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Jie Zhao - One of the best experts on this subject based on the ideXlab platform.
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Scorpion Venom heat resistant peptide is neuroprotective against cerebral ischemia reperfusion injury in association with the nmda mapk pathway
Neuroscience Bulletin, 2020Co-Authors: Xugang Wang, Yan Peng, Dandan Zhu, Yuelin Huang, Yingzi Wang, Ting Zhang, Chenmei Wang, Bin Wang, Jie ZhaoAbstract:Scorpion Venom heat-resistant peptide (SVHRP) is a component purified from Buthus martensii Karsch Scorpion Venom. Our previous studies have shown that SVHRP is neuroprotective in models of Alzheimer’s disease and Parkinson’s disease. The present study aimed to explore the potential neuroprotective effects of SVHRP on cerebral ischemia/reperfusion (I/R) injury, using a mouse model of middle cerebral artery occlusion/reperfusion (MCAO/R) and a cellular model of oxygen-glucose deprivation/reoxygenation (OGD/R). Our results showed that SVHRP treatment decreased the neurological deficit scores, edema formation, infarct volume and neuronal loss in the MCAO/R mice, and protected primary neurons against OGD/R insult. SVHRP pretreatment suppressed the alterations in protein levels of N-methyl-D-aspartate receptors (NMDARs) and phosphorylated p38 MAPK as well as some proinflammatory factors in both the animal and cellular models. These results suggest that SVHRP has neuroprotective effects against cerebral I/R injury, which might be associated with inhibition of the NMDA-MAPK-mediated excitotoxicity.
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Scorpion Venom heat resistant peptide protects transgenic caenorhabditis elegans from β amyloid toxicity
Frontiers in Pharmacology, 2016Co-Authors: Xiaogang Zhang, Wanqin Zhang, Xi Wang, Tingting Zhou, Yan Peng, Jie ZhaoAbstract:Scorpion Venom heat-resistant peptide (SVHRP) is a component purified from Buthus martensii Karsch Scorpion Venom. Our previous studies found SVHRP could enhance neurogenesis and inhibit microglia-mediated neuroinflammation in vivo. Here, we use the transgenic CL4176, CL2006 and CL2355 strains of Caenorhabditis elegans which express the human Aβ1–42 to investigate the effects and the possible mechanisms of SVHRP mediated protection against Aβ toxicity in vivo. The results showed that SVHRP-fed worms displayed remarkably decreased paralysis, less abundant toxic Aβ oligomers, reduced Aβ plaque deposition with respect to untreated animals. SVHRP also suppressed neuronal Aβ expression-induced defects in chemotaxis behavior and attenuated levels of ROS in the transgenic C. elegans. Taken together, these results suggest SVHRP could protect against Aβ-induced toxicity in C. elegans. Further studies need to be conducted in murine models and humans to analyze the effectiveness of the peptide.
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Scorpion Venom heat resistant peptide attenuates glial fibrillary acidic protein expression via c jun ap 1
Cellular and Molecular Neurobiology, 2015Co-Authors: Zhen Cao, Wanqin Zhang, Yan Peng, Rui Zhang, Jinyi Yang, Shuqin Zhang, Jie ZhaoAbstract:Scorpion Venom has been used in the Orient to treat central nervous system diseases for many years, and the protein/peptide toxins in Buthus martensii Karsch (BmK) Venom are believed to be the effective components. Scorpion Venom heat-resistant peptide (SVHRP) is an active component of the Scorpion Venom extracted from BmK. In a previous study, we found that SVHRP could inhibit the formation of a glial scar, which is characterized by enhanced glial fibrillary acidic protein (GFAP) expression, in the epileptic hippocampus. However, the cellular and molecular mechanisms underlying this process remain to be clarified. The results of the present study indicate that endogenous GFAP expression in primary rat astrocytes was attenuated by SVHRP. We further demonstrate that the suppression of GFAP was primarily mediated by inhibiting both c-Jun expression and its binding with AP-1 DNA binding site and other factors at the GFAP promoter. These results support that SVHRP contributes to reducing GFAP at least in part by decreasing the activity of the transcription factor AP-1. In conclusion, the effects of SVHRP on astrocytes with respect to the c-Jun/AP-1 signaling pathway in vitro provide a practical basis for studying astrocyte activation and inhibition and a scientific basis for further studies of traditional medicine.
