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Yarlequé Armando. - One of the best experts on this subject based on the ideXlab platform.
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In vitro activity of venoms Lachesis Muta and Bothrops atroxSOBRE feasibility and embryonic development of eggs Ascaris suum
Facultad de Ciencias Biológicas Universidad Nacional Mayor de San Marcos, 2014Co-Authors: Paredes Claudia, Gárate Inés, Yarlequé Armando.Abstract:Los venenos de serpientes son concentrados polienzimáticos cuya actividad biológica sobre algunas bacterias y protozoos ha sido comprobada. El objetivo principal del presente trabajo fue estudiar la actividad in vitro de los venenos totales de las serpientes Lachesis Muta y Bothrops atrox sobre la viabilidad y el desarrollo embrionario de los huevos de Ascaris suum. Se emplearon los venenos totales en concentraciones de 2, 4, 8 y 16 mg/mL sobre huevos no embrionados y larvados in vitro. Se comparó la actividad de los venenos con la de otras sustancias como el hipoclorito de sodio al 5,25%, Albendazol (solución comercial) y solución salina. Ambos venenos, en concentraciones de 4, 8 y 16 mg/mL, inhibieron la blastulación de estos huevos; hasta el sexto día de incubación; en cambio en concentración de 2 mg/mL la inhibición se dio hasta el cuarto día. Posteriormente iniciaron un proceso de embrionación aparentemente normal hasta la formación del estadio infectante. El veneno de B. atrox fue el que presentó el mayor efecto inhibitorio en concentración de 16 mg/mL. El hipoclorito de sodio destruyó el 100% de los huevos, mientras el albendazol ocasionó que los huevos iniciaran un proceso de segmentación anormal que originó su degeneración. Se concluye que los venenos de L. Muta y B. atrox muestran actividad inhibitoria al inicio de la blastulación de los huevos de A. suum y no ejercen ningún efecto en los huevos larvados.Snake venoms are polienzymatic concentrated whose biological activity on some bacteria and protozoa has been proven. To study the in vitro activity of Lachesis Muta and B othrops atrox venoms on the viability and the development of Ascaris suum eggs is the main objecbve of this work. The venoms were employed in non embryonated and in vitro embryonated eggs of Ascaris suum at different concentrations (2, 4, 8,16 mg/mL). The activity of the venoms in the eggs and other substances like 5,25% sodium hypochlorite, Albendazol (commercial solution) and sodium chloride was compared. Both venoms, at 2, 4, 8, 16 mg/mL concentrations, inhibited segmentation of these eggs until the sixth day of incubation, when they began an apparently normal embryonation process that ended in the formation of the infective stage. The most effective inhibitory concentration was 16 mg/mL of B. atrox venom. The sodium hypochlorite destroyed 100% of eggs, while Albendazol produced abnormal segmentation process on them and their degeneration. We conclude that L. Muta and B. atrox venoms have an inhibitory activity at the begining of segmentation in Ascaris suum eggs and they do not cause any effect on embryonated ones
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Purification of a lectin type C from the venom of Lachesis Muta Peruvian snake.
Sociedad Química del Perú., 2013Co-Authors: Palomino Mercedes., Lazo Fanny., Delgadillo Julio., Severino Ruperto., Yarlequé Armando.Abstract:PALOMINO, Mercedes, LAZO, Fanny, DELGADILLO, Julio [et al.]. Purificación de una lectina tipo C del veneno de la serpiente peruana Lachesis Muta. Revista de la Sociedad Química del Perú [en línea]. 2012, vol. 78, no. 3, p. 161-169. ISSN 1810-634X.A partir del veneno de la serpiente Lachesis Muta, que habita en la amazonía peruana, se purificó y determinó las propiedades bioquímicas de una proteína no enzimática denominada lectina Tipo C. La purificación se logró a través de un único paso cromatográfico utilizando una columna de EAE-Sephadex A-50 equilibrada con buffer acetato de amonio 0,1 M pH 5. La lectina fue reconocida debido a su capacidad para aglutinar glóbulos rojos humanos in vitro; por lo que se trata de una hemoaglutinina. La proteína en estudio fue purificada 3,6 veces y representó el 3,5 % del contenido proteico total del veneno. El análisis por PAGE-SDS, demostró que la lectina se encontraba al estado homogéneo con una masa molecular de 27, 5 kDa y 14,3 kDa en su forma reducida. La lectina fue inhibida en su actividad por la lactosa (1,56 mM), seguida de galactosa, arabinosa, sacarosa y glucosa. En cambio, no se registró inhibición con maltosa, manosa y fructosa. La capacidad hemoaglutinante de la lectina también fue inhibida por EDTA, seguida de DTT y 2-mercaptoetanol a distintas concentraciones; la inhibición causada por EDTA (0,125 - 0,5 mM), fue anulada por los iones +2 +2 +2Ca , Mg y Mn . Los resultados indican que la proteína purificada es una lectina tipo C, la cual es una potente hemoaglutinina
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Biological characterization and inhibitors action of Phospholipase A2 from Lachesis Muta venom
