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Cloning and identification of a new multifunctional Ascaris-type peptide from the hemolymph of Buthus martensii Karsch.
Toxicon. 2020 Sep; 184:167-174.T

Abstract

Only a few work have been done for peptides from non-venom gland tissues of venomous animals. Here, with the help of the whole body transcriptomic and the hemolymph proteomic data of the Chinese scorpion Buthus martensii Karsch, we identified the first Ascaris-type peptide BmHDP from scorpion hemolymph. The precursor of BmHDP has 80 residues, including a 16 residue signal peptide and a 64 residue mature peptide. The mature peptide has 10 conserved cysteines and adopts a conserved Ascaris-type fold. Using combined inclusion body refolding and biochemical identification strategies, recombinant BmHDP was obtained successfully. Protease inhibitory assays showed that BmHDP inhibited chymotrypsin apparently at a concentration of 8 nM. Patch-clamp experiments showed that BmHDP inhibited the Kv1.3 potassium channel apparently at a concentration of 1000 nM. Coagulation experiment assays showed that BmHDP inhibited intrinsic coagulation pathway apparently at a concentration of 500 nM. To the best of our knowledge, BmHDP is the first Ascaris-type peptide from scorpion hemolymph. Our work highlighted a functional link between scorpion non-venom gland peptides and venom gland toxin peptides, and suggested that scorpion hemolymph might be a new source of bioactive peptides.

Authors+Show Affiliations

Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, College of Basic Medicine, Hubei University of Medicine, Hubei, China.Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, College of Basic Medicine, Hubei University of Medicine, Hubei, China.Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, College of Basic Medicine, Hubei University of Medicine, Hubei, China; Institute of Biomedicine and Hubei Key Laboratory of Wudang Local Chinese Medicine Research, Hubei University of Medicine, Hubei, China.Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, College of Basic Medicine, Hubei University of Medicine, Hubei, China; Institute of Biomedicine and Hubei Key Laboratory of Wudang Local Chinese Medicine Research, Hubei University of Medicine, Hubei, China.Department of Clinical Laboratory, Dongfeng Hospital, Hubei University of Medicine, Hubei, China; Institute of Biomedicine and Hubei Key Laboratory of Wudang Local Chinese Medicine Research, Hubei University of Medicine, Hubei, China.Department of Clinical Laboratory, Shiyan Occupational Disease Hospital, Hubei, China.Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, College of Basic Medicine, Hubei University of Medicine, Hubei, China.Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, College of Basic Medicine, Hubei University of Medicine, Hubei, China.Department of Human Parasitology, College of Basic Medical Sciences, Hubei University of Medicine, Hubei, China.Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, College of Basic Medicine, Hubei University of Medicine, Hubei, China; Institute of Biomedicine and Hubei Key Laboratory of Wudang Local Chinese Medicine Research, Hubei University of Medicine, Hubei, China. Electronic address: chenzy2005@126.com.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32565098

Citation

Zhu, Wen, et al. "Cloning and Identification of a New Multifunctional Ascaris-type Peptide From the Hemolymph of Buthus Martensii Karsch." Toxicon : Official Journal of the International Society On Toxinology, vol. 184, 2020, pp. 167-174.
Zhu W, Gao H, Luo X, et al. Cloning and identification of a new multifunctional Ascaris-type peptide from the hemolymph of Buthus martensii Karsch. Toxicon. 2020;184:167-174.
Zhu, W., Gao, H., Luo, X., Ye, X., Ding, L., Hao, J., Shu, Z., Li, S., Li, J., & Chen, Z. (2020). Cloning and identification of a new multifunctional Ascaris-type peptide from the hemolymph of Buthus martensii Karsch. Toxicon : Official Journal of the International Society On Toxinology, 184, 167-174. https://doi.org/10.1016/j.toxicon.2020.06.008
Zhu W, et al. Cloning and Identification of a New Multifunctional Ascaris-type Peptide From the Hemolymph of Buthus Martensii Karsch. Toxicon. 2020;184:167-174. PubMed PMID: 32565098.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning and identification of a new multifunctional Ascaris-type peptide from the hemolymph of Buthus martensii Karsch. AU - Zhu,Wen, AU - Gao,Huanhuan, AU - Luo,Xudong, AU - Ye,Xiangdong, AU - Ding,Li, AU - Hao,Jinbo, AU - Shu,Zhan, AU - Li,Shan, AU - Li,Jian, AU - Chen,Zongyun, Y1 - 2020/06/18/ PY - 2019/10/23/received PY - 2020/06/10/revised PY - 2020/06/15/accepted PY - 2020/6/23/pubmed PY - 2020/6/23/medline PY - 2020/6/23/entrez KW - Animal toxin KW - Anticoagulation KW - Ascaris-type KW - Potassium channel KW - Scorpion hemolymph KW - Serine protease SP - 167 EP - 174 JF - Toxicon : official journal of the International Society on Toxinology JO - Toxicon VL - 184 N2 - Only a few work have been done for peptides from non-venom gland tissues of venomous animals. Here, with the help of the whole body transcriptomic and the hemolymph proteomic data of the Chinese scorpion Buthus martensii Karsch, we identified the first Ascaris-type peptide BmHDP from scorpion hemolymph. The precursor of BmHDP has 80 residues, including a 16 residue signal peptide and a 64 residue mature peptide. The mature peptide has 10 conserved cysteines and adopts a conserved Ascaris-type fold. Using combined inclusion body refolding and biochemical identification strategies, recombinant BmHDP was obtained successfully. Protease inhibitory assays showed that BmHDP inhibited chymotrypsin apparently at a concentration of 8 nM. Patch-clamp experiments showed that BmHDP inhibited the Kv1.3 potassium channel apparently at a concentration of 1000 nM. Coagulation experiment assays showed that BmHDP inhibited intrinsic coagulation pathway apparently at a concentration of 500 nM. To the best of our knowledge, BmHDP is the first Ascaris-type peptide from scorpion hemolymph. Our work highlighted a functional link between scorpion non-venom gland peptides and venom gland toxin peptides, and suggested that scorpion hemolymph might be a new source of bioactive peptides. SN - 1879-3150 UR - https://www.unboundmedicine.com/medline/citation/32565098/Cloning_and_identification_of_a_new_multifunctional_Ascaris-type_peptide_from_the_hemolymph_of_Buthus_martensii_Karsch L2 - https://linkinghub.elsevier.com/retrieve/pii/S0041-0101(20)30287-7 DB - PRIME DP - Unbound Medicine ER -
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