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  1 / 1382 MEDLINE  
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[PMID]:28796463
[Au] Autor:Kim CH; Lee YJ; Go HJ; Oh HY; Lee TK; Park JB; Park NG
[Ad] Endereço:Department of Biotechnology, College of Fisheries Sciences, Pukyong National University, Busan, Korea.
[Ti] Título:Defensin-neurotoxin dyad in a basally branching metazoan sea anemone.
[So] Source:FEBS J;284(19):3320-3338, 2017 Oct.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Recent studies suggest that vertebrate and invertebrate defensins have evolved from two independent ancestors, and that both defensins could share origins with animal toxins. Here, we purified novel sea anemone neurotoxin (BDS)-like antimicrobial peptides (AMPs)-Crassicorin-I and its putative homolog (Crassicorin-II)-from the pharynx extract of an anthozoan sea anemone (Urticina crassicornis). Based on structural analyses and cDNA cloning, mature Crassicorin-I represents a cationic AMP likely generated from a precursor and comprising 40 amino acid residues, including six cysteines forming three intramolecular disulfide bonds. Recombinant Crassicorin-I produced in a heterologous bacterial-expression system displayed antimicrobial activity against both a gram-positive bacterium (Bacillus subtilis) and gram-negative bacteria (Escherichia coli and Salmonella enterica). The Crassicorin-I transcript was upregulated by immune challenge, suggesting its involvement in defense mechanisms against infectious pathogens in sea anemone. Sequence alignment and three-dimensional molecular modeling revealed that Crassicorin-I exhibits high degrees of structural similarity to sea anemone neurotoxins that share ß-defensin fold which is found in vertebrate defensins and invertebrate big-defensins. Consistent with its structural similarity to neurotoxins, Crassicorin-I exhibited paralytic activity toward a crustacean. These findings motivated our investigation and subsequent discovery of antimicrobial activity from other known sea anemone neurotoxins, such as APETx1 and ShK. Collectively, our work signified that Crassicorin-I is the first AMP identified from a sea anemone and provided evidence of a functional linkage between AMPs and neurotoxins in a basally branching metazoan.
[Mh] Termos MeSH primário: Venenos de Cnidários/isolamento & purificação
Neurotoxinas/isolamento & purificação
Anêmonas-do-Mar/química
beta-Defensinas/isolamento & purificação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Bacillus subtilis/efeitos dos fármacos
Bacillus subtilis/crescimento & desenvolvimento
Sequência de Bases
Clonagem Molecular
Venenos de Cnidários/biossíntese
Venenos de Cnidários/química
Venenos de Cnidários/toxicidade
Sequência Conservada
Escherichia coli/efeitos dos fármacos
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Testes de Sensibilidade Microbiana
Modelos Moleculares
Neurotoxinas/biossíntese
Neurotoxinas/química
Neurotoxinas/toxicidade
Penaeidae/efeitos dos fármacos
Penaeidae/fisiologia
Peptídeos
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/toxicidade
Salmonella enterica/efeitos dos fármacos
Salmonella enterica/crescimento & desenvolvimento
Anêmonas-do-Mar/patogenicidade
Anêmonas-do-Mar/fisiologia
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
beta-Defensinas/biossíntese
beta-Defensinas/química
beta-Defensinas/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cnidarian Venoms); 0 (Neurotoxins); 0 (Peptides); 0 (Recombinant Proteins); 0 (beta-Defensins); 0 (crassicorin-I, Urticina crassicornis); 0 (crassicorin-II, Urticina crassicornis)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14194


  2 / 1382 MEDLINE  
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[PMID]:28596383
[Au] Autor:Dang B; Chhabra S; Pennington MW; Norton RS; Kent SBH
[Ad] Endereço:From the Department of Chemistry, University of Chicago, Chicago, Illinois 60637, bbdang@uchicago.edu.
[Ti] Título:Reinvestigation of the biological activity of d-allo-ShK protein.