Revista Peruana de Biología, 2011Co-Authors: Inga Rosalina., Vivas Dan., Palermo Pedro., Mendoza Julio., Lazo Fanny., Yarlequé Armando.Abstract:INGA, Rosalina [et al.]. Caracterización biológica y acción de inhibidores de una fosfolipasa A2 del veneno de Lachesis Muta: Biological characterization and inhibitors action of Phospholipase A2 from Lachesis Muta venom. Revista Peruana de Biología [en línea]. abr. 2010, vol. 17, no. 1, p. 123-128. ISSN 1727-9933.El presente trabajo informa de la purificación y caracterización bioquímica y biológica de la fosfolipasa A2 (PLA2) de Lachesis Muta (Linnaeus, 1766). La purificación se realizó por cromatografía liquida (CL) usando CM-Sephadex C-50 y Sephadex G-50, obteniéndola al estado homogéneo con un peso molecular de 18749 Da. Los ensayos con PLA2 realizados sobre fosfolípidos de yema de huevo y lecitina comercial, mostraron que los agentes EDTA, PMSF, glutatión y cisteína, inhibieron la actividad con valores mayores al 50%. La PLA2 de L. Muta produjo un notable efecto anticoagulante, observándose un retardo de 2'30" en el tiempo de coagulación con 9,6 µg de la enzima. La hemólisis indirecta sobre eritrocitos humanos dio un equivalente de 4,35 µg como dosis hemolítica media (HD50). Los valores de dosis edemática media y dosis miotóxica mínima fueron de 91,5 µg y 125,89 µg/mL respectivamente; valores por debajo de PLA2 de otros venenos. No se registró actividad hemorrágica directa. Las pruebas de inmunodifusión e inmunoelectroforésis revelaron que PLA2 de L. Muta tuvo reactividad inmunogénica contra el antiveneno lachésico monovalente (INS-Perú). Sin embargo, la neutralización por el antiveneno fue parcial
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Clonaje caracterización molecular in silico de un transcrito de fosfolipasa A, aislado del veneno de la serpiente peruana Lachesis Muta
Instituto Nacional de Salud, 2010Co-Authors: Jimenez, Karim L., Yarlequé Armando., Zavaleta Amparo, Izaguirre Victor, Inga, Rosio R.Abstract:Objective. Isolate and characterize in silico gene phospholipase A2 (PLA2 ) isolated from Lachesis Muta venom of the Peruvian Amazon. Material and methods. Technique RT-PCR from total RNA was using specific primers, the amplified DNA product was inserted into the pGEM vector for subsequent sequencing. By bioinformatic analysis identified an open reading frame of 414 nucleotides that encoded 138 amino acids including a signal peptide of 16 aminoacids, molecular weight and pI were 13 976 kDa and 5.66 respectively. Results. The aminoacid sequence was called Lm-PLA2 -Peru, contains an aspartate at position 49, this aminoacid in conjunction with other conserved residues such as Tyr-28, Gly-30, Gly-32, His-48, Tyr52, Asp99 are important for enzymatic activity. The comparison with the amino acid sequence data banks showed of similarity between PLA2 from Lachesis stenophrys (93%) and other PLA2 snake venoms and over 80% of other sPLA2 family Viperidae venoms. A phylogenetic analysis showed that Lm-PLA2 -Peru grouped with other acidic [Asp49] sPLA2 previously isolated from Bothriechis schlegelii venom showing 89 % nucleotide sequence identity. Finally, the computer modeling indicated that enzyme had the characteristic structure of sPLA2 group II that consisted of three α-helices, a β-wing, a short helix and a calcium-binding loop. Conclusion. The nucleotide sequence corresponding to the first transcript of gene from PLA2 cloned of Lachesis Muta venom, snake from the Peruvian rainforest.Objetivo. Aislar y caracterizar in silico un transcrito del gen de fosfolipasa A2 (PLA2 ) aislado del veneno de Lachesis Muta de la Amazonía peruana. Materiales y métodos. Se amplificó el transcrito del gen sPLA2 mediante la técnica de RT-PCR a partir de RNA total utilizando cebadores específicos, el producto de DNA amplificado se insertó en el vector pGEM para su posterior secuenciación. Mediante análisis bioinformático de la secuencia nucleotídica se determinó un marco de lectura abierta de 414 nucleótidos que codifica 138 aminoácidos, incluyendo16 aminoácidos del péptido señal, el peso molecular y el pI fueron de 13 976 kDa y 5,66 respectivamente. Resultados. La secuencia aminoacídica denominada Lm-PLA2 - Perú, contiene Asp49, así como Tyr-28, Gly-30, Gly-32, His-48, Tyr52, Asp99 importantes para la actividad enzimática. La comparación de Lm-PLA2 -Perú con las secuencias aminoacídicas de los bancos de datos mostró 93% de similitud con las sPLA2 de Lachesis stenophrys y más del 80% con otras sPLA2 de venenos de la familia Viperidae. El análisis filogenético de la secuencia nucleotídica del transcrito del gen sPLA2 indica que Lm-PLA2 -Perú se agrupa con otras sPLA2 [Asp49] ácidas previamente aisladas del veneno de Bothriechis schlegelii con un 89% de identidad. El modelaje tridimensional de Lm-PLA2 -Perú, presenta una estructura característica de sPLA2 del Grupo II formada por tres hélices-α, una lámina-β, una hélice corta y un lazo de unión con calcio. Conclusión. La secuencia nucleotídica corresponde al primer transcripto del gen de PLA2 clonado a partir del veneno de la serpiente Lachesis Muta, que habita en la selva del Perú
