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β/δ-PrIT1, a highly insecticidal toxin from the venom of the Brazilian spider Phoneutria reidyi (F.O. Pickard-Cambridge, 1897).
Toxicon. 2015 Sep 15; 104:73-82.T

Abstract

A potent insecticidal toxin, β/δ-PrIT1, molecular mass of 5598.86 [M+H](+), was characterized from Phoneutria reidyi spider venom. Its partial amino acid sequence showed high similarity with insecticidal spider toxins from the genus Phoneutria. β/δ-PrIT1 was very toxic (LD50 = 4 nmol/g) to flies (Musca domestica), but not to mice (Mus musculus). Kinetic studies showed that (125)I-β/δ-PrIT1 binds to two distinct sites in insect sodium channels, with close affinity (Kd1 = 34.7 pM and Kd2 = 35.1 pM). Its association is rather fast (t1/2(1) = 1.4 min, t1/2(2) = 8.5 min) and its dissociation is a slower process (t1/2(1) = 5.4 min, t1/2(2) = 32.8 min). On rat brain synaptosomes β/δ-PrIT1 partially competed (∼30%) with the beta-toxin (125)I-CssIV, but did not compete with the alpha-toxin of reference (125)I-AaII, nor with the beta-toxin (125)I-TsVII. On cockroach nerve cord synaptosomes, β/δ-PrIT1 did not compete with the anti-insect toxin (125)I-LqqIT1, but it competed (IC50 = 80 pM) with the "alpha-like" toxin (125)I-BomIV. In cockroach neurons, β/δ-PrIT1 inhibited the inactivation of Nav-channels and it shifted the sodium channel activation to hyperpolarizing potentials. These results indicate two different binding sites for β/δ-PrIT1, leading to two different pharmacological responses. β/δ-PrIT1 is one of the most toxic spider toxins to insects without apparent toxicity to mammals, and provide new model for the development of insecticides.

Authors+Show Affiliations

Departamento de Farmácia, Universidade Federal dos Vales do Jequitinhonha e Mucuri, Rua da Glória, 187 - Centro, 39100-000 Diamantina, MG, Brazil; Departamento de Fisiologia e Biofísica, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, 31270-901 Belo Horizonte, MG, Brazil.Departamento de Bioquímica e Imunologia, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, 31270-901 Belo Horizonte, MG, Brazil.Departamento de Ciências Fisiológicas, Centro de Ciências da Saúde, Universidade Federal do Espírito Santo, Avenida Marechal Campos, 1468, 29043-900, Maruípe, Vitória, ES, Brazil.Centro de Pesquisa e Desenvolvimento "Prof. Carlos Ribeiro Diniz", Fundação Ezequiel Dias, Rua Conde Pereira Carneiro, 80, 30550-010 Belo Horizonte, MG, Brazil.Departamento de Fisiologia e Biofísica, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, 31270-901 Belo Horizonte, MG, Brazil.Centro de Pesquisa e Desenvolvimento "Prof. Carlos Ribeiro Diniz", Fundação Ezequiel Dias, Rua Conde Pereira Carneiro, 80, 30550-010 Belo Horizonte, MG, Brazil.Departamento de Bioquímica e Imunologia, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, 31270-901 Belo Horizonte, MG, Brazil.Aix-Marseille University, CNRS UMR 7286, CRN2M, School of Medicine, Bd Pierre Dramard, 13916 Marseille Cedex 20, France.Departamento de Bioquímica e Imunologia, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, 31270-901 Belo Horizonte, MG, Brazil.Departamento de Bioquímica e Imunologia, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, 31270-901 Belo Horizonte, MG, Brazil. Electronic address: melenalima@icb.ufmg.br.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

