Recombinant expression and antigenicity of two peptide families of neurotoxins from

Androctonus Antibodies Protein expression Scorpion venom

Journal

The journal of venomous animals and toxins including tropical diseases
ISSN: 1678-9199
Titre abrégé: J Venom Anim Toxins Incl Trop Dis
Pays: Brazil
ID NLM: 101201501

Informations de publication

Date de publication:
2022
Historique:
received: 26 05 2022
accepted: 23 09 2022
entrez: 29 12 2022
pubmed: 30 12 2022
medline: 30 12 2022
Statut: epublish

Résumé

Scorpion neurotoxins such as those that modify the mammalian voltage-gated sodium ion channels (Nav) are the main responsible for scorpion envenomation. Their neutralization is crucial in the production of antivenoms against scorpion stings. In the present study, two Following bacterial expression, the two expressed neurotoxins, hereafter named HisrAcra4 and HisrSccTx, were obtained from inclusion bodies. Both recombinant neurotoxins were obtained in multiple Cys-Cys isoforms. After refolding, the active protein fractions were identified with molecular masses of 8,947.6 and 9,989.1 Da for HisrAcra4 and HisrSccTx, respectively, which agreed with their expected theoretical masses. HisrAcra4 and HisrSccTx were used as antigens to immunize two groups of rabbits, to produce either anti-HisrAcra4 or anti-HisrSccTx serum antibodies, which in turn could recognize and neutralize neurotoxins from venoms of scorpion species from the Middle East and North Africa. The antibodies obtained from rabbits neutralized the 3LD Two recombinant Nav neurotoxins, from different peptide families, were used as antigens to generate IgGs for neutralizing scorpion venoms of species from the Middle East and North Africa.

Sections du résumé

Background UNASSIGNED
Scorpion neurotoxins such as those that modify the mammalian voltage-gated sodium ion channels (Nav) are the main responsible for scorpion envenomation. Their neutralization is crucial in the production of antivenoms against scorpion stings.
Methods UNASSIGNED
In the present study, two
Results UNASSIGNED
Following bacterial expression, the two expressed neurotoxins, hereafter named HisrAcra4 and HisrSccTx, were obtained from inclusion bodies. Both recombinant neurotoxins were obtained in multiple Cys-Cys isoforms. After refolding, the active protein fractions were identified with molecular masses of 8,947.6 and 9,989.1 Da for HisrAcra4 and HisrSccTx, respectively, which agreed with their expected theoretical masses. HisrAcra4 and HisrSccTx were used as antigens to immunize two groups of rabbits, to produce either anti-HisrAcra4 or anti-HisrSccTx serum antibodies, which in turn could recognize and neutralize neurotoxins from venoms of scorpion species from the Middle East and North Africa. The antibodies obtained from rabbits neutralized the 3LD
Conclusions UNASSIGNED
Two recombinant Nav neurotoxins, from different peptide families, were used as antigens to generate IgGs for neutralizing scorpion venoms of species from the Middle East and North Africa.

Identifiants

pubmed: 36578820
doi: 10.1590/1678-9199-JVATITD-2022-0026
pmc: PMC9769139
doi:

Types de publication

Journal Article

Langues

eng

Pagination

e20220026

Déclaration de conflit d'intérêts

Competing interests: The authors declare that they have no competing interests

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Auteurs

Samuel Cardoso-Arenas (S)

Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico (UNAM), Cuernavaca, Morelos, Mexico.

Herlinda Clement (H)

Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico (UNAM), Cuernavaca, Morelos, Mexico.

Iván Arenas (I)

Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico (UNAM), Cuernavaca, Morelos, Mexico.

Felipe Olvera (F)

Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico (UNAM), Cuernavaca, Morelos, Mexico.

Fernando Zamudio (F)

Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico (UNAM), Cuernavaca, Morelos, Mexico.

Figen Caliskan (F)

Department of Biology, Faculty of Science and Letters, Eskisehir Osmangazi University, Eskisehir, Turkey.

Ligia Luz Corrales-García (LL)

Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico (UNAM), Cuernavaca, Morelos, Mexico.
Department of Food Sciences, School of Pharmaceutical and Food Sciences, University of Antioquia (UdeA), Medellín, Colombia.

Gerardo Corzo (G)

Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico (UNAM), Cuernavaca, Morelos, Mexico.

Classifications MeSH