[So] Source:J Biol Chem;292(30):12599-12605, 2017 Jul 28.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ShK toxin from the sea anemone is a 35-residue protein that binds to the Kv1.3 ion channel with high affinity. Recently we determined the X-ray structure of ShK toxin by racemic crystallography, in the course of which we discovered that d-ShK has a near-background IC value ∼50,000 times lower than that of the l-ShK toxin. This lack of activity was at odds with previously reported results for an ShK diastereomer designated d-allo-ShK, for which significant biological activity had been observed in a similar receptor-blocking assay. As reported, d-allo-ShK was made up of d-amino acids, but with retention of the natural stereochemistry of the chiral side chains of the Ile and Thr residues, containing d-allo-Ile and d-allo-Thr along with d-amino acids and glycine. To understand its apparent biological activity, we set out to chemically synthesize d-allo-ShK and determine its X-ray structure by racemic crystallography. Using validated allo-Thr and allo-Ile, both l-allo-ShK and d-allo-ShK polypeptide chains were prepared by total chemical synthesis. Neither the l-allo-ShK nor the d-allo-ShK polypeptides folded, whereas both l-ShK and d-ShK folded smoothly under the same conditions. Re-examination of NMR spectra of the previously reported d-allo-ShK protein revealed that diagnostic Thr and Ile signals were the same as for authentic d-ShK. On the basis of these results, we conclude that the previously reported d-allo-ShK was in fact d-ShK, the true enantiomer of natural l-ShK toxin, and that the apparent biological activity may have arisen from inadvertent contamination with trace amounts of l-ShK toxin.
[Mh] Termos MeSH primário: Venenos de Cnidários/metabolismo
Anêmonas-do-Mar/química
[Mh] Termos MeSH secundário: Animais
Venenos de Cnidários/química
Canal de Potássio Kv1.3/química
Canal de Potássio Kv1.3/metabolismo
Conformação Molecular
Ressonância Magnética Nuclear Biomolecular
Anêmonas-do-Mar/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cnidarian Venoms); 0 (Kv1.3 Potassium Channel); 0 (ShK neurotoxin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.793943


  3 / 1382 MEDLINE  
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[PMID]:28475608
[Au] Autor:Nikolaev MV; Dorofeeva NA; Komarova MS; Korolkova YV; Andreev YA; Mosharova IV; Grishin EV; Tikhonov DB; Kozlov SA
[Ad] Endereço:I.M.Sechenov Institute of Evolutionary Physiology and Biochemistry RAS, St.Petersburg, Russia.
[Ti] Título:TRPV1 activation power can switch an action mode for its polypeptide ligands.
[So] Source:PLoS One;12(5):e0177077, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:TRPV1 (vanilloid) receptors are activated by different types of stimuli including capsaicin, acidification and heat. Various ligands demonstrate stimulus-dependent action on TRPV1. In the present work we studied the action of polypeptides isolated from sea anemone Heteractis crispa (APHC1, APHC2 and APHC3) on rat TRPV1 receptors stably expressed in CHO cells using electrophysiological recordings, fluorescent Ca2+ measurements and molecular modeling. The APHCs potentiated TRPV1 responses to low (3-300 nM) concentrations of capsaicin but inhibited responses to high (>3.0 µM) concentrations. The activity-dependent action was also found for TRPV1 responses to 2APB and acidification. Thus the action mode of APHCs is bimodal and depended on the activation stimuli strength-potentiation of low-amplitude responses and no effect/inhibition of high-amplitude responses. The double-gate model of TRPV1 activation suggests that APHC-polypeptides may stabilize an intermediate state during the receptor activation. Molecular modeling revealed putative binding site at the outer loops of TRPV1. Binding to this site can directly affect activation by protons and can be allosterically coupled with capsaicin site. The results are important for further investigations of both TRPV1 and its ligands for potential therapeutic use.