26220799

Citation

de Oliveira, Leida Calegário, et al. "Β/δ-PrIT1, a Highly Insecticidal Toxin From the Venom of the Brazilian Spider Phoneutria Reidyi (F.O. Pickard-Cambridge, 1897)." Toxicon : Official Journal of the International Society On Toxinology, vol. 104, 2015, pp. 73-82.
de Oliveira LC, Campos FV, Figueiredo SG, et al. Β/δ-PrIT1, a highly insecticidal toxin from the venom of the Brazilian spider Phoneutria reidyi (F.O. Pickard-Cambridge, 1897). Toxicon. 2015;104:73-82.
de Oliveira, L. C., Campos, F. V., Figueiredo, S. G., Cordeiro, M. N., Adaime, B. R., Richardson, M., Pimenta, A. M., Martin-Eauclaire, M. F., Beirão, P. S., & De Lima, M. E. (2015). Β/δ-PrIT1, a highly insecticidal toxin from the venom of the Brazilian spider Phoneutria reidyi (F.O. Pickard-Cambridge, 1897). Toxicon : Official Journal of the International Society On Toxinology, 104, 73-82. https://doi.org/10.1016/j.toxicon.2015.07.010
de Oliveira LC, et al. Β/δ-PrIT1, a Highly Insecticidal Toxin From the Venom of the Brazilian Spider Phoneutria Reidyi (F.O. Pickard-Cambridge, 1897). Toxicon. 2015 Sep 15;104:73-82. PubMed PMID: 26220799.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - β/δ-PrIT1, a highly insecticidal toxin from the venom of the Brazilian spider Phoneutria reidyi (F.O. Pickard-Cambridge, 1897). AU - de Oliveira,Leida Calegário, AU - Campos,Fabiana V, AU - Figueiredo,Suely Gomes, AU - Cordeiro,Marta N, AU - Adaime,Beatriz R, AU - Richardson,Michael, AU - Pimenta,Adriano M C, AU - Martin-Eauclaire,Marie-France, AU - Beirão,Paulo S L, AU - De Lima,Maria Elena, Y1 - 2015/07/26/ PY - 2015/02/03/received PY - 2015/06/08/revised PY - 2015/07/16/accepted PY - 2015/7/30/entrez PY - 2015/7/30/pubmed PY - 2016/7/21/medline KW - Anti-insect toxins KW - Phoneutria reidyi KW - Spider venoms KW - Voltage-gated sodium channels SP - 73 EP - 82 JF - Toxicon : official journal of the International Society on Toxinology JO - Toxicon VL - 104 N2 - A potent insecticidal toxin, β/δ-PrIT1, molecular mass of 5598.86 [M+H](+), was characterized from Phoneutria reidyi spider venom. Its partial amino acid sequence showed high similarity with insecticidal spider toxins from the genus Phoneutria. β/δ-PrIT1 was very toxic (LD50 = 4 nmol/g) to flies (Musca domestica), but not to mice (Mus musculus). Kinetic studies showed that (125)I-β/δ-PrIT1 binds to two distinct sites in insect sodium channels, with close affinity (Kd1 = 34.7 pM and Kd2 = 35.1 pM). Its association is rather fast (t1/2(1) = 1.4 min, t1/2(2) = 8.5 min) and its dissociation is a slower process (t1/2(1) = 5.4 min, t1/2(2) = 32.8 min). On rat brain synaptosomes β/δ-PrIT1 partially competed (∼30%) with the beta-toxin (125)I-CssIV, but did not compete with the alpha-toxin of reference (125)I-AaII, nor with the beta-toxin (125)I-TsVII. On cockroach nerve cord synaptosomes, β/δ-PrIT1 did not compete with the anti-insect toxin (125)I-LqqIT1, but it competed (IC50 = 80 pM) with the "alpha-like" toxin (125)I-BomIV. In cockroach neurons, β/δ-PrIT1 inhibited the inactivation of Nav-channels and it shifted the sodium channel activation to hyperpolarizing potentials. These results indicate two different binding sites for β/δ-PrIT1, leading to two different pharmacological responses. β/δ-PrIT1 is one of the most toxic spider toxins to insects without apparent toxicity to mammals, and provide new model for the development of insecticides. SN - 1879-3150 UR - https://www.unboundmedicine.com/medline/citation/26220799/β/δ_PrIT1_a_highly_insecticidal_toxin_from_the_venom_of_the_Brazilian_spider_Phoneutria_reidyi__F_O__Pickard_Cambridge_1897__ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0041-0101(15)30019-2 DB - PRIME DP - Unbound Medicine ER -