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Caracterización biológica y acción de inhibidores de una fosfolipasa A2 del veneno de Lachesis Muta
Facultad de Ciencias Biológicas Universidad Nacional Mayor de San Marcos, 2010Co-Authors: Inga Rosalina., Vivas Dan., Palermo Pedro., Mendoza Julio., Lazo Fanny., Yarlequé Armando.Abstract:In the present study, phospholipase A2 (PLA2) from Lachesis Muta (Linnaeus, 1766), is isolated, purified and characterized biochemically and biologically. Purification was performed by liquid chromatography (LC) using CM-Sephadex C-50 and Sephadex G-50, homogenized enzyme had a molecular weight of 18749 Da. Trials with egg yolk phospholipids, and commercial lecithin showed that EDTA, PMSF, glutathione and cysteine inhibited the activity with values greater than 50%. The PLA2 had a significant anticoagulant effect, showing a delay of 2'30" on the coagulation time with 9.6 µg of the enzyme. The indirect impact on human erythrocyte hemolysis gave an equivalent of 4.35 µg as HD50. Mean edematic dose and minimum myotoxic dose were 91.5 mg and 125.89 mg / mL respectively, these values were below enzymes phospholipase A2 from others poisons. There was no hemorrhagic activity. Immunodiffusion tests and immunoelectrophoresis revealed that the PLA2 of L. Muta was immunogenic reactivity against lachesic monovalent antivenom (INS-Peru). However, the neutralization by the antivenom was partial.El presente trabajo informa de la purificación y caracterización bioquímica y biológica de la fosfolipasa A2 (PLA2) de Lachesis Muta (Linnaeus, 1766). La purificación se realizó por cromatografía liquida (CL) usando CM-Sephadex C-50 y Sephadex G-50, obteniéndola al estado homogéneo con un peso molecular de 18749 Da. Los ensayos con PLA2 realizados sobre fosfolípidos de yema de huevo y lecitina comercial, mostraron que los agentes EDTA, PMSF, glutatión y cisteína, inhibieron la actividad con valores mayores al 50%. La PLA2 de L. Muta produjo un notable efecto anticoagulante, observándose un retardo de 2'30" en el tiempo de coagulación con 9,6 µg de la enzima. La hemólisis indirecta sobre eritrocitos humanos dio un equivalente de 4,35 µg como dosis hemolítica media (HD50). Los valores de dosis edemática media y dosis miotóxica mínima fueron de 91,5 µg y 125,89 µg/mL respectivamente; valores por debajo de PLA2 de otros venenos. No se registró actividad hemorrágica directa. Las pruebas de inmunodifusión e inmunoelectroforésis revelaron que PLA2 de L. Muta tuvo reactividad inmunogénica contra el antiveneno lachésico monovalente (INS-Perú). Sin embargo, la neutralización por el antiveneno fue parcial
Daniela C S Damico - One of the best experts on this subject based on the ideXlab platform.
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Research Article Rapid Purification and Procoagulant and Platelet Aggregating Activities of Rhombeobin: A Thrombin-Like/Gyroxin-Like Enzyme from Lachesis Muta rhombeata Snake Venom
2013Co-Authors: Frank Denis Torres-huaco, Sergio Marangoni, Edson Antunes, Camila B Mendes, Claudio C Werneck, Cristina Pontes Vicente, Talita Vassequi-silva, Ana Cláudia Coelho Nery-diez, Daniela C S DamicoAbstract:Copyright © 2013 Frank Denis Torres-Huaco et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. We report a rapid purification method using one-step chromatography of SVSP Rhombeobin (LMR-47) from Lachesis Muta rhombeata venom and its procoagulant activities and effects on platelet aggregation. The venom was fractionated by a single chromatographic step in RP-HPLC on a C8 Discovery BIO Wide Pore, showing high degree of molecular homogeneity with molecular mass of 47035.49Da. Rhombeobin showed amidolytic activity upon B
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lmrtx a basic pla2 d49 purified from Lachesis Muta rhombeata snake venom with enzymatic related antithrombotic and anticoagulant activity
Toxicon, 2012Co-Authors: Daniela C S Damico, Edson Antunes, T Vassequisilva, Frank Denis Torreshuaco, A C C Nerydiez, R C G De Souza, S L Da Silva, Cristina P Vicente, Camila B Mendes, Claudio C WerneckAbstract:Abstract A basic phospholipase A 2 (LmrTX) isoform was isolated from Lachesis Muta rhombeata snake venom and partially characterized. The venom was fractionated by molecular exclusion chromatography in ammonium bicarbonate buffer followed by reverse-phase HPLC on a C-5 Discovery ® Bio Wide column. From liquid chromatography–electrospray ionization/mass spectrometry, the molecular mass of LmrTX was measured as 14.277.50 Da. The amino acid sequence showed a high degree of homology between PLA 2 LmrTX from L. Muta rhombeata and other PLA 2 from snake venoms, like CB1 and CB2 from Crotalus durissus terrificus ; LmTX-I and LmTX-II from Lachesis Muta Muta . LmrTX had PLA 2 activity in the presence of a synthetic substrate and alkylation of histidine residues significantly inhibited ( P 2 from L. Muta rhombeata venom, caused a change in the occlusion time to 99 ± 10 min with doses of 7.5 μg/mice. Additionally, LmrTX showed the anticoagulant activity in vitro and ex vivo and prolonging the time aggregation in wash platelet induced by ADP and Thrombin.
