Genomic organization and cloning of novel genes encoding toxin-like peptides of three superfamilies from the spider Orinithoctonus huwena

Jiang, Liping; Chen, Jinjun; Li, Peng; Zhang, Yongqun; Xiong, Xingjiang; Liang, Songping

doi:10.1016/j.peptides.2008.06.001

Cited by 15 publications

(27 citation statements)

References 29 publications

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“…1A). More recently, 24 genes encoding ICK-containing venom peptides were sequenced from two mygalomorph spiders, namely the Chinese bird spider Haplopelma huwenum and the Chinese Black Earth Tiger tarantula Haplopelma hainanum [16]–[18]. All of these genes lacked introns, in striking contrast to the gene encoding μ-diguetoxin-Dc1a.…”

Section: Discussionmentioning

confidence: 99%

“…Intron-exon organization for genes encoding (A) μ-diguetoxin-Dc1a from the American desert spider Diguetia canities [15]; (B) 24 different disulfide-rich venom peptides from the Chinese tarantulas Haplopelma hainanum and Haplopelma huwenum [16]–[18]. In panel (A), the colors denote exons encoding the signal peptide, propeptide, and mature toxin.…”

Section: Introductionmentioning

confidence: 99%

“…However, recent work on the mygalomorph spiders H. huwenum and H. hainanum has shown that, in contrast with cone snails, the genetic architecture of genes encoding venom peptides in spiders is much more variable since all of the toxin genes sequenced from these spiders are intronless (Fig. 1B) [16]–[18].…”

Section: Introductionmentioning

confidence: 99%

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The Lethal Toxin from Australian Funnel-Web Spiders Is Encoded by an Intronless Gene

et al. 2012

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Australian funnel-web spiders are generally considered the most dangerous spiders in the world, with envenomations from the Sydney funnel-web spider Atrax robustus resulting in at least 14 human fatalities prior to the introduction of an effective anti-venom in 1980. The clinical envenomation syndrome resulting from bites by Australian funnel-web spiders is due to a single 42-residue peptide known as δ-hexatoxin. This peptide delays the inactivation of voltage-gated sodium channels, which results in spontaneous repetitive firing and prolongation of action potentials, thereby causing massive neurotransmitter release from both somatic and autonomic nerve endings. Here we show that δ-hexatoxin from the Australian funnel-web spider Hadronyche versuta is produced from an intronless gene that encodes a prepropeptide that is post-translationally processed to yield the mature toxin. A limited sampling of genes encoding unrelated venom peptides from this spider indicated that they are all intronless. Thus, in distinct contrast to cone snails and scorpions, whose toxin genes contain introns, spiders may have developed a quite different genetic strategy for evolving their venom peptidome.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Lethal Toxin from Australian Funnel-Web Spiders Is Encoded by an Intronless Gene

et al. 2012

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“…This inevitably resulted in a considerable escalation in the number of expressed sequence tags (ESTs) being sequenced, which significantly increased the rate at which new toxin superfamilies were discovered. This approach also led to the first overview of the entire toxin repertoire of several species of spiders including Agelena orientalis [33], Chilobrachys jingzhao [34], Haplopelma hainanum [35], Haplopema huwenum [36], Loxosceles intermedia [37], Loxosceles laeta [38], Lycosa singoriensis [39] and Pelinobius muticus (formerly Citharischius crawshayi) [40].…”

Section: Venommentioning

confidence: 99%

“…There is scant evidence that this venom is selective for tumor cells, although it was recently demonstrated that it suppresses the growth of the myelogenous leukemia cell line K562 (ED 50 5.1 μg/ml) with about sevenfold greater potency than its effect on human lymphocytes (ED 50 36.9 μg/ ml) [138]. Nevertheless, M. raveni venom was found to have anticancer properties in vivo.…”

Section: Antitumorigenic Spider Venomsmentioning

confidence: 99%

Spider Venomics: Implications for Drug Discovery

et al. 2014

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Over a period of more than 300 million years, spiders have evolved complex venoms containing an extraordinary array of toxins for prey capture and defense against predators. The major components of most spider venoms are small disulfide-bridged peptides that are highly stable and resistant to proteolytic degradation. Moreover, many of these peptides have high specificity and potency toward molecular targets of therapeutic importance. This unique combination of bioactivity and stability has made spider-venom peptides valuable both as pharmacological tools and as leads for drug development. This review describes recent advances in spider-venom-based drug discovery pipelines. We discuss spider-venom-derived peptides that are currently under investigation for treatment of a diverse range of pathologies including pain, stroke and cancer.

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Spider Transcriptomes from Venom Glands: Molecular Diversity of Ion Channel Toxins and Antimicrobial Peptide Transcripts

et al. 2016

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Genomic organization and cloning of novel genes encoding toxin-like peptides of three superfamilies from the spider Orinithoctonus huwena

Cited by 15 publications

References 29 publications

The Lethal Toxin from Australian Funnel-Web Spiders Is Encoded by an Intronless Gene

The Lethal Toxin from Australian Funnel-Web Spiders Is Encoded by an Intronless Gene

Spider Venomics: Implications for Drug Discovery

Spider Transcriptomes from Venom Glands: Molecular Diversity of Ion Channel Toxins and Antimicrobial Peptide Transcripts

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