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Peptide-rich venom from the spider Heteropoda venatoria potently inhibits insect voltage-gated sodium channels.
Toxicon. 2017 Jan; 125:44-49.T

Abstract

Heteropoda venatoria is a venomous spider species distributed worldwide and has a characteristic habit of feeding on insects. Reverse-phase high-performance liquid chromatography and matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry analyses revealed that H. venatoria venom contains hundreds of peptides with a predominant molecular weights of 3000-5000 Da. Intra-abdominal injection of the venom had severe toxic effects on cockroaches and caused death at higher concentrations. The LD50 was 28.18 μg/g of body weight in the cockroach. It was found that the venom had potent inhibitory effect on voltage-gated sodium channels (VGSCs) in Periplaneta americana cockroach dorsal unpaired median (DUM) neurons with an IC50 values of 6.25 ± 0.02 μg/mL. However, 100 μg/mL venom only partially blocked VGSC currents in rat dorsal root ganglion cells, a much lower inhibitory effect than that on DUM VGSCs. Our results indicate that the venom of H. venatoria contains diverse neurotoxins that might become new leads for bioinsecticides.

Authors+Show Affiliations

The National & Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China.The National & Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China.The National & Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China.The National & Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China.The National & Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China.The National & Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China.The National & Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China.The National & Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China; The Key Laboratory of Protein Chemistry and Developmental Biology of the Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China.The National & Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China; The Key Laboratory of Protein Chemistry and Developmental Biology of the Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China. Electronic address: liuzh@hunnu.edu.cn.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

27867092

Citation

Huang, Yazhou, et al. "Peptide-rich Venom From the Spider Heteropoda Venatoria Potently Inhibits Insect Voltage-gated Sodium Channels." Toxicon : Official Journal of the International Society On Toxinology, vol. 125, 2017, pp. 44-49.
Huang Y, Wu X, Zhang P, et al. Peptide-rich venom from the spider Heteropoda venatoria potently inhibits insect voltage-gated sodium channels. Toxicon. 2017;125:44-49.
Huang, Y., Wu, X., Zhang, P., Duan, Z., Zhou, X., Chen, M., Farooq, A., Liang, S., & Liu, Z. (2017). Peptide-rich venom from the spider Heteropoda venatoria potently inhibits insect voltage-gated sodium channels. Toxicon : Official Journal of the International Society On Toxinology, 125, 44-49. https://doi.org/10.1016/j.toxicon.2016.11.252
Huang Y, et al. Peptide-rich Venom From the Spider Heteropoda Venatoria Potently Inhibits Insect Voltage-gated Sodium Channels. Toxicon. 2017;125:44-49. PubMed PMID: 27867092.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Peptide-rich venom from the spider Heteropoda venatoria potently inhibits insect voltage-gated sodium channels. AU - Huang,Yazhou, AU - Wu,Xinzhou, AU - Zhang,Peng, AU - Duan,Zhigui, AU - Zhou,Xi, AU - Chen,Minzhi, AU - Farooq,Athar, AU - Liang,Songping, AU - Liu,Zhonghua, Y1 - 2016/11/17/ PY - 2016/07/01/received PY - 2016/09/21/revised PY - 2016/11/16/accepted PY - 2016/11/22/pubmed PY - 2017/7/25/medline PY - 2016/11/22/entrez KW - Dorsal unpaired median neurons KW - H. venatoria venom KW - Insecticides KW - Voltage-gated sodium channels SP - 44 EP - 49 JF - Toxicon : official journal of the International Society on Toxinology JO - Toxicon VL - 125 N2 - Heteropoda venatoria is a venomous spider species distributed worldwide and has a characteristic habit of feeding on insects. Reverse-phase high-performance liquid chromatography and matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry analyses revealed that H. venatoria venom contains hundreds of peptides with a predominant molecular weights of 3000-5000 Da. Intra-abdominal injection of the venom had severe toxic effects on cockroaches and caused death at higher concentrations. The LD50 was 28.18 μg/g of body weight in the cockroach. It was found that the venom had potent inhibitory effect on voltage-gated sodium channels (VGSCs) in Periplaneta americana cockroach dorsal unpaired median (DUM) neurons with an IC50 values of 6.25 ± 0.02 μg/mL. However, 100 μg/mL venom only partially blocked VGSC currents in rat dorsal root ganglion cells, a much lower inhibitory effect than that on DUM VGSCs. Our results indicate that the venom of H. venatoria contains diverse neurotoxins that might become new leads for bioinsecticides. SN - 1879-3150 UR - https://www.unboundmedicine.com/medline/citation/27867092/Peptide_rich_venom_from_the_spider_Heteropoda_venatoria_potently_inhibits_insect_voltage_gated_sodium_channels_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0041-0101(16)30584-0 DB - PRIME DP - Unbound Medicine ER -