[Mh] Termos MeSH primário: Capsaicina/farmacologia
Canais de Cátion TRPV/metabolismo
[Mh] Termos MeSH secundário: Animais
Células CHO
Venenos de Cnidários/farmacologia
Cricetulus
Ligantes
Modelos Moleculares
Peptídeos/farmacologia
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cnidarian Venoms); 0 (Ligands); 0 (Peptides); 0 (TRPV Cation Channels); 0 (Trpv1 protein, rat); 0 (analgesic polypeptide HC1, Heteractis crispa); S07O44R1ZM (Capsaicin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170506
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0177077


  4 / 1382 MEDLINE  
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[PMID]:28398099
[Au] Autor:Norton RS
[Ad] Endereço:a Medicinal Chemistry , Monash Institute of Pharmaceutical Sciences, Monash University , Parkville , Australia.
[Ti] Título:Enhancing the therapeutic potential of peptide toxins.
[So] Source:Expert Opin Drug Discov;12(6):611-623, 2017 Jun.
[Is] ISSN:1746-045X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Peptide toxins are potent and often exquisitely selective probes of the structure and function of ion channels and receptors, and as such are of significant interest to the pharmaceutical and biotech industries as both therapeutic leads and pharmacological tools. Their progression as clinical candidates, however, faces many of the challenges that are common to peptide drugs generally. Areas covered: The attributes of peptide toxins as therapeutic leads are outlined, as well as some of the limiting factors that have hampered the clinical development of many promising candidates. Strategies to overcome or circumvent these limitations are described, and their applications to peptide toxins from cone snails, sea anemones and scorpions are exemplified. Expert opinion: Peptide toxins have exceeded their promise as valuable pharmacological tools but have yet to yield the anticipated bounty of therapeutic leads. As the number of new peptides identified in venom transcriptomes and proteomes expands rapidly, screening approaches that capture those with genuine therapeutic potential are required, along with methods for enhancing the stability, pharmacokinetics and pharmacodynamics of these peptides.
[Mh] Termos MeSH primário: Desenho de Drogas
Descoberta de Drogas/métodos
Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Animais
Venenos de Cnidários/isolamento & purificação
Venenos de Cnidários/farmacologia
Caramujo Conus/metabolismo
Seres Humanos
Venenos de Moluscos/isolamento & purificação
Venenos de Moluscos/farmacologia
Peptídeos/isolamento & purificação
Proteoma
Venenos de Escorpião/isolamento & purificação
Venenos de Escorpião/farmacologia
Escorpiões/metabolismo
Anêmonas-do-Mar/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Cnidarian Venoms); 0 (Mollusk Venoms); 0 (Peptides); 0 (Proteome); 0 (Scorpion Venoms)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170412
[St] Status:MEDLINE
[do] DOI:10.1080/17460441.2017.1317243


  5 / 1382 MEDLINE  
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[PMID]:28396016
[Au] Autor:Soto C; Del Valle A; Valiente PA; Ros U; Lanio ME; Hernández AM; Alvarez C
[Ad] Endereço:Center for Protein Studies, Faculty of Biology, Havana University, Havana, CP 10400, Cuba.
[Ti] Título:Differential binding and activity of the pore-forming toxin sticholysin II in model membranes containing diverse ceramide-derived lipids.
[So] Source:Biochimie;138:20-31, 2017 Jul.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Sticholysin II is a pore-forming toxin produced by the sea anemone Stichodactyla helianthus that belongs to the actinoporin protein family. The high affinity of actinoporins for sphingomyelin (SM)-containing membranes has been well documented. However, the molecular determinants that define this affinity have not been fully clarified. Here, we have examined the binding and permeabilizing activity of StII to different single and mixed lipidic systems by combining lipid monolayers, liposomes, and permeabilizing assays. This study characterizes the contribution of ceramide-derived compounds for StII-membrane interaction. Molecular dynamics simulations revealed a differential binding mode of StII with the polar head group of SM and PC. The electrostatic interaction energies were the major energetic contributors to the better affinity of StII for SM compared to PC, while the van der Waals interaction energies were the major driving forces of the better affinity of StII for SM respect to Cer. Furthermore, the presence of sugar residues in glycosphingolipids modulated binding and pore-formation by actinoporins probably by hindering StII to reach relevant structural motifs in membrane for binding or inducing a non-competent adsorption to membrane. Our results demonstrate that StII-membrane interaction, leading to pore formation, may critically respond to changes in lipid head group properties, and the access to SM interfacial structural motif.
