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[PMID]:29229330
[Au] Autor:Guan F; You Y; Li X; Robinson MA
[Ad] Endereço:Department of Clinical Studies, School of Veterinary Medicine, University of Pennsylvania, New Bolton Center Campus, 382 West Street Road, Kennett Square, PA, 19348, USA; Pennsylvania Equine Toxicology and Research Laboratory, 220 East Rosedale Avenue, West Chester, PA, 19382, USA. Electronic addres
[Ti] Título:Detection and confirmation of α-cobratoxin in equine plasma by solid-phase extraction and liquid chromatography coupled to mass spectrometry.
[So] Source:J Chromatogr A;1533:38-48, 2018 Jan 19.
[Is] ISSN:1873-3778
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:α-Cobratoxin (CTX) is a large peptide (71 amino acids) with strong analgesic effect and may be misused in sports such as horse racing. To prevent such misuse, a sensitive method is required for detection and confirmation of the toxin in equine samples. CTX was extracted from equine plasma using an optimized mixed-mode solid-phase extraction (SPE) procedure. Extracted CTX was reduced with dithiothreitol and alkylated with iodoacetamide, and then was digested by trypsin at 56°C for 30min. The digest was analysed by liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS), and tryptic peptides T2 ( CFITPDITSK ) and T4 ( TWCDAFCSIR ) were monitored for detection and confirmation of CTX. The limit of detection (LOD) was 0.05ng/mL for CTX in plasma, and the limit of confirmation (LOC) 0.2ng/mL. Unlike small peptides consisting of the 20 canonical amino acids, CTX was stable in equine plasma at ambient temperature for at least 24h. The developed analytical method was successfully applied to analysis of incurred plasma samples; CTX was detected in plasma collected 15min through 36h post subcutaneous administration of CTX (2.0mg dose) to a research horse, and confirmed 30min through 24h. Additionally, an approach named "reliable targeted SEQUEST search" has been proposed for assessing the specificity of T2 at product ion spectrum level for confirmation of CTX. T2 is uniquely specific for CTX, as evaluated with this approach and BLAST search. Furthermore, the effect of dimethyl sulfoxide (DMSO) as a mobile phase additive on electrospray (ESI) response of T2 and T4, background noise level and signal to noise ratio (S/N) was examined; DMSO increased signal intensity of T2 and T4 by a factor of less than 2. It is the first report that DMSO raised background noise level and did not improve S/N for the peptides, to the authors' knowledge. The developed analytical method may be applicable for analysis of CTX in plasma from other species such as greyhound dogs or even human beings.
[Mh] Termos MeSH primário: Análise Química do Sangue/métodos
Cromatografia Líquida
Proteínas Neurotóxicas de Elapídeos/sangue
Doping nos Esportes/prevenção & controle
Extração em Fase Sólida
Espectrometria de Massas em Tandem
[Mh] Termos MeSH secundário: Animais
Análise Química do Sangue/normas
Cavalos
Limite de Detecção
Preparações Farmacêuticas/sangue
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cobra Neurotoxin Proteins); 0 (Pharmaceutical Preparations); 69344-74-7 (alpha-cobratoxin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE


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[PMID]:28496322
[Au] Autor:Yang Q; Zhao C; Zhao J; Ye Y
[Ad] Endereço:Department of Pharmaceutical Engineering, School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou, People's Republic of China.
[Ti] Título:Photoresponsive nanocapsulation of cobra neurotoxin and enhancement of its central analgesic effects under red light.
[So] Source:Int J Nanomedicine;12:3463-3470, 2017.
[Is] ISSN:1178-2013
[Cp] País de publicação:New Zealand
[La] Idioma:eng
[Ab] Resumo:Cobra neurotoxin (CNT), a peptide isolated from snake venom of , shows central analgesic effects in our previous research. In order to help CNT pass through blood-brain barrier (BBB) and improve its central analgesic effects, a new kind of CNT nanocapsules were prepared by double emulsification with soybean lecithin and cholesterol as the shell, and pheophorbide as the photosensitizer added to make it photoresponsive. The analgesic effects were evaluated by hot plate test and acetic acid-induced writhing in mice. The CNT nanocapsules had an average particle size of 229.55 nm, zeta potential of -53.00 mV, encapsulation efficiency of 84.81% and drug loading of 2.98%, when the pheophorbide content was 1% of lecithin weight. Pheophorbide was mainly distributed in outer layer of the CNT nanocapsules and increased the release of the CNT nanocapsules after 650 nm illumination. The central analgesic effects were improved after intraperitoneal injection of CNT at 25 and 50 µg·kg under 650 nm irradiation for 30 min in the nasal cavity. Activation of pheophorbide by red light generated reactive oxygen species which opened the nanocapsules and BBB and helped the CNT enter the brain. This research provides a new drug delivery for treatment of central pain.