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inflammatory oedema induced by Lachesis Muta Muta surucucu venom and lmtx i in the rat paw and dorsal skin
Toxicon, 2009Co-Authors: Tatiane Ferreira, Enilton A Camargo, Maria Teresa C P Ribela, Daniela C S Damico, Sergio Marangoni, Edson Antunes, Gilberto De Nucci, Elen C T LanducciAbstract:The ability of crude venom and a basic phospholipase A2 (LmTX-I) from Lachesis Muta Muta venom to increase the microvascular permeability in rat paw and skin was investigated. Crude venom or LmTX-I were injected subplantarly or intradermally and rat paw oedema and dorsal skin plasma extravasation were measured. Histamine release from rat peritoneal mast cell was also assessed. Crude venom or LmTX-I induced dose-dependent rat paw oedema and dorsal skin plasma extravasation. Venom-induced plasma extravasation was inhibited by the histamine H1 antagonist mepyramine (6 mg/kg), histamine/5-hydroxytriptamine antagonist cyproheptadine (2 mg/kg), cyclooxygenase inhibitor indomethacin (5 mg/kg), nitric oxide synthesis inhibitor L-NAME (100 nmol/site), tachykinin NK1 antagonist SR140333 (1 nmol/site) and bradykinin B2 receptor antagonist Icatibant (0.6 mg/kg). Platelet-activating factor (PAF) antagonist PCA4248 (5 mg/kg) had no effect. LmTX-I-induced skin extravasation was inhibited by cyproheptadine, mepyramine, indomethacin and PCA4248, while L-NAME and SR140333 had no effect. Additionally, both Lachesis Muta Muta venom and LmTX-I concentration-dependently induced histamine release from rat mast cells. In conclusion, Lachesis Muta Muta venom and LmTX-I increase microvascular permeability by mechanisms involving in vivo mast cell activation and arachidonic acid metabolites. Additionally, crude venom-induced responses also involve substance P, nitric oxide and bradykinin release, whether LmTX-I-induced responses involve PAF. 2008 Published by Elsevier Ltd.
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functional characterization of a basic d49 phospholipase a2 lmtx i from the venom of the snake Lachesis Muta Muta bushmaster
Toxicon, 2006Co-Authors: Daniela C S Damico, Sergio Marangoni, Lilian G F Bueno, Lea Rodriguessimioni, Maria Alice Da Cruzhofling, Jose C NovelloAbstract:Abstract The whole venom of Lachesis Muta Muta is preponderantly neurotoxic but moderately myotoxic on the chick biventer cervicis preparation (BCp). We have now examined these toxic activities of a basic phospholipase A 2 , LmTX-I, isolated from the whole venom. LmTX-I caused a significant concentration–dependent neuromuscular blockade in the BCp. The time to produce 50% neuromuscular blockade was 14.7±0.75 min (30 μg/ml), 23.6±0.9 min (10 μg/ml), 34±1.7 min (2.5 μg/ml) and 39.2±3.6 min (1 μg/ml), ( n =5/concentration; p p 2 present on venom from L. m. Muta (LmTX-I) possesses a dominant neurotoxic action on isolated chick nerve-muscle preparations, whereas myotoxicity was mainly observed at the highest concentration used (30 μg/ml). These effects of LmTX-I closely reproduce the effects of the whole venom of L. m. Muta in chick neuromuscular preparations.
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biochemical and enzymatic characterization of two basic asp49 phospholipase a2 isoforms from Lachesis Muta Muta surucucu venom
Biochimica et Biophysica Acta, 2005Co-Authors: Daniela C S Damico, Gilberto De Nucci, Jose C Novello, Sergio Lilla, Luis Alberto Poncesoto, Flavia Vischi Winck, Sergio MarangoniAbstract:Abstract Two basic phospholipase A2 (PLA2) isoforms were isolated from Lachesis Muta Muta snake venom and partially characterized. The venom was fractionated by molecular exclusion chromatography in ammonium bicarbonate buffer followed by reverse-phase HPLC on a C-18 μ-Bondapack column and RP-HPLC on a C-8 column. From liquid chromatography-electrospray ionization/mass spectrometry, the molecular mass of the two isoforms LmTX-I and LmTX-II was respectively measured as 14,245.4 and 14,186.2 Da. The pI was respectively estimated to be 8.7 and 8.6 for LmTX-I and LmTX-II, as determined by two-dimensional electrophoresis. The two proteins were sequenced and differentiated from each other by a single amino acid substitution, Arg65 (LmTX-I) → Pro65 (LmTX-II). The amino acid sequence showed a high degree of homology between PLA2 isoforms from Lachesis Muta Muta and other PLA2 snake venoms. LmTX-I and LmTX-II had PLA2 activity in the presence of a synthetic substrate and showed a minimum sigmoidal behaviour; with maximal activity at pH 8.0 and 35–45 °C. Full PLA2 activity required Ca2+ and was respectively inhibited by Cu2+ and Zn2+ in the presence and absence of Ca2+. Crotapotin from Crotalus durissus cascavella rattlesnake venom significantly inhibited (P
Andre Lopes Fuly - One of the best experts on this subject based on the ideXlab platform.
