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General mechanism of spider toxin family I acting on sodium channel Nav1.7

Zoological Research 2022年第5期43卷 886-896页

作者： Fu-Chu Yuan Fu-De Sun Lin Zhang Biao Huang Hai-Long An Ming-Qiang Rong Can-Wei Du National&Local Joint Engineering Laboratory of Animal peptide Drug Development College of Life SciencesHunan Normal UniversityChangshaHunan 410006China Key Laboratory of Molecular Biophysics Hebei ProvinceInstitute of BiophysicsSchool of Health Science&Biomedical EngineeringHebei University of TechnologyTianjin 300401China Chengdu Pepbiomedical Co. Ltd.ChengduSichuan 610219China

Various peptide toxins in animal venom inhibit voltage-gated sodium ion channel Nav1.7, including Nav-targeting spider toxin(NaSpTx) Family I. toxins in NaSpTx Family I share a similar structure, i.e., Nterminal, loops 1–4, and C-terminal. Here, we used Mu-theraphotoxin-Ca2a(Ca2a), a peptide isolated from Cyriopagopus albostriatus, as a template to investigate the general properties of toxins in NaSpTx Family I. The toxins interacted with the cell membrane prior to binding to Nav1.7 via similar hydrophobic residues. Residues in loop 1, loop 4,and the C-terminal primarily interacted with the S3–S4 linker of domain II, especially basic amino acids binding to E818. We also identified the critical role of loop 2 in Ca2a regarding its affinity to Nav1.7.Our results provide further evidence that NaSpTx Family I toxins share similar structures and mechanisms of binding to Nav1.7.

关键词： Spider Nav1.7 peptide toxin ICK motif

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The cDNA and Genomic DNA Organization of a Novel toxin SHT-I from Spider Ornithoctonus huwena

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Acta Biochimica et Biophysica Sinica 2004年第10期36卷 656-660页

作者： Peng QIAO, Xiao-Pan ZUO, Zhi-Fang CHAI, and Yong-Hua JI* Institute of Physiology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Graduate School of the Chinese Academy of Sciences, Shanghai 200031, China Institute of Physiology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences Graduate School of the Chinese Academy of SciencesShanghai 200031 China

In present study the full-length cDNA of a novel toxin from the venom gland of spider Ornithoctonus huwena, named as SHT-I, has been cloned using the strategy of rapid amplification of cDNA ends, and then the whole genomic sequence of SHT-I (Selenocosmia huwena toxin-I) was determined using sequence-specific primers synthesized based on the acquired 3’ and 5’ ends of SHT-I cDNA sequence. It is unexpectedly found that intron was lacking in the genomic sequence of SHT-I. The result might evoke an interesting question whether the gene code of inhibitor cystine-knot peptides from spider venom is distinct from that of those known toxic peptides of scorpion and cone snail.

关键词： Ornithoctonus huwena spider cDNA genomic DNA peptide toxin ICK motif

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