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the alterations of apoptosis factor bcl 2 bax in the early parkinson s disease rats and the protective effect of Scorpion Venom derived activity peptide
Chinese journal of applied physiology, 2015Co-Authors: Shengming Yin, Wei Chen, Dan Zhao, Xu Meng, Yiping Sun, Jie Zhao, Wanqin ZhangAbstract:OBJECTIVE: To explore the alterations of apoptosis factor Bcl-2/Bax in the early Parkinson's disease (PD) rats and the protective effect of Scorpion Venom derived bioactive peptide. METHODS: Healthy male SD rats (180-220 g) were randomly divided into 4 groups (n = 10): early PD model group, sham operation group, Scorpion Venom derived bioactive peptide control group, Scorpion Venom derived bioactive peptide therapy group. 6-hydroxydopamine (6-OHDA) was used to prepare the early PD rat model. The immunohistochemistry was used to detect the expression of Bax and Bcl-2 and further explore the mechanism of anti-apoptosis regarding the neuroprotective effect of Scorpion Venom derived bioactive peptide. RESULTS: The results indicated that compared with the control rats, the immunostaining of Bax in the brain increased significantly while that of Bcl-2 decreased significantly in the lesion side of 6-OHDA treated rats. Interestingly, Scorpion Venom derived bioactive peptide could attenuate the above abnormal changes. CONCLUSION: Up-regulation of Bax and down-regulation of Bcl-2 could participate in the early stage of PD and the anti-apoptotic mechanism could be involved in the neuroprotective effect exerted by Scorpion Venom derived activity peptide regarding the dopaminergic neuron in the early stage.
Eliane Candiani Arantes - One of the best experts on this subject based on the ideXlab platform.
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Scorpion Venom Research Around the World: Tityus serrulatus
Scorpion Venoms, 2021Co-Authors: Karla De Castro Figueiredo Bordon, Camila Takeno Cologna, Eliane Candiani ArantesAbstract:Tityus serrulatus is considered the most dangerous Scorpion in Brazil. It is widely distributed, especially in the Southeast region, and is responsible for the highest number and most severe accidents. This chapter focuses on Tityus serrulatus Scorpion Venom (Tsv) and aspires to unravel its complex composition with emphases on its isolated proteins, their targets, structures, and functions. It takes a closer look at the peptides related to the Na+ and K+ channel toxin families, NaTx and KTx, respectively, including their toxin precursors. Additionally, a hyaluronidase, a serine proteinase, metalloproteinases, and many other proteins/peptides, such as a nontoxic protein (Ts4), PAPE peptides, bradykinin-potentiating peptides (BPP), antimicrobial peptides (AMP), anionic peptides, and Venom peptides with undetermined functions, were reported.
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Scorpion Venom: Detriments and Benefits
Biomedicines, 2020Co-Authors: Shirin Ahmadi, Eliane Candiani Arantes, Julius M Knerr, Lídia M. Argemí, Karla De Castro Figueiredo Bordon, Manuela Berto Pucca, Felipe A. Cerni, Figen Caliskan, Andreas Hougaard LaustsenAbstract:Scorpion Venom may cause severe medical complications and untimely death if injected into the human body. Neurotoxins are the main components of Scorpion Venom that are known to be responsible for the pathological manifestations of enVenoming. Besides neurotoxins, a wide range of other bioactive molecules can be found in Scorpion Venoms. Advances in separation, characterization, and biotechnological approaches have enabled not only the development of more effective treatments against Scorpion enVenomings, but have also led to the discovery of several Scorpion Venom peptides with interesting therapeutic properties. Thus, Scorpion Venom may not only be a medical threat to human health, but could prove to be a valuable source of bioactive molecules that may serve as leads for the development of new therapies against current and emerging diseases. This review presents both the detrimental and beneficial properties of Scorpion Venom toxins and discusses the newest advances within the development of novel therapies against Scorpion enVenoming and the therapeutic perspectives for Scorpion toxins in drug discovery.