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Research Article Inhibitory Effect of Plant Manilkara subsericea against Biological Activities of Lachesis Muta Snake Venom
2016Co-Authors: Eduardo Coriolano, Eládio Flores Sanchez, De Oliveira, Caio Pinho Fern, Ro Rocha, Andre Lopes FulyAbstract:Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Snake venom is composed of a mixture of substances that caused in victims a variety of pathophysiological effects. Besides antivenom, literature has described plants able to inhibit injuries and lethal activities induced by snake venoms.This work describes the inhibitory potential of ethanol, hexane, ethyl acetate, or dichloromethane extracts and fractions from stem and leaves of Manilkara subsericea against in vivo (hemorrhagic and edema) and in vitro (clotting, hemolysis, and proteolysis) activities caused by Lachesis Muta venom. All the tested activities were totally or at least partially reduced byM. subsericea. However, when L. Muta venom was injected into mice 15min first or after the materials, hemorrhage and edema were not inhibited. Thus, M. subsericea could be used as antivenom in snakebites of L. Muta. And, this work also highlights Brazilian flora as a rich source of molecules with antivenom properties. 1
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sulfated galactan from palisada flagellifera inhibits toxic effects of Lachesis Muta snake venom
Marine Drugs, 2015Co-Authors: Ana Claudia Rodrigues Da Silva, Eladio F Sanchez, Luciana G Ferreira, Maria Eugenia R Duarte, Miguel D Noseda, Andre Lopes FulyAbstract:In Brazil, snakebites are a public health problem and accidents caused by Lachesis Muta have the highest mortality index. Envenomation by L. Muta is characterized by systemic (hypotension, bleeding and renal failure) and local effects (necrosis, pain and edema). The treatment to reverse the evolution of all the toxic effects is performed by injection of antivenom. However, such therapy does not effectively neutralize tissue damage or any other local effect, since in most cases victims delay seeking appropriate medical care. In this way, alternative therapies are in demand, and molecules from natural sources have been exhaustively tested. In this paper, we analyzed the inhibitory effect of a sulfated galactan obtained from the red seaweed Palisada flagellifera against some toxic activities of L. Muta venom. Incubation of sulfated galactan with venom resulted in inhibition of hemolysis, coagulation, proteolysis, edema and hemorrhage. Neutralization of hemorrhage was also observed when the galactan was administered after or before the venom injection; thus mimicking a real in vivo situation. Moreover, the galactan blocked the edema caused by a phospholipase A2 isolated from the same venom. Therefore, the galactan from P. flagellifera may represent a promising tool to treat envenomation by L. Muta as a coadjuvant for the conventional antivenom.
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inhibitory effect of plant manilkara subsericea against biological activities of Lachesis Muta snake venom
BioMed Research International, 2014Co-Authors: Eduardo Coriolano De Oliveira, Eladio F Sanchez, Caio P Fernandes, Leandro Rocha, Andre Lopes FulyAbstract:Snake venom is composed of a mixture of substances that caused in victims a variety of pathophysiological effects. Besides antivenom, literature has described plants able to inhibit injuries and lethal activities induced by snake venoms. This work describes the inhibitory potential of ethanol, hexane, ethyl acetate, or dichloromethane extracts and fractions from stem and leaves of Manilkara subsericea against in vivo (hemorrhagic and edema) and in vitro (clotting, hemolysis, and proteolysis) activities caused by Lachesis Muta venom. All the tested activities were totally or at least partially reduced by M. subsericea. However, when L. Muta venom was injected into mice 15 min first or after the materials, hemorrhage and edema were not inhibited. Thus, M. subsericea could be used as antivenom in snakebites of L. Muta. And, this work also highlights Brazilian flora as a rich source of molecules with antivenom properties.
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antivenom effects of 1 2 3 triazoles against bothrops jararaca and Lachesis Muta snakes
BioMed Research International, 2013Co-Authors: Thaisa Francielle Souza Domingos, Eladio F Sanchez, Carla Carvalho, Laura De Andrade Moura, Vinicius R Campos, Alessandro K Jordao, Anna C Cunha, Vitor F Ferreira, Maria Cecilia B V De Souza, Andre Lopes FulyAbstract:Snake venoms are complex mixtures of proteins of both enzymes and nonenzymes, which are responsible for producing several biological effects. Human envenomation by snake bites particularly those of the viperid family induces a complex pathophysiological picture characterized by spectacular changes in hemostasis and frequently hemorrhage is also seen. The present work reports the ability of six of a series of 1,2,3-triazole derivatives to inhibit some pharmacological effects caused by the venoms of Bothrops jararaca and Lachesis Muta. In vitro assays showed that these compounds were impaired in a concentration-dependent manner, the fibrinogen or plasma clotting, hemolysis, and proteolysis produced by both venoms. Moreover, these compounds inhibited biological effects in vivo as well. Mice treated with these compounds were fully protected from hemorrhagic lesions caused by such venoms. But, only the B. jararaca edema-inducing activity was neutralized by the triazoles. So the inhibitory effect of triazoles derivatives against some in vitro and in vivo biological assays of snake venoms points to promising aspects that may indicate them as molecular models to improve the production of effective antivenom or to complement antivenom neutralization, especially the local pathological effects, which are partially neutralized by antivenoms.