[Mh] Termos MeSH primário: Analgésicos/administração & dosagem
Analgésicos/farmacologia
Proteínas Neurotóxicas de Elapídeos/farmacologia
Nanocápsulas/química
[Mh] Termos MeSH secundário: Analgésicos/química
Animais
Barreira Hematoencefálica/efeitos dos fármacos
Encéfalo/efeitos dos fármacos
Clorofila/análogos & derivados
Clorofila/química
Proteínas Neurotóxicas de Elapídeos/administração & dosagem
Proteínas Neurotóxicas de Elapídeos/química
Sistemas de Liberação de Medicamentos/métodos
Avaliação Pré-Clínica de Medicamentos/métodos
Injeções Intraperitoneais
Luz
Camundongos
Nanocápsulas/administração & dosagem
Dor/induzido quimicamente
Tamanho da Partícula
Fármacos Fotossensibilizantes/administração & dosagem
Fármacos Fotossensibilizantes/química
Fármacos Fotossensibilizantes/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Analgesics); 0 (Cobra Neurotoxin Proteins); 0 (Nanocapsules); 0 (Photosensitizing Agents); 1406-65-1 (Chlorophyll); IA2WNI2HO2 (pheophorbide a)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170513
[St] Status:MEDLINE
[do] DOI:10.2147/IJN.S132510


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[PMID]:28209480
[Au] Autor:Anderson GP; Liu JH; Zabetakis D; Liu JL; Goldman ER
[Ad] Endereço:US Naval Research Laboratory, Center for Biomolecular Science and Engineering, 4555 Overlook Ave SW, Washington, DC, 20375, USA. Electronic address: george.anderson@nrl.navy.mil.
[Ti] Título:Thermal stabilization of anti-α-cobratoxin single domain antibodies.
[So] Source:Toxicon;129:68-73, 2017 Apr.
[Is] ISSN:1879-3150
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:There is an unmet need for snake antivenoms that can be stored ready to use near the point of care. To address that need we have taken two anti-α-cobratoxin single domain antibodies and increased their thermal stability to improve their ambient temperature shelf-life. The anti-α-cobratoxin single domain antibodies C2 and C20 were first isolated, and demonstrated to be toxin neutralizing by Richard et al., 2013 (Richard, G., Meyers, A.J., McLean, M.D., Arbabi-Ghahroudi, M., MacKenzie, R., Hall, J.C., 2013. In vivo neutralization of alpha-cobratoxin with high-affinity llama single-domain antibodies (VHHs) and a VHH-Fc antibody. PLoS One 8, e69495). To thermal stabilize C2 and C20, we first made changes to their frame work 1 region that we had previously identified to be stabilizing, as well as reverted to the hallmark amino acids highly conserved in VHH domains; these changes improved their melting temperature (Tm) by 2 and 6 °C respectively. The further addition of a non-canonical disulfide bond raised the Tm an additional 13 and 9 °C respectively; giving final Tm values of 86 and 75 °C. Testing these mutants at 1 mg/mL at a range of elevated temperatures for an hour; we found that at 65 °C the wild type C2 and C20 had lost 35 and 95% of their binding activity respectively, while the mutants with the added disulfide bond retained nearly 100% of their initial binding activity. While significant work remains to formulate and field a shelf-stable antivenom, our results indicate such a product should be attainable in the near future.