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Microbial production of toxins from the Scorpion Venom: properties and applications
Applied Microbiology and Biotechnology, 2018Co-Authors: Fernanda Gobbi Amorim, Francielle Almeida Cordeiro, Ernesto Lopes Pinheiro-júnior, Johara Boldrini-frança, Eliane Candiani ArantesAbstract:Scorpion Venom are composed mainly of bioactive proteins and peptides that may serve as lead compounds for the design of biotechnological tools and therapeutic drugs. However, exploring the therapeutic potential of Scorpion Venom components is mainly impaired by the low yield of purified toxins from milked Venom. Therefore, production of toxin-derived peptides and proteins by heterologous expression is the strategy of choice for research groups and pharmaceutical industry to overcome this limitation. Recombinant expression in microorganisms is often the first choice, since bacteria and yeast systems combine high level of recombinant protein expression, fast cell growth and multiplication and simple media requirement. Herein, we present a comprehensive revision, which describes the Scorpion Venom components that were produced in their recombinant forms using microbial systems. In addition, we highlight the pros and cons of performing the heterologous expression of these compounds, regarding the particularities of each microorganism and how these processes can affect the application of these Venom components. The most used microbial system in the heterologous expression of Scorpion Venom components is Escherichia coli (85%), and among all the recombinant Venom components produced, 69% were neurotoxins. This review may light up future researchers in the choice of the best expression system to produce Scorpion Venom components of interest.
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tityus serrulatus Scorpion Venom and toxins an overview
Protein and Peptide Letters, 2009Co-Authors: Camila Takeno Cologna, Silvana Marcussi, Jose R Giglio, Andreimar M Soares, Eliane Candiani ArantesAbstract:Tityus serrulatus is considered the most dangerous Scorpion in South America and responsible for most of the fatal cases. This review will focus on Tityus serrulatus Scorpion Venom (Tsv), its long-chain Na(+)-channel toxins (NaTx), which include alpha- and beta-neurotoxins, short-chain K(+)-channel toxins (KTx), hyaluronidase, proteases and other peptides hitherto identified.
Zhijian Cao - One of the best experts on this subject based on the ideXlab platform.
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Extreme diversity of Scorpion Venom peptides and proteins revealed by transcriptomic analysis: Implication for proteome evolution of Scorpion Venom arsenal
Journal of Proteomics, 2012Co-Authors: Ruiming Zhao, Zhijian CaoAbstract:Venom is an important genetic development crucial to the survival of Scorpions for over 400 million years. We studied the evolution of the Scorpion Venom arsenal by means of comparative transcriptome analysis of Venom glands and phylogenetic analysis of shared types of Venom peptides and proteins between buthids and euscorpiids. Fifteen types of Venom peptides and proteins were sequenced during the Venom gland transcriptome analyses of two Buthidae species (Lychas mucronatus and Isometrus maculatus) and one Euscorpiidae species (Scorpiops margerisonae). Great diversity has been observed in translated amino acid sequences of these transcripts for Venom peptides and proteins. Seven types of Venom peptides and proteins were shared between buthids and euscorpiids. Molecular phylogenetic analysis revealed that at least five of the seven common types of Venom peptides and proteins were likely recruited into the Scorpion Venom proteome before the lineage split between Buthidae and Euscorpiidae with their corresponding genes undergoing individual or multiple gene duplication events. These are α-KTxs, βKSPNs (β-KTxs and scorpines), anionic peptides, La1-like peptides, and SPSVs (serine proteases from Scorpion Venom). Multiple types of Venom peptides and proteins were demonstrated to be continuously recruited into the Venom proteome during the evolution process of individual Scorpion lineages. Our results provide an insight into the recruitment pattern of the Scorpion Venom arsenal for the first time.
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sdpi the first functionally characterized kunitz type trypsin inhibitor from Scorpion Venom
PLOS ONE, 2011Co-Authors: Ruiming Zhao, Hui Dai, Su Qiu, Zongyun Chen, Zhijian CaoAbstract:Background Kunitz-type Venom peptides have been isolated from a wide variety of Venomous animals. They usually have protease inhibitory activity or potassium channel blocking activity, which by virtue of the effects on predator animals are essential for the survival of Venomous animals. However, no Kunitz-type peptides from Scorpion Venom have been functionally characterized. Principal Findings A new Kunitz-type Venom peptide gene precursor, SdPI, was cloned and characterized from a Venom gland cDNA library of the Scorpion Lychas mucronatus. It codes for a signal peptide of 21 residues and a mature peptide of 59 residues. The mature SdPI peptide possesses a unique cysteine framework reticulated by three disulfide bridges, different from all reported Kunitz-type proteins. The recombinant SdPI peptide was functionally expressed. It showed trypsin inhibitory activity with high potency (Ki = 1.6×10−7 M) and thermostability. Conclusions The results illustrated that SdPI is a potent and stable serine protease inhibitor. Further mutagenesis and molecular dynamics simulation revealed that SdPI possesses a serine protease inhibitory active site similar to other Kunitz-type Venom peptides. To our knowledge, SdPI is the first functionally characterized Kunitz-type trypsin inhibitor derived from Scorpion Venom, and it represents a new class of Kunitz-type Venom peptides.