[Mh] Termos MeSH primário: Venenos de Cnidários/metabolismo
Simulação de Dinâmica Molecular
Anêmonas-do-Mar/química
Esfingomielinas/metabolismo
Termodinâmica
[Mh] Termos MeSH secundário: Animais
Venenos de Cnidários/química
Interações Hidrofóbicas e Hidrofílicas
Bicamadas Lipídicas/química
Lipossomos/química
Esfingomielinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cnidarian Venoms); 0 (Lipid Bilayers); 0 (Liposomes); 0 (Sphingomyelins); 0 (sticholysin II)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170412
[St] Status:MEDLINE


  6 / 1382 MEDLINE  
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[PMID]:28358312
[Au] Autor:Karas JA; Sani MA; Separovic F
[Ad] Endereço:School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne, VIC 3010, Australia. jkaras@unimelb.edu.au.
[Ti] Título:Chemical Synthesis and Characterization of an Equinatoxin II(1-85) Analogue.
[So] Source:Molecules;22(4), 2017 Mar 30.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The chemical synthesis of an 85 residue analogue of the pore-forming protein, Equinatoxin II (EqtII), was achieved. Peptide precursors with over 40 residues were assembled by solid phase synthesis. The EqtII(1-46) fragment was modified to the reactive C-terminal thioester and native chemical ligation was performed with the A47C mutated EqtII(47-85) peptide to form the EqtII(1-85) analogue. Circular dichroism spectroscopy indicated that the N-terminal domain of EqtII(1-46) and EqtII(1-85) maintains predominantly an α-helical structure in solution and also in the presence of lipid micelles. This demonstrates the feasibility of assembling the full 179 residue protein EqtII via chemical means. Site-specific isotopic labels could be incorporated for structural studies in membranes by solid-state NMR spectroscopy.
[Mh] Termos MeSH primário: Venenos de Cnidários/síntese química
[Mh] Termos MeSH secundário: Dicroísmo Circular
Venenos de Cnidários/química
Lipídeos/química
Espectroscopia de Ressonância Magnética
Micelas
Modelos Moleculares
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cnidarian Venoms); 0 (Lipids); 0 (Micelles); 54578-46-0 (equinatoxin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170518
[Lr] Data última revisão:
170518
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE


  7 / 1382 MEDLINE  
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[PMID]:28327816
[Au] Autor:Bastos DM; Haddad V; Nunes JL
[Ad] Endereço:Programa de Pós-Graduação em Saúde e Ambiente, Universidade Federal do Maranhão, São Luis, Maranhão, Brasil.
[Ti] Título:Human envenomations caused by Portuguese man-of-war (Physalia physalis) in urban beaches of São Luis City, Maranhão State, Northeast Coast of Brazil.
[So] Source:Rev Soc Bras Med Trop;50(1):130-134, 2017 Jan-Feb.
[Is] ISSN:1678-9849
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION:: The clinical and epidemiological aspects associated with Portuguese man-of-war envenomation were investigated and characterized. METHODS:: Data from recorded envenomation events between 2005 and 2013 were provided by the GBMar (Group of Firemen Maritime of Maranhão State) and SEMUSC (Municipal Secretary of Security with Citizenship). RESULTS:: Most victims were children, and clinical manifestations included intense pain, edema, erythema, and rare systemic manifestations. CONCLUSIONS:: The envenomation events were predictable and based on patterns involving multiple factors (environmental and/or human behavior); however, the initially applied measures did not match the current recommendations of the Health Ministry of Brazil.
[Mh] Termos MeSH primário: Venenos de Cnidários/envenenamento
Hidrozoários
[Mh] Termos MeSH secundário: Adolescente
Adulto
Animais
Praias
Brasil/epidemiologia
Criança
Pré-Escolar
Feminino
Seres Humanos
Lactente
Masculino
Meia-Idade
Estações do Ano
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cnidarian Venoms)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170503
[Lr] Data última revisão:
170503
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170323
[St] Status:MEDLINE


  8 / 1382 MEDLINE  
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[PMID]:28294982
[Au] Autor:Yanagihara AA; Wilcox CL
[Ad] Endereço:Department of Tropical Medicine, Medical Microbiology and Pharmacology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, HI 96822, USA. ayanagih@hawaii.edu.