[Mh] Termos MeSH primário: Antivenenos/farmacologia
Proteínas Neurotóxicas de Elapídeos/imunologia
Anticorpos de Domínio Único/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Antivenenos/química
Dicroísmo Circular
Elapidae
Estabilidade Proteica
Anticorpos de Domínio Único/química
Ressonância de Plasmônio de Superfície
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antivenins); 0 (Cobra Neurotoxin Proteins); 0 (Single-Domain Antibodies); 69344-74-7 (alpha-cobratoxin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170218
[St] Status:MEDLINE


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[PMID]:27840083
[Au] Autor:Zhu Q; Huang J; Wang SZ; Qin ZH; Lin F
[Ad] Endereço:Department of Pharmacology, Laboratory of Aging and Nervous Diseases (SZS0703), Soochow University School of Pharmaceutical Science, Su Zhou 215123, China.. Electronic address: imzhuqi@163.com.
[Ti] Título:Cobrotoxin extracted from Naja atra venom relieves arthritis symptoms through anti-inflammation and immunosuppression effects in rat arthritis model.
[So] Source:J Ethnopharmacol;194:1087-1095, 2016 Dec 24.
[Is] ISSN:1872-7573
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:ETHNOPHARMACOLOGICAL RELEVANCE: The Naja atra (Chinese cobra), primarily distributing in the low or medium altitude areas of southern China and Taiwan, was considered as a medicine in traditional Chinese medicine and used to treat pain, inflammation and arthritis. AIM OF THE STUDY: To study the anti-inflammatory and anti-arthritic activities of cobrotoxin (CTX), an active component of the venom from Naja atra. MATERIALS AND METHODS: Adjuvant-induced arthritis (AA) rats were used as the animal model of rheumatoid arthritis. The anti-arthritic effects of CTX were evaluated through the arthritis score, paw edema and histopathology changes of joints. The anti-inflammation effects were assayed by the level of IL-6, TNF-α, IL-1ß and the number of inflammatory cells in peripheral blood, as well as the proliferation of fibroblast-like synoviocytes (FLS). The immune level was valued by the proliferation of T cells and the level of CD4 and CD8. RESULTS: CTX alleviated the disease development of AA rats according to the ameliorating arthritis score, paw edema and histopathology character. At the meanwhile, CTX decreased the levels of IL-6, TNF-α, IL-1ß and the numbers of inflammatory cells in peripheral blood. CTX also suppressed the abnormal increasing of CD4+ T cells/ CD8+ T cells ratio, and could significantly inhibit T cell proliferation. Consistent with its effects on inhibiting granuloma's formation, CTX inhibited the proliferation of the cultured FLSs. Further studies on inflammatory signaling in FLSs revealed that CTX could inhibit the NF-κB signaling pathway. CONCLUSIONS: CTX has beneficial effects on rheumatoid arthritis by its immune regulation effects and anti-inflammation effects. The inhibition of NF-κB pathway partly contributes to the anti-inflammatory properties of CTX.
[Mh] Termos MeSH primário: Anti-Inflamatórios/farmacologia
Artrite Reumatoide/tratamento farmacológico
Proteínas Neurotóxicas de Elapídeos/química
Proteínas Neurotóxicas de Elapídeos/farmacologia
Venenos Elapídicos/química
Imunossupressores/farmacologia
[Mh] Termos MeSH secundário: Animais
Artrite Experimental/tratamento farmacológico
Linfócitos T CD4-Positivos/efeitos dos fármacos
Linfócitos T CD4-Positivos/metabolismo
Linfócitos T CD8-Positivos/efeitos dos fármacos
Linfócitos T CD8-Positivos/metabolismo
Proliferação Celular/efeitos dos fármacos
Modelos Animais de Doenças
Edema/tratamento farmacológico
Edema/metabolismo
Fibroblastos/efeitos dos fármacos
Fibroblastos/metabolismo
Imunossupressão/métodos
Interleucina-1beta/metabolismo
Interleucina-6/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos ICR
NF-kappa B/metabolismo
Ratos
Ratos Wistar
Transdução de Sinais/efeitos dos fármacos
Membrana Sinovial/efeitos dos fármacos
Fator de Necrose Tumoral alfa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Cobra Neurotoxin Proteins); 0 (Elapid Venoms); 0 (Immunosuppressive Agents); 0 (Interleukin-1beta); 0 (Interleukin-6); 0 (NF-kappa B); 0 (Tumor Necrosis Factor-alpha)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161115
[St] Status:MEDLINE


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[PMID]:27417718
[Au] Autor:Faure G; Shelukhina IV; Porowinska D; Shulepko MA; Lyukmanova EN; Dolgikh DA; Spirova EN; Kasheverov IE; Utkin YN; Corringer JP; Tsetlin VI
[Ad] Endereço:Pasteur Institute, Paris, France. ner-neri@yandex.ru.
