

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Main Authors: Ramla Ben Yekhlef, Liza Felicori, Lucianna Helene Santos, Camila F. B. Oliveira, Raoudha Fadhloun, Elham Torabi, Delavar Shahbazzadeh, Kamran Pooshang Bagheri, Rafaela Salgado Ferreira, Lamia Borchani
Format: Article
Language:English
Published: MDPI AG 2020-10-01
Series:Toxins
Subjects:
Online Access:https://www.mdpi.com/2072-6651/12/10/631
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spelling doaj-df95f9ccb2784ca3962ffbbe2778452f2020-11-25T02:50:03ZengMDPI AGToxins2072-66512020-10-011263163110.3390/toxins12100631Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative InvestigationRamla Ben Yekhlef0Liza Felicori1Lucianna Helene Santos2Camila F. B. Oliveira3Raoudha Fadhloun4Elham Torabi5Delavar Shahbazzadeh6Kamran Pooshang Bagheri7Rafaela Salgado Ferreira8Lamia Borchani9Laboratoire des Venins et Biomolécules Thérapeutiques LR16IPT08, Université de Tunis El Manar, Institut Pasteur de Tunis, Tunis 1002, TunisiaDepartamento de Bioquímica e Imunologia, Universida de Federal de Minas Gerais, Belo Horizonte, Minas Gerais 31270-901, BrazilDepartamento de Bioquímica e Imunologia, Universida de Federal de Minas Gerais, Belo Horizonte, Minas Gerais 31270-901, BrazilDepartamento de Bioquímica e Imunologia, Universida de Federal de Minas Gerais, Belo Horizonte, Minas Gerais 31270-901, BrazilLaboratoire des Venins et Biomolécules Thérapeutiques LR16IPT08, Université de Tunis El Manar, Institut Pasteur de Tunis, Tunis 1002, TunisiaVenom and Biotherapeutic Molecules Lab., Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran 13169-43551, IranVenom and Biotherapeutic Molecules Lab., Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran 13169-43551, IranVenom and Biotherapeutic Molecules Lab., Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran 13169-43551, IranDepartamento de Bioquímica e Imunologia, Universida de Federal de Minas Gerais, Belo Horizonte, Minas Gerais 31270-901, BrazilLaboratoire des Venins et Biomolécules Thérapeutiques LR16IPT08, Université de Tunis El Manar, Institut Pasteur de Tunis, Tunis 1002, TunisiaThe <i>Hemiscorpius lepturus</i> scorpion and brown spider <i>Loxosceles intermedia</i> 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 <i>Hemiscorpius lepturus</i> envenomation as well as on loxoscelism.https://www.mdpi.com/2072-6651/12/10/631<i>Hemiscorpius</i><i>Loxosceles</i>phospholipase Dtransphosphatidylase activitycyclic phosphatidic acid
collection DOAJ
language English
format Article
sources DOAJ
author Ramla Ben Yekhlef
Liza Felicori
Lucianna Helene Santos
Camila F. B. Oliveira
Raoudha Fadhloun
Elham Torabi
Delavar Shahbazzadeh
Kamran Pooshang Bagheri
Rafaela Salgado Ferreira
Lamia Borchani
spellingShingle Ramla Ben Yekhlef
Liza Felicori
Lucianna Helene Santos
Camila F. B. Oliveira
Raoudha Fadhloun
Elham Torabi
Delavar Shahbazzadeh
Kamran Pooshang Bagheri
Rafaela Salgado Ferreira
Lamia Borchani
Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation
Toxins
<i>Hemiscorpius</i>
<i>Loxosceles</i>
phospholipase D
transphosphatidylase activity
cyclic phosphatidic acid
author_facet Ramla Ben Yekhlef
Liza Felicori
Lucianna Helene Santos
Camila F. B. Oliveira
Raoudha Fadhloun
Elham Torabi
Delavar Shahbazzadeh
Kamran Pooshang Bagheri
Rafaela Salgado Ferreira
Lamia Borchani
author_sort Ramla Ben Yekhlef
title Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation
title_short Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation
title_full Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation
title_fullStr Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation
title_full_unstemmed Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation
title_sort antigenic and substrate preference differences between scorpion and spider dermonecrotic toxins, a comparative investigation
publisher MDPI AG
series Toxins
issn 2072-6651
publishDate 2020-10-01
description The <i>Hemiscorpius lepturus</i> scorpion and brown spider <i>Loxosceles intermedia</i> 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 <i>Hemiscorpius lepturus</i> envenomation as well as on loxoscelism.
topic <i>Hemiscorpius</i>
<i>Loxosceles</i>
phospholipase D
transphosphatidylase activity
cyclic phosphatidic acid
url https://www.mdpi.com/2072-6651/12/10/631
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