[Ti] Título:Cubozoan Sting-Site Seawater Rinse, Scraping, and Ice Can Increase Venom Load: Upending Current First Aid Recommendations.
[So] Source:Toxins (Basel);9(3), 2017 Mar 15.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Cnidarian envenomations are the leading cause of severe and lethal human sting injuries from marine life. The total amount of venom discharged into sting-site tissues, sometimes referred to as "venom load", has been previously shown to correlate with tentacle contact length and sequelae severity. Since <1% of cnidae discharge upon initial tentacle contact, effective and safe removal of adherent tentacles is of paramount importance in the management of life-threatening cubozoan stings. We evaluated whether common rinse solutions or scraping increased venom load as measured in a direct functional assay of venom activity (hemolysis). Scraping significantly increased hemolysis by increasing cnidae discharge. For , increases did not occur if the tentacles were first doused with vinegar or if heat was applied. However, in , vinegar dousing and heat treatment were less effective, and the best outcomes occurred with the use of venom-inhibiting technologies (Sting No More products). Seawater rinsing, considered a "no-harm" alternative, significantly increased venom load. The application of ice severely exacerbated stings, but had a less pronounced effect on stings, while heat application markedly reduced hemolysis for both species. Our results do not support scraping or seawater rinsing to remove adherent tentacles.
[Mh] Termos MeSH primário: Mordeduras e Picadas/terapia
Cubomedusas
Primeiros Socorros/métodos
[Mh] Termos MeSH secundário: Animais
Venenos de Cnidários
Gelo
Água do Mar
Pele
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cnidarian Venoms); 0 (Ice)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE


  9 / 1382 MEDLINE  
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[PMID]:28258523
[Au] Autor:Frazão B; Campos A; Osório H; Thomas B; Leandro S; Teixeira A; Vasconcelos V; Antunes A
[Ad] Endereço:CIIMAR/CIMAR, Interdisciplinary Centre of Marine and Environmental Research, University of Porto, Terminal de Cruzeiros do Porto de Leixões, Av. General Norton de Matos, s/n, 4450-208, Porto, Portugal.
[Ti] Título:Analysis of Pelagia noctiluca proteome Reveals a Red Fluorescent Protein, a Zinc Metalloproteinase and a Peroxiredoxin.
[So] Source:Protein J;36(2):77-97, 2017 Apr.
[Is] ISSN:1875-8355
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pelagia noctiluca is the most venomous jellyfish in the Mediterranean Sea where it forms dense blooms. Although there is several published research on this species, until now none of the works has been focused on a complete protein profile of the all body constituents of this organism. Here, we have performed a detailed proteomics characterization of the major protein components expressed by P. noctiluca. With that aim, we have considered the study of jellyfish proteins involved in defense, body constituents and metabolism, and furthered explore the significance and potential application of such bioactive molecules. P. noctiluca body proteins were separated by1D SDS-PAGE and 2DE followed by characterization by nanoLC-MS/MS and MALDI-TOF/TOF techniques. Altogether, both methods revealed 68 different proteins, including a Zinc Metalloproteinase, a Red Fluorescent Protein (RFP) and a Peroxiredoxin. These three proteins were identified for the first time in P. noctiluca. Zinc Metalloproteinase was previously reported in the venom of other jellyfish species. Besides the proteins described above, the other 65 proteins found in P. noctiluca body content were identified and associated with its clinical significance. Among all the proteins identified in this work we highlight: Zinc metalloproteinase, which has a ShK toxin domain and therefore should be implicated in the sting toxicity of P. noctiluca.; the RFP which are a very important family of proteins due to its possible application as molecular markers; and last but not least the discovery of a Peroxiredoxin in this organism makes it a new natural resource of antioxidant and anti-UV radiation agents.