[Ti] Título:Interaction of three-finger proteins from snake venoms and from mammalian brain with the cys-loop receptors and their models.
[So] Source:Dokl Biochem Biophys;468(1):193-6, 2016 May.
[Is] ISSN:1608-3091
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:With the use of surface plasmon resonance (SPR) it was shown that ws-Lynx1, a water-soluble analog of the three-finger membrane-bound protein Lynx1, that modulates the activity of brain nicotinic acetylcholine receptors (nAChRs), interacts with the acetylcholine-binding protein (AChBP) with high affinity, K D = 62 nM. This result agrees with the earlier demonstrated competition of ws-Lynx1 with radioiodinated α-bungarotoxin for binding to AChBP. For the first time it was shown that ws-Lynx1 binds to GLIC, prokaryotic Cys-loop receptor (K D = 1.3 µM). On the contrary, SPR revealed that α-cobratoxin, a three-finger protein from cobra venom, does not bind to GLIC. Obtained results indicate that SPR is a promising method for analysis of topography of ws-Lynx1 binding sites using its mutants and those of AChBP and GLIC.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Encéfalo/metabolismo
Proteínas Neurotóxicas de Elapídeos/metabolismo
Receptores de Canais Iônicos de Abertura Ativada por Ligante com Alça de Cisteína/metabolismo
Glicoproteínas de Membrana/metabolismo
Receptor Nicotínico de Acetilcolina alfa7/metabolismo
[Mh] Termos MeSH secundário: Animais
Aplysia
Proteínas de Bactérias/química
Sítios de Ligação
Linhagem Celular
Linhagem Celular Tumoral
Cianobactérias
Receptores de Canais Iônicos de Abertura Ativada por Ligante com Alça de Cisteína/química
Drosophila melanogaster
Venenos Elapídicos/química
Venenos Elapídicos/metabolismo
Elapidae
Escherichia coli
Células HEK293
Seres Humanos
Glicoproteínas de Membrana/química
Glicoproteínas de Membrana/genética
Modelos Moleculares
Estrutura Secundária de Proteína
Ressonância de Plasmônio de Superfície
Receptor Nicotínico de Acetilcolina alfa7/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cobra Neurotoxin Proteins); 0 (Cysteine Loop Ligand-Gated Ion Channel Receptors); 0 (Elapid Venoms); 0 (Membrane Glycoproteins); 0 (Naja kaouthia venom); 0 (alpha7 Nicotinic Acetylcholine Receptor); 69344-74-7 (alpha-cobratoxin)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160716
[St] Status:MEDLINE
[do] DOI:10.1134/S1607672916030091


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[PMID]:26972756
[Au] Autor:Tan KY; Tan CH; Sim SM; Fung SY; Tan NH
[Ad] Endereço:Department of Molecular Medicine, Faculty of Medicine, University of Malaya, 50603 Kuala Lumpur, Malaysia.
[Ti] Título:Geographical venom variations of the Southeast Asian monocled cobra (Naja kaouthia): venom-induced neuromuscular depression and antivenom neutralization.
[So] Source:Comp Biochem Physiol C Toxicol Pharmacol;185-186:77-86, 2016 Jul-Aug.
