Variability of Potassium Channel Blockers in Mesobuthus eupeus Scorpion Venom with Focus on Kv1.1

Kuzmenkov, Alexey I.; Vassilevski, Alexander A.; Kudryashova, Kseniya S.; Nekrasova, Oksana V.; Peigneur, Steve; Tytgat, Jan; Feofanov, Аlexey V.; Kirpichnikov, Mikhaǐl P.; Grishin, Eugene V.

doi:10.1074/jbc.m115.637611

Cited by 44 publications

(44 citation statements)

References 67 publications

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“…Most of the similar toxins were identified from the same scorpion speciies, M. martensii . However, BmTX4-1 exhibits 92% similarity to BmTX4 from M. eupeus , and four other potassium channel toxins (BmKTx30-1, BmKTx18-3, BmKTx9-1 and BmKTx3-1) are also proved to show amino acid sequence similarities to toxins from M. eupeus [27], suggesting that the two scorpions had a closer relative relationship. The novel toxins found increase the diversity of the scorpion toxins from M. martensii .…”

Section: Discussionmentioning

confidence: 99%

A Combinational Strategy upon RNA Sequencing and Peptidomics Unravels a Set of Novel Toxin Peptides in Scorpion Mesobuthus martensii

Luan

Wang

Liu

et al. 2016

Toxins

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Scorpion venom is deemed to contain many toxic peptides as an important source of natural compounds. Out of the two hundred proteins identified in Mesobuthus martensii (M. martensii), only a few peptide toxins have been found so far. Herein, a combinational approach based upon RNA sequencing and Liquid chromatography-mass spectrometry/mass spectrometry (LC MS/MS) was employed to explore the venom peptides in M. martensii. A total of 153 proteins were identified from the scorpion venom, 26 previously known and 127 newly identified. Of the novel toxins, 97 proteins exhibited sequence similarities to known toxins, and 30 were never reported. Combining peptidomic and transcriptomic analyses, the peptide sequence of BmKKx1 was reannotated and four disulfide bridges were confirmed within it. In light of the comparison of conservation and variety of toxin amino acid sequences, highly conserved and variable regions were perceived in 24 toxins that were parts of two sodium channel and two potassium channel toxins families. Taking all of this evidences together, the peptidomic analysis on M. martensii indeed identified numerous novel scorpion peptides, expanded our knowledge towards the venom diversity, and afforded a set of pharmaceutical candidates.

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Section: Discussionmentioning

confidence: 99%

A Combinational Strategy upon RNA Sequencing and Peptidomics Unravels a Set of Novel Toxin Peptides in Scorpion Mesobuthus martensii

Luan

Wang

Liu

et al. 2016

Toxins

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“…After reaching a threshold concentration, cyclotides form multimeric structures, leading to pores, which could cause membrane damage and changes in ion fluxes [33,48]. In this regard, several cystine-knot toxins produced by spiders, scorpions and sea anemone act as selective blockers of K, Na and acid-sensing channels [49][50][51][52][53].…”

Section: Biological Activities and Molecular Targets Of Cystine-knot mentioning

confidence: 99%

Plant cystine‐knot peptides: pharmacological perspectives

Molesini

Treggiari

Dalbeni

et al. 2016

Brit J Clinical Pharma

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Cystine-knot miniproteins are a class of 30-50 amino acid long peptides widespread in eukaryotic organisms. Due to their very peculiar three-dimensional structure, they exhibit high resistance to heat and peptidase attack. The cystine-knot peptides are well represented in several plant species including medicinal herbs and crops. The pharmacological interest in plant cystine-knot peptides derives from their broad biological activities, mainly cytotoxic, antimicrobial and peptidase inhibitory and in the possibility to engineer them to incorporate pharmacophoric information for oral delivery or disease biomonitoring. The mechanisms of action of plant cystine-knot peptides are still largely unknown, although the capacity to interfere with plasma membranes seems a feature common to several cystine-knot peptides. In some cases, such as potato carboxypetidase inhibitor (PCI) and tomato cystine-knot miniproteins (TCMPs), the cystine-knot peptides target human growth factor receptors either by acting as growth factor antagonist or by altering their signal transduction pathway. The possibility to identify specific molecular targets of plant cystine-knot peptides in human cells opens novel possibilities for the pharmacological use of these peptides besides their use as scaffold to develop stable disease molecular markers and therapeutic agents.

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“…The ␣-KTx family is the largest scorpion neurotoxin family and is divided into at least 30 subfamilies, defined according to the primary sequence alignments of the toxins [10]. Each member has diverse, specific blocking activities against voltage-gated (K v ) and/or calcium-activated (K Ca ) channels.…”

Section: Introductionmentioning

confidence: 99%

Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel α-KTx subfamily

et al. 2016

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Variability of Potassium Channel Blockers in Mesobuthus eupeus Scorpion Venom with Focus on Kv1.1

Cited by 44 publications

References 67 publications

A Combinational Strategy upon RNA Sequencing and Peptidomics Unravels a Set of Novel Toxin Peptides in Scorpion Mesobuthus martensii

A Combinational Strategy upon RNA Sequencing and Peptidomics Unravels a Set of Novel Toxin Peptides in Scorpion Mesobuthus martensii

Plant cystine‐knot peptides: pharmacological perspectives

Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel α-KTx subfamily

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