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Characterization of LmTxLP11 and LmVP1.1 transcripts and genomic organizations: Alternative splicing contributing to the diversity of Scorpion Venom peptides
Toxicon, 2009Co-Authors: Ruiming Zhao, Shaozhong Fan, Hui Liu, Zhijian CaoAbstract:Abstract Scorpion Venoms are rich resources of bioactive peptides with extreme variability. Multiple molecular mechanisms are involved in the diversity of Scorpion Venom peptides. However, alternative splicing, which plays a major role in the generation of proteomic and functional diversity in metazoan organisms, hasn't been reported in genes coding for Scorpion Venom peptides. In the EST analysis of Venom peptide transcripts from Scorpion Lychas mucronatus , we reported an alternative splicing event. Transcripts of LmTxLP11 and LmVP1.1 share identical 5′ region. LmVP1.1 is a novel type of Scorpion Venom peptides constrained by one disulfide bridge, whereas LmTxLP11 is an extended version of LmVP1.1. By transcript alignment with its genomic sequence, it is found that both transcripts are generated from a single gene by alternative poly A site and terminal exon. The gene encoding LmTxLP11 and LmVP1.1 is the first one harboring three introns ever reported from Scorpion Venoms. This work demonstrates for the first time that alternative splicing is involved in regulating the diversity of Scorpion Venom peptides.
Yan Peng - One of the best experts on this subject based on the ideXlab platform.
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Scorpion Venom heat resistant peptide is neuroprotective against cerebral ischemia reperfusion injury in association with the nmda mapk pathway
Neuroscience Bulletin, 2020Co-Authors: Xugang Wang, Yan Peng, Dandan Zhu, Yuelin Huang, Yingzi Wang, Ting Zhang, Chenmei Wang, Bin Wang, Jie ZhaoAbstract:Scorpion Venom heat-resistant peptide (SVHRP) is a component purified from Buthus martensii Karsch Scorpion Venom. Our previous studies have shown that SVHRP is neuroprotective in models of Alzheimer’s disease and Parkinson’s disease. The present study aimed to explore the potential neuroprotective effects of SVHRP on cerebral ischemia/reperfusion (I/R) injury, using a mouse model of middle cerebral artery occlusion/reperfusion (MCAO/R) and a cellular model of oxygen-glucose deprivation/reoxygenation (OGD/R). Our results showed that SVHRP treatment decreased the neurological deficit scores, edema formation, infarct volume and neuronal loss in the MCAO/R mice, and protected primary neurons against OGD/R insult. SVHRP pretreatment suppressed the alterations in protein levels of N-methyl-D-aspartate receptors (NMDARs) and phosphorylated p38 MAPK as well as some proinflammatory factors in both the animal and cellular models. These results suggest that SVHRP has neuroprotective effects against cerebral I/R injury, which might be associated with inhibition of the NMDA-MAPK-mediated excitotoxicity.
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Scorpion Venom heat resistant peptide protects transgenic caenorhabditis elegans from β amyloid toxicity
Frontiers in Pharmacology, 2016Co-Authors: Xiaogang Zhang, Wanqin Zhang, Xi Wang, Tingting Zhou, Yan Peng, Jie ZhaoAbstract:Scorpion Venom heat-resistant peptide (SVHRP) is a component purified from Buthus martensii Karsch Scorpion Venom. Our previous studies found SVHRP could enhance neurogenesis and inhibit microglia-mediated neuroinflammation in vivo. Here, we use the transgenic CL4176, CL2006 and CL2355 strains of Caenorhabditis elegans which express the human Aβ1–42 to investigate the effects and the possible mechanisms of SVHRP mediated protection against Aβ toxicity in vivo. The results showed that SVHRP-fed worms displayed remarkably decreased paralysis, less abundant toxic Aβ oligomers, reduced Aβ plaque deposition with respect to untreated animals. SVHRP also suppressed neuronal Aβ expression-induced defects in chemotaxis behavior and attenuated levels of ROS in the transgenic C. elegans. Taken together, these results suggest SVHRP could protect against Aβ-induced toxicity in C. elegans. Further studies need to be conducted in murine models and humans to analyze the effectiveness of the peptide.