[Is] ISSN:1532-0456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Southeast Asian monocled cobras (Naja kaouthia) exhibit geographical variations in their venom proteomes, especially on the composition of neurotoxins. This study compared the neuromuscular depressant activity of the venoms of N. kaouthia from Malaysia (NK-M), Thailand (NK-T) and Vietnam (NK-V), and the neutralization of neurotoxicity by a monospecific antivenom. On chick biventer cervicis nerve-muscle preparation, all venoms abolished the indirect twitches, with NK-T venom being the most potent (shortest t90, time to 90% twitch inhibition), followed by NK-V and NK-M. Acetylcholine and carbachol failed to reverse the blockade, indicating irreversible/pseudo-irreversible post-synaptic neuromuscular blockade. KCl restored the twitches variably (NK-M preparation being the least responsive), consistent with different degree of muscle damage. The findings support that NK-T venom has the most abundant curarimimetic alpha-neurotoxins, while NK-M venom contains more tissue-damaging cytotoxins. Pre-incubation of tissue with N. kaouthia monovalent antivenom (NKMAV) prevented venom-induced twitch depression, with the NK-T preparation needing the largest antivenom dose. NKMAV added after the onset of neuromuscular depression could only halt the inhibitory progression but failed to restore full contraction. The findings highlight the urgency of early antivenom administration to sequester as much circulating neurotoxins as possible, thereby hastening toxin elimination from the circulation. In envenomed mice, NKMAV administered upon the first neurological sign neutralized the neurotoxic effect, with the slowest full recovery noticed in the NK-T group. This is consistent with the high abundance of neurotoxins in the NK-T venom, implying that a larger amount or repeated dosing of NKMAV may be required in NK-T envenomation.
[Mh] Termos MeSH primário: Antivenenos/farmacologia
Proteínas Neurotóxicas de Elapídeos/toxicidade
Venenos Elapídicos/toxicidade
Elapidae/metabolismo
Contração Muscular/efeitos dos fármacos
Junção Neuromuscular/efeitos dos fármacos
Mordeduras de Serpentes/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Galinhas
Agonistas Colinérgicos/farmacologia
Proteínas Neurotóxicas de Elapídeos/metabolismo
Modelos Animais de Doenças
Relação Dose-Resposta a Droga
Venenos Elapídicos/metabolismo
Malásia
Masculino
Camundongos Endogâmicos ICR
Junção Neuromuscular/metabolismo
Junção Neuromuscular/patologia
Junção Neuromuscular/fisiopatologia
Recuperação de Função Fisiológica
Mordeduras de Serpentes/metabolismo
Mordeduras de Serpentes/patologia
Mordeduras de Serpentes/fisiopatologia
Tailândia
Fatores de Tempo
Vietnã
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antivenins); 0 (Cholinergic Agonists); 0 (Cobra Neurotoxin Proteins); 0 (Elapid Venoms); 0 (Naja kaouthia venom)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160315
[St] Status:MEDLINE


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[PMID]:26293154
[Au] Autor:Das D; Sharma M; Kumar Das H; Pratim Sahu P; Doley R
[Ad] Endereço:Molecular Toxinology Laboratory, Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur-, 784028, India.
[Ti] Título:Purification and Characterization of Nk-3FTx: A Three Finger Toxin from the Venom of North East Indian Monocled Cobra.
[So] Source:J Biochem Mol Toxicol;30(2):59-70, 2016 Feb.
[Is] ISSN:1099-0461
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Snake venom three finger toxins (3FTxs) are a non-enzymatic family of venom proteins abundantly found in elapids. We have purified a 7579.5 ± 0.591 Da 3FTx named as Nk-3FTx from the venom of Naja kaouthia of North East India origin. The primary structure was determined by a combination of N-terminal sequencing and electrospray ionization liquid chromatography-mass spectrometry/mass spectrometry. Biochemical and biological characterization reveal that it is nontoxic to human cell lines and exhibit mild anticoagulant activity when tested on citrated human plasma. Nk-3FTx was found to affect the compound action potential (CAP) and nerve conduction velocity of isolated toad sciatic nerve. This is the first report of a non-conventional 3FTx from Naja kaouthia venom that reduces CAP for its neurotoxic effect. Further studies can be carried out to understand the mechanism of action and to explore its potential therapeutic application.
[Mh] Termos MeSH primário: Proteínas Neurotóxicas de Elapídeos/química
Venenos Elapídicos/química
Elapidae
[Mh] Termos MeSH secundário: Potenciais de Ação/efeitos dos fármacos
Animais
Bufonidae
Linhagem Celular
Proteínas Neurotóxicas de Elapídeos/isolamento & purificação
Proteínas Neurotóxicas de Elapídeos/farmacologia
Venenos Elapídicos/farmacologia
Seres Humanos
Camundongos
Condução Nervosa/efeitos dos fármacos
Nervo Isquiático/efeitos dos fármacos
Mordeduras de Serpentes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cobra Neurotoxin Proteins); 0 (Elapid Venoms); 0 (Naja kaouthia venom)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150822
[St] Status:MEDLINE
[do] DOI:10.1002/jbt.21734


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[PMID]:26518551
[Au] Autor:Utkin YN; Kasheverov IE; Kudryavtsev DS; Andreeva TV; Starkov VG; Ziganshin RH; Kuznetsov DV; Anh HN; Thao NT; Khoa NC; Tsetlin VI
[Ad] Endereço:Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia. utkin@mx.ibch.ru.