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Appraisal of Antiophidic Potential of Marine Sponges against Bothrops jararaca and Lachesis Muta Venom
MDPI AG, 2013Co-Authors: Guilherme Muricy, Eduardo Coriolano De Oliveira, Thaisa Francielle Souza Domingos, Eládio Flores Sanchez, Suzi Ribeiro, Camila Nunes Faioli, Andre Lopes FulyAbstract:Snakebites are a health problem in many countries due to the high incidence of such accidents. Antivenom treatment has regularly been used for more than a century, however, this does not neutralize tissue damage and may even increase the severity and morbidity of accidents. Thus, it has been relevant to search for new strategies to improve antiserum therapy, and a variety of molecules from natural sources with antiophidian properties have been reported. In this paper, we analyzed the ability of ten extracts from marine sponges (Amphimedon viridis, Aplysina fulva, Chondrosia collectrix, Desmapsamma anchorata, Dysidea etheria, Hymeniacidon heliophila, Mycale angulosa, Petromica citrina, Polymastia janeirensis, and Tedania ignis) to inhibit the effects caused by Bothrops jararaca and Lachesis Muta venom. All sponge extracts inhibited proteolysis and hemolysis induced by both snake venoms, except H. heliophila, which failed to inhibit any biological activity. P. citrina inhibited lethality, hemorrhage, plasma clotting, and hemolysis induced by B. jararaca or L. Muta. Moreover, other sponges inhibited hemorrhage induced only by B. jararaca. We conclude that Brazilian sponges may be a useful aid in the treatment of snakebites caused by L. Muta and B. jararaca and therefore have potential for the discovery of molecules with antiophidian properties
Sergio Marangoni - One of the best experts on this subject based on the ideXlab platform.
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Research Article Rapid Purification and Procoagulant and Platelet Aggregating Activities of Rhombeobin: A Thrombin-Like/Gyroxin-Like Enzyme from Lachesis Muta rhombeata Snake Venom
2013Co-Authors: Frank Denis Torres-huaco, Sergio Marangoni, Edson Antunes, Camila B Mendes, Claudio C Werneck, Cristina Pontes Vicente, Talita Vassequi-silva, Ana Cláudia Coelho Nery-diez, Daniela C S DamicoAbstract:Copyright © 2013 Frank Denis Torres-Huaco et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. We report a rapid purification method using one-step chromatography of SVSP Rhombeobin (LMR-47) from Lachesis Muta rhombeata venom and its procoagulant activities and effects on platelet aggregation. The venom was fractionated by a single chromatographic step in RP-HPLC on a C8 Discovery BIO Wide Pore, showing high degree of molecular homogeneity with molecular mass of 47035.49Da. Rhombeobin showed amidolytic activity upon B
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inflammatory oedema induced by Lachesis Muta Muta surucucu venom and lmtx i in the rat paw and dorsal skin
Toxicon, 2009Co-Authors: Tatiane Ferreira, Enilton A Camargo, Maria Teresa C P Ribela, Daniela C S Damico, Sergio Marangoni, Edson Antunes, Gilberto De Nucci, Elen C T LanducciAbstract:The ability of crude venom and a basic phospholipase A2 (LmTX-I) from Lachesis Muta Muta venom to increase the microvascular permeability in rat paw and skin was investigated. Crude venom or LmTX-I were injected subplantarly or intradermally and rat paw oedema and dorsal skin plasma extravasation were measured. Histamine release from rat peritoneal mast cell was also assessed. Crude venom or LmTX-I induced dose-dependent rat paw oedema and dorsal skin plasma extravasation. Venom-induced plasma extravasation was inhibited by the histamine H1 antagonist mepyramine (6 mg/kg), histamine/5-hydroxytriptamine antagonist cyproheptadine (2 mg/kg), cyclooxygenase inhibitor indomethacin (5 mg/kg), nitric oxide synthesis inhibitor L-NAME (100 nmol/site), tachykinin NK1 antagonist SR140333 (1 nmol/site) and bradykinin B2 receptor antagonist Icatibant (0.6 mg/kg). Platelet-activating factor (PAF) antagonist PCA4248 (5 mg/kg) had no effect. LmTX-I-induced skin extravasation was inhibited by cyproheptadine, mepyramine, indomethacin and PCA4248, while L-NAME and SR140333 had no effect. Additionally, both Lachesis Muta Muta venom and LmTX-I concentration-dependently induced histamine release from rat mast cells. In conclusion, Lachesis Muta Muta venom and LmTX-I increase microvascular permeability by mechanisms involving in vivo mast cell activation and arachidonic acid metabolites. Additionally, crude venom-induced responses also involve substance P, nitric oxide and bradykinin release, whether LmTX-I-induced responses involve PAF. 2008 Published by Elsevier Ltd.