[Mh] Termos MeSH primário: Proteínas Luminescentes/análise
Metaloproteases/análise
Peroxirredoxinas/análise
Proteoma/análise
Cifozoários/metabolismo
[Mh] Termos MeSH secundário: Animais
Venenos de Cnidários/análise
Venenos de Cnidários/química
Eletroforese
Proteínas Luminescentes/química
Proteínas Luminescentes/metabolismo
Mar Mediterrâneo
Metaloproteases/química
Metaloproteases/metabolismo
Peroxirredoxinas/química
Peroxirredoxinas/metabolismo
Domínios Proteicos
Espectrometria de Massas por Ionização por Electrospray
Espectrometria de Massas em Tandem
Zinco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cnidarian Venoms); 0 (Luminescent Proteins); 0 (Proteome); 0 (ShK neurotoxin); 0 (red fluorescent protein); EC 1.11.1.15 (Peroxiredoxins); EC 3.4.- (Metalloproteases); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170305
[St] Status:MEDLINE
[do] DOI:10.1007/s10930-017-9695-0


  10 / 1382 MEDLINE  
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[PMID]:28258198
[Au] Autor:Laborde RJ; Sanchez-Ferras O; Luzardo MC; Cruz-Leal Y; Fernández A; Mesa C; Oliver L; Canet L; Abreu-Butin L; Nogueira CV; Tejuca M; Pazos F; Álvarez C; Alonso ME; Longo-Maugéri IM; Starnbach MN; Higgins DE; Fernández LE; Lanio ME
[Ad] Endereço:Center for Protein Studies, Faculty of Biology, University of Havana, Havana 10400, Cuba.
[Ti] Título:Novel Adjuvant Based on the Pore-Forming Protein Sticholysin II Encapsulated into Liposomes Effectively Enhances the Antigen-Specific CTL-Mediated Immune Response.
[So] Source:J Immunol;198(7):2772-2784, 2017 Apr 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vaccine strategies to enhance CD8 CTL responses remain a current challenge because they should overcome the plasmatic and endosomal membranes for favoring exogenous Ag access to the cytosol of APCs. As a way to avoid this hurdle, sticholysin (St) II, a pore-forming protein from the Caribbean Sea anemone , was encapsulated with OVA into liposomes (Lp/OVA/StII) to assess their efficacy to induce a CTL response. OVA-specific CD8 T cells transferred to mice immunized with Lp/OVA/StII experienced a greater expansion than when the recipients were injected with the vesicles without St, mostly exhibiting a memory phenotype. Consequently, Lp/OVA/StII induced a more potent effector function, as shown by CTLs, in vivo assays. Furthermore, treatment of E.G7-OVA tumor-bearing mice with Lp/OVA/StII significantly reduced tumor growth being more noticeable in the preventive assay. The contribution of CD4 and CD8 T cells to CTL and antitumor activity, respectively, was elucidated. Interestingly, the irreversibly inactive variant of the StI mutant StI W111C, encapsulated with OVA into Lp, elicited a similar OVA-specific CTL response to that observed with Lp/OVA/StII or vesicles encapsulating recombinant StI or the reversibly inactive StI W111C dimer. These findings suggest the relative independence between StII pore-forming activity and its immunomodulatory properties. In addition, StII-induced in vitro maturation of dendritic cells might be supporting these properties. These results are the first evidence, to our knowledge, that StII, a pore-forming protein from a marine eukaryotic organism, encapsulated into Lp functions as an adjuvant to induce a robust specific CTL response.
[Mh] Termos MeSH primário: Adjuvantes Imunológicos/administração & dosagem
Vacinas Anticâncer/imunologia
Venenos de Cnidários/administração & dosagem
Neoplasias Experimentais/patologia
Linfócitos T Citotóxicos/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Venenos de Cnidários/imunologia
Feminino
Citometria de Fluxo
Lipossomos/imunologia
Camundongos
Camundongos Endogâmicos C57BL
Linfócitos T Citotóxicos/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adjuvants, Immunologic); 0 (Cancer Vaccines); 0 (Cnidarian Venoms); 0 (Liposomes); 0 (sticholysin II)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170305
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1600310



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