[Ti] Título:Nonconventional three-finger toxin BMLCL from krait Bungarus multicinctus venom with high affinity interacts with nicotinic acetylcholine receptors.
[So] Source:Dokl Biochem Biophys;464:294-7, 2015.
[Is] ISSN:1608-3091
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:Nonconventional three-finger toxin BMLCL was isolated from B. multicinctus venom, and its interaction with different subtypes of nicotinic acetylcholine receptor (nAChR) was studied. It was found that BMLCL is able to interact with high efficiency with both α7 and muscle type nAChRs.
[Mh] Termos MeSH primário: Bungarotoxinas/metabolismo
Bungarotoxinas/farmacologia
Colinérgicos/farmacologia
Receptores Nicotínicos/metabolismo
Proteínas de Répteis/metabolismo
Proteínas de Répteis/farmacologia
[Mh] Termos MeSH secundário: Acetilcolina/farmacologia
Sequência de Aminoácidos
Animais
Aplysia
Bungarotoxinas/química
Bungarotoxinas/isolamento & purificação
Bungarus
Colinérgicos/química
Colinérgicos/isolamento & purificação
Colinérgicos/metabolismo
Proteínas Neurotóxicas de Elapídeos/farmacologia
Seres Humanos
Lymnaea
Potenciais da Membrana/efeitos dos fármacos
Potenciais da Membrana/fisiologia
Dados de Sequência Molecular
Oócitos
Ratos
Proteínas de Répteis/química
Proteínas de Répteis/isolamento & purificação
Homologia de Sequência de Aminoácidos
Xenopus
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (BMLCL protein, Bungarus multicinctus multicinctus); 0 (Bungarotoxins); 0 (Cholinergic Agents); 0 (Cobra Neurotoxin Proteins); 0 (Receptors, Nicotinic); 0 (Reptilian Proteins); 69344-74-7 (alpha-cobratoxin); N9YNS0M02X (Acetylcholine)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151101
[St] Status:MEDLINE
[do] DOI:10.1134/S1607672915050099


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[PMID]:26221036
[Au] Autor:Kudryavtsev DS; Shelukhina IV; Son LV; Ojomoko LO; Kryukova EV; Lyukmanova EN; Zhmak MN; Dolgikh DA; Ivanov IA; Kasheverov IE; Starkov VG; Ramerstorfer J; Sieghart W; Tsetlin VI; Utkin YN
[Ad] Endereço:From the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya Street, Moscow 117997, Russia.
[Ti] Título:Neurotoxins from snake venoms and α-conotoxin ImI inhibit functionally active ionotropic γ-aminobutyric acid (GABA) receptors.
[So] Source:J Biol Chem;290(37):22747-58, 2015 Sep 11.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ionotropic receptors of γ-aminobutyric acid (GABAAR) regulate neuronal inhibition and are targeted by benzodiazepines and general anesthetics. We show that a fluorescent derivative of α-cobratoxin (α-Ctx), belonging to the family of three-finger toxins from snake venoms, specifically stained the α1ß3γ2 receptor; and at 10 µm α-Ctx completely blocked GABA-induced currents in this receptor expressed in Xenopus oocytes (IC50 = 236 nm) and less potently inhibited α1ß2γ2 ≈ α2ß2γ2 > α5ß2γ2 > α2ß3γ2 and α1ß3δ GABAARs. The α1ß3γ2 receptor was also inhibited by some other three-finger toxins, long α-neurotoxin Ls III and nonconventional toxin WTX. α-Conotoxin ImI displayed inhibitory activity as well. Electrophysiology experiments showed mixed competitive and noncompetitive α-Ctx action. Fluorescent α-Ctx, however, could be displaced by muscimol indicating that most of the α-Ctx-binding sites overlap with the orthosteric sites at the ß/α subunit interface. Modeling and molecular dynamic studies indicated that α-Ctx or α-bungarotoxin seem to interact with GABAAR in a way similar to their interaction with the acetylcholine-binding protein or the ligand-binding domain of nicotinic receptors. This was supported by mutagenesis studies and experiments with α-conotoxin ImI and a chimeric Naja oxiana α-neurotoxin indicating that the major role in α-Ctx binding to GABAAR is played by the tip of its central loop II accommodating under loop C of the receptors.