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functional characterization of a basic d49 phospholipase a2 lmtx i from the venom of the snake Lachesis Muta Muta bushmaster
Toxicon, 2006Co-Authors: Daniela C S Damico, Sergio Marangoni, Lilian G F Bueno, Lea Rodriguessimioni, Maria Alice Da Cruzhofling, Jose C NovelloAbstract:Abstract The whole venom of Lachesis Muta Muta is preponderantly neurotoxic but moderately myotoxic on the chick biventer cervicis preparation (BCp). We have now examined these toxic activities of a basic phospholipase A 2 , LmTX-I, isolated from the whole venom. LmTX-I caused a significant concentration–dependent neuromuscular blockade in the BCp. The time to produce 50% neuromuscular blockade was 14.7±0.75 min (30 μg/ml), 23.6±0.9 min (10 μg/ml), 34±1.7 min (2.5 μg/ml) and 39.2±3.6 min (1 μg/ml), ( n =5/concentration; p p 2 present on venom from L. m. Muta (LmTX-I) possesses a dominant neurotoxic action on isolated chick nerve-muscle preparations, whereas myotoxicity was mainly observed at the highest concentration used (30 μg/ml). These effects of LmTX-I closely reproduce the effects of the whole venom of L. m. Muta in chick neuromuscular preparations.
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biochemical and enzymatic characterization of two basic asp49 phospholipase a2 isoforms from Lachesis Muta Muta surucucu venom
Biochimica et Biophysica Acta, 2005Co-Authors: Daniela C S Damico, Gilberto De Nucci, Jose C Novello, Sergio Lilla, Luis Alberto Poncesoto, Flavia Vischi Winck, Sergio MarangoniAbstract:Abstract Two basic phospholipase A2 (PLA2) isoforms were isolated from Lachesis Muta Muta snake venom and partially characterized. The venom was fractionated by molecular exclusion chromatography in ammonium bicarbonate buffer followed by reverse-phase HPLC on a C-18 μ-Bondapack column and RP-HPLC on a C-8 column. From liquid chromatography-electrospray ionization/mass spectrometry, the molecular mass of the two isoforms LmTX-I and LmTX-II was respectively measured as 14,245.4 and 14,186.2 Da. The pI was respectively estimated to be 8.7 and 8.6 for LmTX-I and LmTX-II, as determined by two-dimensional electrophoresis. The two proteins were sequenced and differentiated from each other by a single amino acid substitution, Arg65 (LmTX-I) → Pro65 (LmTX-II). The amino acid sequence showed a high degree of homology between PLA2 isoforms from Lachesis Muta Muta and other PLA2 snake venoms. LmTX-I and LmTX-II had PLA2 activity in the presence of a synthetic substrate and showed a minimum sigmoidal behaviour; with maximal activity at pH 8.0 and 35–45 °C. Full PLA2 activity required Ca2+ and was respectively inhibited by Cu2+ and Zn2+ in the presence and absence of Ca2+. Crotapotin from Crotalus durissus cascavella rattlesnake venom significantly inhibited (P
Eladio F Sanchez - One of the best experts on this subject based on the ideXlab platform.
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sulfated galactan from palisada flagellifera inhibits toxic effects of Lachesis Muta snake venom
Marine Drugs, 2015Co-Authors: Ana Claudia Rodrigues Da Silva, Eladio F Sanchez, Luciana G Ferreira, Maria Eugenia R Duarte, Miguel D Noseda, Andre Lopes FulyAbstract:In Brazil, snakebites are a public health problem and accidents caused by Lachesis Muta have the highest mortality index. Envenomation by L. Muta is characterized by systemic (hypotension, bleeding and renal failure) and local effects (necrosis, pain and edema). The treatment to reverse the evolution of all the toxic effects is performed by injection of antivenom. However, such therapy does not effectively neutralize tissue damage or any other local effect, since in most cases victims delay seeking appropriate medical care. In this way, alternative therapies are in demand, and molecules from natural sources have been exhaustively tested. In this paper, we analyzed the inhibitory effect of a sulfated galactan obtained from the red seaweed Palisada flagellifera against some toxic activities of L. Muta venom. Incubation of sulfated galactan with venom resulted in inhibition of hemolysis, coagulation, proteolysis, edema and hemorrhage. Neutralization of hemorrhage was also observed when the galactan was administered after or before the venom injection; thus mimicking a real in vivo situation. Moreover, the galactan blocked the edema caused by a phospholipase A2 isolated from the same venom. Therefore, the galactan from P. flagellifera may represent a promising tool to treat envenomation by L. Muta as a coadjuvant for the conventional antivenom.
