Two novel antimicrobial peptides from centipede venoms

Peng, Kanfu; Kong, Yi; Zhai, Lei; Wu, Xing-Zheng; Jia, Peng; Liu, Jingze; Yu, Haining

doi:10.1016/j.toxicon.2009.07.040

Cited by 67 publications

(44 citation statements)

References 21 publications

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“…Venom was collected manually by stimulating the venom glands in the first pair forceps of centipedes using a 3 V alternating current as in our previous report (22). The venoms were stored at Ϫ20°C until further use.…”

Section: Methodsmentioning

confidence: 99%

Chemical Punch Packed in Venoms Makes Centipedes Excellent Predators

Yang

Xiao

et al. 2012

Molecular & Cellular Proteomics

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Centipedes are excellent predatory arthropods that inject venom to kill or immobilize their prey. Although centipedes have long been known to be venomous, their venoms remain largely unexplored. The chemical components responsible for centipede predation and the functional mechanisms are unknown. Twenty-six neurotoxin-like peptides belonging to ten groups were identified from the centipede venoms, Scolopendra subspinipes mutilans L. Koch by peptidomics combined with transcriptome analysis, revealing the diversity of neurotoxins. These neurotoxins each contain two to four intramolecular disulfide bridges, and in most cases the disulfide framework is different from that found in neurotoxins from the venoms of spiders, scorpions, marine cone snails, sea anemones, and snakes (5S animals). Several neurotoxins contain potential insecticidal abilities, and they are found to act on voltage-gated sodium, potassium, and calcium channels, respectively. Although these neurotoxins are functionally similar to the disulfiderich neurotoxins found in the venoms of 5S animals in that they modulate the activity of voltage-gated ion channels, in almost all cases the primary structures of the centipede venom peptides are unique. This represents an interesting case of convergent evolution in which different venomous animals have evolved different molecular strategies for targeting the same ion channels in prey and predators. Moreover, the high level of biochemical diversity revealed in this study suggests that centipede venoms might be attractive subjects for prospecting and screening for peptide candidates with potential pharmaceutical or agrochemical applications. Molecular & Cellular

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Section: Methodsmentioning

confidence: 99%

Chemical Punch Packed in Venoms Makes Centipedes Excellent Predators

Yang

Xiao

et al. 2012

Molecular & Cellular Proteomics

Self Cite

113

146

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“…These systems work together complementarily when infections occur. To date, many bioactive substances have been characterized in arthropods (Bulet and Stocklin 2005;Bulet et al 2004;Wenhua et al 2006;Peng et al 2010). The big centipede (Scolopendra subspinipes mutilans) has been used in oriental medicine over centuries to treat various diseases, such as lumbar pain.…”

Section: Introductionmentioning

confidence: 99%

“…Few AMP molecules from this centipede have been reported, such as scolopendrin I and scolopins 1 and 2, which were characterized from the body and venom of S. subspinipes mutilans, respectively (Peng et al 2010;Wenhua et al 2006).…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial peptides in the centipede Scolopendra subspinipes mutilans

Yoo

Lee

Shin

et al. 2014

Funct Integr Genomics

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The centipede Scolopendra subspinipes mutilans is an environmentally beneficial and medically important arthropod species. Although this species is increasingly applied as a reliable source of new antimicrobial peptides, the transcriptome of this species is a prerequisite for more rational selection of antimicrobial peptides. In this report, we isolated total RNA from the whole body of adult centipedes, S. subspinipes mutilans, that were nonimmunized and immunized against Escherichia coli, and we generated a total of 77,063 pooled contigs and singletons using high-throughput sequencing. To screen putative antimicrobial peptides, in silico analyses of the S. subspinipes mutilans transcriptome were performed based on the physicochemical evidence of length, charge, isoelectric point, and in vitro and in vivo aggregation scores together with the existence of continuous antimicrobial peptide stretches. Moreover, we excluded some transcripts that showed similarity with both previously known antimicrobial peptides and the human proteome, had a proteolytic cleavage site, and had downregulated expression compared with the nonimmunized sample. As a result, we selected 17 transcripts and tested their antimicrobial activity with a radial diffusion assay. Among them, ten synthetic peptides experimentally showed antimicrobial activity against microbes and no toxicity to mouse erythrocytes. Our results provide not only a useful set of antimicrobial peptide candidates and an efficient strategy for novel antimicrobial peptide development but also the transcriptome data of a big centipede as a valuable resource.

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“…Small, non-reticulated peptides with antimicrobial activity have also been isolated from centipede venoms [58,59]. While some of these peptides may be interesting from a drug discovery perspective, similar pharmacological activities have been noted previously for venom peptides from a wide variety of venomous taxa.…”

Section: Novel Pharmacological Activities In Centipede Venom Peptidesmentioning

confidence: 58%

Centipede venoms as a source of drug leads

Undheim

Jenner

King

2016

Expert Opinion on Drug Discovery

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Introduction: Centipedes are one of the oldest and most successful lineages of venomous terrestrial predators. Despite their use for centuries in traditional medicine, centipede venoms remain poorly studied. However, recent work indicates that centipede venoms are highly complex chemical arsenals that are rich in disulfide-constrained peptides that have novel pharmacology and three-dimensional structure. Areas covered:This review summarizes what is currently know about centipede venom proteins, with a focus on disulfide-rich peptides that have novel or unexpected pharmacology that might be useful from a therapeutic perspective. We also highlight the remarkable diversity of constrained threedimensional peptide scaffolds present in these venoms that might be useful for bioengineering of drug leads. Expert opinion:The resurgence of interest in peptide drugs has stimulated interest in venoms as a source of highly stable, disulfide-constrained peptides with potential as therapeutics. Well-studied venomous taxa such as cone snails and snakes have yielded FDA-approved drugs, while ancient invertebrate predators such as spiders and sea anemones have yielded molecules that are currently in preclinical studies and clinical trials, respectively. However, until recently, the paucity of research on centipede venoms made it easy to discount them as a potential source of peptides with therapeutically useful properties. Seminal studies over the past five years have revealed that centipede venoms have exceedingly complex proteomes that are perhaps richer than any other venom in unique disulfide-rich peptide scaffolds. Like most arthropod predators, centipede venoms are rich in peptides that target neuronal ion channels and receptors, but it is also becoming increasingly apparent that many of these peptides have novel or unexpected pharmacological properties with potential applications in drug discovery and development.

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Two novel antimicrobial peptides from centipede venoms

Cited by 67 publications

References 21 publications

Chemical Punch Packed in Venoms Makes Centipedes Excellent Predators

Chemical Punch Packed in Venoms Makes Centipedes Excellent Predators

Antimicrobial peptides in the centipede Scolopendra subspinipes mutilans

Centipede venoms as a source of drug leads

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