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Scorpion Venom heat resistant peptide attenuates glial fibrillary acidic protein expression via c jun ap 1
Cellular and Molecular Neurobiology, 2015Co-Authors: Zhen Cao, Wanqin Zhang, Yan Peng, Rui Zhang, Jinyi Yang, Shuqin Zhang, Jie ZhaoAbstract:Scorpion Venom has been used in the Orient to treat central nervous system diseases for many years, and the protein/peptide toxins in Buthus martensii Karsch (BmK) Venom are believed to be the effective components. Scorpion Venom heat-resistant peptide (SVHRP) is an active component of the Scorpion Venom extracted from BmK. In a previous study, we found that SVHRP could inhibit the formation of a glial scar, which is characterized by enhanced glial fibrillary acidic protein (GFAP) expression, in the epileptic hippocampus. However, the cellular and molecular mechanisms underlying this process remain to be clarified. The results of the present study indicate that endogenous GFAP expression in primary rat astrocytes was attenuated by SVHRP. We further demonstrate that the suppression of GFAP was primarily mediated by inhibiting both c-Jun expression and its binding with AP-1 DNA binding site and other factors at the GFAP promoter. These results support that SVHRP contributes to reducing GFAP at least in part by decreasing the activity of the transcription factor AP-1. In conclusion, the effects of SVHRP on astrocytes with respect to the c-Jun/AP-1 signaling pathway in vitro provide a practical basis for studying astrocyte activation and inhibition and a scientific basis for further studies of traditional medicine.
Shunyi Zhu - One of the best experts on this subject based on the ideXlab platform.
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Meucin-49, a multifunctional Scorpion Venom peptide with bactericidal synergy with neurotoxins
Amino Acids, 2018Co-Authors: Bin Gao, Julie E. Dalziel, Simone Tanzi, Shunyi ZhuAbstract:Besides key roles in prey capture and predator defense, Scorpion Venom also functions as internal immune agents protecting the Venom gland from infection and external immune agents cleaning saprophytic microbes from their own body surfaces. However, antimicrobials (typically antimicrobial peptides, AMPs) in the Venom often exist in low abundance that might exclude their immune role alone, leaving an open question with regard to their in vivo biological function. Here, we report the bactericidal activity of seven peptides isolated from the Scorpion Mesobuthus eupeus Venom, including one classical α-helical AMP and five ion channel-targeted neurotoxins. This AMP of 49 amino acids (named Meucin-49) is a multifunctional molecule that displays a wide-spectrum and highly potent activity against Gram-positive and Gram-negative bacteria with strong hemotoxicity on Scorpion’s predators (i.e., mammals, lizards, and birds) and high insecticidal activity. Although the neurotoxins targeting voltage-gated sodium (Nav) and/or large conductance calcium-activated potassium (BK) channels showed only marginal activity towards several species of bacteria, they were capable of significantly potentiating the bactericidal potency of Meucin-49. This observation highlights, for the first time, the Venom’s antibacterial immune function mediated by a joint action between neurotoxins and AMPs. The findings that traditionally defined neurotoxins possess (synergistic) bactericidal activity, while the classical AMPs play predatory and defensive roles, provide new evidence in favor of a general and intrinsic multifunctionality of Scorpion Venom components.
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Exon Shuffling and Origin of Scorpion Venom Biodiversity.
Toxins, 2016Co-Authors: Xueli Wang, Bin Gao, Shunyi ZhuAbstract:Scorpion Venom is a complex combinatorial library of peptides and proteins with multiple biological functions. A combination of transcriptomic and proteomic techniques has revealed its enormous molecular diversity, as identified by the presence of a large number of ion channel-targeted neurotoxins with different folds, membrane-active antimicrobial peptides, proteases, and protease inhibitors. Although the biodiversity of Scorpion Venom has long been known, how it arises remains unsolved. In this work, we analyzed the exon-intron structures of an array of Scorpion Venom protein-encoding genes and unexpectedly found that nearly all of these genes possess a phase-1 intron (one intron located between the first and second nucleotides of a codon) near the cleavage site of a signal sequence despite their mature peptides remarkably differ. This observation matches a theory of exon shuffling in the origin of new genes and suggests that recruitment of different folds into Scorpion Venom might be achieved via shuffling between body protein-coding genes and ancestral Venom gland-specific genes that presumably contributed tissue-specific regulatory elements and secretory signal sequences.
