Venomic analyses of Scolopendra viridicornis nigra and Scolopendra angulata (Centipede, Scolopendromorpha): Shedding light on venoms from a neglected group

Rates, Breno; Bemquerer, Marcelo P.; Richardson, Michael; Borges, Márcia Helena; Morales, Rodrigo; Lima, Maria Elena de; Pimenta, Adriano M.C.

doi:10.1016/j.toxicon.2006.12.001

Cited by 61 publications

(62 citation statements)

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“…The venom peptides, which are of most interest from a drug discovery perspective, are extraordinarily diverse [25,[27][28][29][30][31][32]. Undheim et al [30] classified centipede venom peptides into 31 phylogenetically distinct families of scutigerotoxins (SCUTX1-3) and scoloptoxins ( .…”

Section: Centipede Venoms Are Complex Chemical Arsenalsmentioning

confidence: 99%

“…Remarkably, despite this taxonomic bias, the small number of studies undertaken to date have revealed that centipede venoms contain a remarkable diversity of disulfide-rich peptides that encompass a greater variety of constrained peptide scaffolds than present in any other venom [27][28][29][30].…”

Section: Expert Opinionmentioning

confidence: 99%

“…What was unanticipated, but perhaps should not have been given their unique venom apparatus and long evolutionary history, is that the composition of centipede venoms is vastly different to that of all other venomous animals. Only seven studies to date have probed the centipede venom proteome in detail [25,[27][28][29][30][31][32]], yet these limited investigations have uncovered 19 novel disulfide-constrained peptide families. Given the very limited taxonomic sampling of centipede venoms to date, this is likely to be the tip of the iceberg and the next decade promises to reveal more novel centipede venom peptides as additional species are examined.…”

Section: Expert Opinionmentioning

confidence: 99%

“…Detailed investigation of centipede venoms only became a reality this century when advances in proteomics and transcriptomics allowed the study of small venomous animals that secrete tiny amounts of venom [12]; the first detailed proteomic study of centipede venom was published in 2007 [27] and the first combined proteomic/transcriptomic study in 2012 [29]. Investigations of centipede venoms are therefore still largely at the exploratory stage, with very few studies focused on drug discovery.…”

Section: Expert Opinionmentioning

confidence: 99%

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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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Section: Centipede Venoms Are Complex Chemical Arsenalsmentioning

confidence: 99%

Section: Expert Opinionmentioning

confidence: 99%

Section: Expert Opinionmentioning

confidence: 99%

Section: Expert Opinionmentioning

confidence: 99%

See 2 more Smart Citations

Centipede venoms as a source of drug leads

Undheim

Jenner

King

2016

Expert Opinion on Drug Discovery

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“…Thus, knowledge on centipede venom is limited, because centipedes are regarded as a neglected group of venomous animals due to their limited venom quantity [10]. Nevertheless, centipede venom is a complex mixture and may be a potential source of bioactive molecules.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and sequence analysis of serine protease cDNA from the venom of the centipede Scolopendra subspinipes dehaani

Meunchan¹,

Thammasirirak²,

Daduang³

et al. 2015

Turk J Bioch

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Molecular cloning and sequence analysis of serine protease cDNA from the venom of the centipede Scolopendra subspinipes dehaani [Scolopendra subspinipes dehaani kırkayak zehrinden elde edilen serin proteaz cDNA'sının moleküler klonlaması ve dizi analizi] ABSTRACT Objective: Proteolytic enzymes are one of the well-known components of animal venom. The aim of this study was to identify protease from the venom gland of Scolopendra subspinipes dehaani. Methods: After total RNA extraction, a cDNA encoding a serine protease was identified by RT-PCR and was subsequently sequenced. The sequence was analysed by multiple alignment and homology modelling. Results: A cDNA encoding the precursor of a centipede venom serine protease was identified. The full-length cDNA was 1,014 nucleotides with 780 nucleotides of open reading frame. The precursor nucleotide sequence encoded a signal peptide of 19 residues and a mature protein of 260 residues. It belonged to clan PA of serine proteases in the MEROPS database classification. Catalytic residues were identified by multiple alignments, including an unusual hydrogen bond network in the catalytic site. Secondary structure prediction and homology modelling revealed a chymotrypsin-like fold, which is characteristic of PA clan proteases. Conclusion:The sequence of the identified serine protease showed unusual features, making this centipede venom serine protease an interesting candidate to investigate. A better understanding of the molecular mechanism of venom components will be useful for further applications and help to improve envenomation treatment. Key Words: Scolopendra subspinipes dehaani, cDNA, serine protease Conflict of Interest: The authors have no conflict of interest. ÖZETAmaç: Proteolitik enzimler hayvan zehirlerinin en çok bilinen bileşenlerinden biridir. Bu ça-lışmanın amacı Scolopendra subspinipes dehaani zehir salgı bezinden proteaz enziminin tanımlanmasıdır. Metod: Toplam RNA eldesinin ardından, RT-PCR tekniği kullanılarak serin proteaz proteinini kodlayan gene ait cDNA tanımlanmış ve dizi analizine tabi tutulmuştur. Elde edilen dizi çoklu dizi hizalama ve homoloji modelleme ile analiz edilmiştir. Bulgular: Kırkayak zehirinde bulunan serin proteaz öncülünü kodlayan bir cDNA tanımlan-mıştır. cDNA, 780 nükleotit açık okuma çerçevesinde olmak üzere, toplam 1.014 nükleotit uzunluğundadır. Öncül nükleotit dizisi 19 amino asitlik bir sinyal peptidini ve 260 amino asitlik olgun proteini kodlamaktadır. Bu protein MEROPS veritabanı sınıflandırmasına göre serin proteazlardan PA grubuna aittir. Çoklu dizi hizalama kullanılarak alışılmadık bir hidrojen bağı örgüsüne sahip katalitik bölge ve bu bölgedeki katalitik aminoasitler tanımlanmıştır. İkincil yapı tahmin ve homoloji modelleme çalışmaları PA grup proteazlara özgün olan kimotiripsin benzeri katlanmayı göstermiştir. Sonuç: Tanımlanan serin proteaz dizisi alışılmadık özellikler göstermesi sebebiyle kırkayak zehrindeki serin proteaz enzimini ileri çalışmalar için aday yapmıştır. Venom bileşenlerinin moleküler mekanizmalarının...

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Centipedes (Subclass: Chilopoda)

Barceloux

2008

Medical Toxicology of Natural Substances

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Venomic analyses of Scolopendra viridicornis nigra and Scolopendra angulata (Centipede, Scolopendromorpha): Shedding light on venoms from a neglected group

Cited by 61 publications

References 35 publications

Centipede venoms as a source of drug leads

Centipede venoms as a source of drug leads

Molecular cloning and sequence analysis of serine protease cDNA from the venom of the centipede Scolopendra subspinipes dehaani

Centipedes (Subclass: Chilopoda)

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