[Mh] Termos MeSH primário: Proteínas Neurotóxicas de Elapídeos
Conotoxinas
Simulação de Dinâmica Molecular
Receptores de GABA-A/química
Receptores de GABA-A/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Linhagem Celular Tumoral
Proteínas Neurotóxicas de Elapídeos/química
Proteínas Neurotóxicas de Elapídeos/farmacologia
Conotoxinas/química
Conotoxinas/farmacologia
Elapidae
Camundongos
Estrutura Secundária de Proteína
Receptores de GABA-A/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cobra Neurotoxin Proteins); 0 (Conotoxins); 0 (Receptors, GABA-A); 69344-74-7 (alpha-cobratoxin)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150730
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.648824


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[PMID]:26026717
[Au] Autor:Leong PK; Fung SY; Tan CH; Sim SM; Tan NH
[Ad] Endereço:Department of Molecular Medicine, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia.
[Ti] Título:Immunological cross-reactivity and neutralization of the principal toxins of Naja sumatrana and related cobra venoms by a Thai polyvalent antivenom (Neuro Polyvalent Snake Antivenom).
[So] Source:Acta Trop;149:86-93, 2015 Sep.
[Is] ISSN:1873-6254
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The low potency of cobra antivenom has been an area of concern in immunotherapy for cobra envenomation. This study sought to investigate factors limiting the neutralizing potency of cobra antivenom, using a murine model. We examined the immunological reactivity and neutralizing potency of a Thai polyvalent antivenom against the principal toxins of Naja sumatrana (Equatorial spitting cobra) venom and two related Asiatic cobra venom α-neurotoxins. The antivenom possesses moderate neutralizing potency against phospholipases A2 (P, potency of 0.98mg/mL) and moderately weak neutralizing potency against long-chain α-neurotoxins (0.26-0.42mg/mL) but was only weakly effective in neutralizing the short-chain α-neurotoxins and cardiotoxins (0.05-0.08mg/mL). The poor neutralizing potency of the antivenom on the low molecular mass short-chain neurotoxins and cardiotoxins is presumably the main limiting factor of the efficacy of the cobra antivenom. Our results also showed that phospholipase A2, which exhibited the highest ELISA reactivity and avidity, was most effectively neutralized, whereas N. sumatrana short-chain neurotoxin, which exhibited the lowest ELISA reactivity and avidity, was least effectively neutralized by the antivenom. These observations suggest that low immunoreactivity (low ELISA reactivity and avidity) is one of the reasons for poor neutralization of the cobra venom low molecular mass toxins. Nevertheless, the overall results show that there is a lack of congruence between the immunological reactivity of the toxins toward antivenom and the effectiveness of toxin neutralization by the antivenom, indicating that there are other factors that also contribute to the weak neutralization capacity of the antivenom. Several suggestions have been put forward to overcome the low efficacy of the cobra antivenom. The use of a 'proper-mix' formulation of cobra venoms as immunogen, whereby the immunogen mixture used for hyperimmunization contains a mix of various types of α-neurotoxins and cardiotoxins in sufficient amount, may also help to improve the efficacy and broaden the neutralization spectrum of the antivenom.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/imunologia
Antivenenos/imunologia
Proteínas Neurotóxicas de Elapídeos/imunologia
[Mh] Termos MeSH secundário: Animais
Reações Cruzadas
Venenos Elapídicos/imunologia
Elapidae
Ensaio de Imunoadsorção Enzimática
Glicoproteínas/imunologia
Imunização
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Antivenins); 0 (Cobra Neurotoxin Proteins); 0 (Elapid Venoms); 0 (Glycoproteins)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150601
[St] Status:MEDLINE



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