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Functional evolution of Scorpion Venom peptides with an inhibitor cystine knot fold
2016Co-Authors: Bin Gao, Michel Ronjat, Michel De Waard, Peta J. Harvey, David J. Craik, Shunyi ZhuAbstract:The ICK (inhibitor cystine knot) defines a large superfamily of polypeptides with high structural stability and functional diversity. Here, we describe a new Scorpion Venom-derived K+ channel toxin (named λ-MeuKTx-1) with an ICK fold through gene cloning, chemical synthesis, nuclear magnetic resonance spectroscopy, Ca2 + release measurements and electrophysiological recordings. λ-MeuKTx-1 was found to adopt an ICK fold that contains a three-strand anti-parallel β-sheet and a 310-helix. Functionally, this peptide selectively inhibits the Drosophila Shaker K+ channel but is not capable of activating skeletal-type Ca2 + release channels/ryanodine receptors, which is remarkably different from the previously known Scorpion Venom ICK peptides. The removal of two C-terminal residues of λ-MeuKTx-1 led to the loss of the inhibitory activity on the channel, whereas the C-terminal amidation resulted in the emergence of activity on four mammalian K+ channels accompanied by the loss of activity on the Shaker channel. A combination of structural and pharmacological data allows the recognition of three putative functional sites involved in channel blockade of λ-MeuKTx-1. The presence of a functional dyad in λ-MeuKTx-1 supports functional convergence among Scorpion Venom peptides with different folds. Furthermore, similarities in precursor organization, exon–intron structure, 3D-fold and function suggest that Scorpion Venom ICK-type K+ channel inhibitors and Ca2 + release channel activators share a common ancestor and their divergence occurs after speciation between buthidae and non-buthids. The structural an
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Functional evolution of Scorpion Venom peptides with an inhibitor cystine knot fold.
Bioscience Reports, 2013Co-Authors: Bin Gao, Peta Harvey, David Craik, Michel Ronjat, Michel De Waard, Shunyi ZhuAbstract:The ICK (inhibitor cystine knot) defines a large superfamily of polypeptides with high structural stability and functional diversity. Here, we describe a new Scorpion Venom-derived K+ channel toxin (named λ-MeuKTx-1) with an ICK fold through gene cloning, chemical synthesis, nuclear magnetic resonance spectroscopy, Ca2+ release measurements and electrophysiological recordings. λ-MeuKTx-1 was found to adopt an ICK fold that contains a three-strand anti-parallel β-sheet and a 310-helix. Functionally, this peptide selectively inhibits the Drosophila Shaker K+ channel but is not capable of activating skeletal-type Ca2+ release channels/ryanodine receptors, which is remarkably different from the previously known Scorpion Venom ICK peptides. The removal of two C-terminal residues of λ-MeuKTx-1 led to the loss of the inhibitory activity on the channel, whereas the C-terminal amidation resulted in the emergence of activity on four mammalian K+ channels accompanied by the loss of activity on the Shaker channel. A combination of structural and pharmacological data allows the recognition of three putative functional sites involved in channel blockade of λ-MeuKTx-1. The presence of a functional dyad in λ-MeuKTx-1 supports functional convergence among Scorpion Venom peptides with different folds. Furthermore, similarities in precursor organization, exon-intron structure, 3D-fold and function suggest that Scorpion Venom ICK-type K+ channel inhibitors and Ca2+ release channel activators share a common ancestor and their divergence occurs after speciation between buthidae and non-buthids. The structural and functional characterizations of the first Scorpion Venom ICK toxin with K+ channel-blocking activity sheds light on functionally divergent and convergent evolution of this conserved scaffold of ancient origin.
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Inducible antibacterial response of Scorpion Venom gland.
Peptides, 2007Co-Authors: Bin Gao, Caihuan Tian, Shunyi ZhuAbstract:Innate immunity is the first line defense of multicellular organisms that rapidly operates to limit aggression upon exposure to pathogen microorganisms. Although the existence of some antibacterial peptides in Scorpion Venoms suggests that Venom gland could be protected by these effector molecules, antibacterial activity of Venom itself has not been assessed. In this study, we reported the antibacterial activity of the Venom of Chinese Scorpion Buthus martensii. Protease K digestion test indicated that it is Venom peptide/ protein components, as key players, which are involved in such antibacterial response. As the first step toward studying molecular mechanism of Scorpion Venom gland immunity, we established an infection model which supports inducible antibacterial response of Scorpion Venom gland. A known B. martensii antibacterial peptide gene BmKb1 was up-regulated at the transcriptional level after Venom gland was challenged, suggesting its key defense role. This is further strengthened by the presence of several immune response elements in the BmKb1 promoter region. Our work thus provides the first evidence supporting the role of Venom antibacterial peptides (ABPs) in controlling Scorpion Venom gland infection and lays a basis for characterizing related components involved in regulation of Scorpion Venom gland ABP gene expression.