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inhibitory effect of plant manilkara subsericea against biological activities of Lachesis Muta snake venom
BioMed Research International, 2014Co-Authors: Eduardo Coriolano De Oliveira, Eladio F Sanchez, Caio P Fernandes, Leandro Rocha, Andre Lopes FulyAbstract:Snake venom is composed of a mixture of substances that caused in victims a variety of pathophysiological effects. Besides antivenom, literature has described plants able to inhibit injuries and lethal activities induced by snake venoms. This work describes the inhibitory potential of ethanol, hexane, ethyl acetate, or dichloromethane extracts and fractions from stem and leaves of Manilkara subsericea against in vivo (hemorrhagic and edema) and in vitro (clotting, hemolysis, and proteolysis) activities caused by Lachesis Muta venom. All the tested activities were totally or at least partially reduced by M. subsericea. However, when L. Muta venom was injected into mice 15 min first or after the materials, hemorrhage and edema were not inhibited. Thus, M. subsericea could be used as antivenom in snakebites of L. Muta. And, this work also highlights Brazilian flora as a rich source of molecules with antivenom properties.
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antivenom effects of 1 2 3 triazoles against bothrops jararaca and Lachesis Muta snakes
BioMed Research International, 2013Co-Authors: Thaisa Francielle Souza Domingos, Eladio F Sanchez, Carla Carvalho, Laura De Andrade Moura, Vinicius R Campos, Alessandro K Jordao, Anna C Cunha, Vitor F Ferreira, Maria Cecilia B V De Souza, Andre Lopes FulyAbstract:Snake venoms are complex mixtures of proteins of both enzymes and nonenzymes, which are responsible for producing several biological effects. Human envenomation by snake bites particularly those of the viperid family induces a complex pathophysiological picture characterized by spectacular changes in hemostasis and frequently hemorrhage is also seen. The present work reports the ability of six of a series of 1,2,3-triazole derivatives to inhibit some pharmacological effects caused by the venoms of Bothrops jararaca and Lachesis Muta. In vitro assays showed that these compounds were impaired in a concentration-dependent manner, the fibrinogen or plasma clotting, hemolysis, and proteolysis produced by both venoms. Moreover, these compounds inhibited biological effects in vivo as well. Mice treated with these compounds were fully protected from hemorrhagic lesions caused by such venoms. But, only the B. jararaca edema-inducing activity was neutralized by the triazoles. So the inhibitory effect of triazoles derivatives against some in vitro and in vivo biological assays of snake venoms points to promising aspects that may indicate them as molecular models to improve the production of effective antivenom or to complement antivenom neutralization, especially the local pathological effects, which are partially neutralized by antivenoms.
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inhibitory effect of a brazilian marine brown alga spatoglossum schroederi on biological activities of Lachesis Muta snake venom
Revista Brasileira De Farmacognosia-brazilian Journal of Pharmacognosy, 2012Co-Authors: Thaisa Francielle Souza Domingos, Eladio F Sanchez, Valeria Laneuville Teixeira, Fredy A Ortizramirez, Roberto Campos Villaca, Diana Negrao Cavalcanti, Andre Lopes FulyAbstract:The ability of crude extracts of the brown seaweed Spatoglossum schroederi to counteract some of the biological activities of Lachesis Muta snake venom was evaluated. In vitro assays showed that only the extract of S. schroederi prepared in ethyl acetate was able to inhibit the clotting of fibrinogen induced by L. Muta venom. On the other hand, all extracts were able to inhibit partially the hemolysis caused by venom and those prepared in dichloromethane or ethyl acetate fully neutralized the proteolysis and hemorrhage produced by the venom. Moreover, the dichloromethane or ethyl acetate extracts inhibited the hemolysis induced by an isolated phospholipase A2 from L. Muta venom, called LM-PLA2-I. In contrast, the hexane extract failed to protect mice from hemorrhage or to inhibit proteolysis and clotting. These results show that the polarity of the solvent used to prepare the extracts of S. schroederi algae influenced the potency of the inhibitory effect of the biological activities induced by L. Muta venom. Thus, the seaweed S. schroederi may be a promising source of natural inhibitors of the enzymes involved in biological activities of L. Muta venom.
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mimotopes of Mutalysin ii from Lachesis Muta snake venom induce hemorrhage inhibitory antibodies upon vaccination of rabbits
Peptides, 2011Co-Authors: R Machado A De Avila, Eladio F Sanchez, Stephanie Stransky, M Velloso, Paula Castanheira, Francisco Santos Schneider, Evanguedes Kalapothakis, Christophe Nguyen, F Molina, Claude GranierAbstract:Mutalysin-II (mut-II) from Lachesis Muta snake venom is an endopeptidase with hemorrhagic activity. A mAb against Mutalysin-II that neutralized the hemorrhagic effect was produced previously. To identify the mAb epitopes, sets of 15-mer overlapping peptides covering the mut-II amino acid sequence were synthesized using the SPOT method and tested but failed to react with the mAb. Using a phage-display approach seventeen clones reactive with mAb were identified. Additional immunoassays with the peptides and mAb identified the QCTMDQGRLRCR, TCATDQGRLRCT, HCFHDQGRVRCA, HCTMDQGRLRCR and SCMLDQGRSRCR sequences as possible epitopes. Immunization of rabbits with these peptides induced antibodies that recognize mut-II and protected against the hemorrhagic effects of Lachesis venom.
