| fractionation of bothrops pirajai snake venom: isolation and characterization of piratoxin-i, a new myotoxic protein. | whole desiccated venom of bothrops pirajai was fractionated on a gel filtration (sephadex g-75) column. phospholipase a2, arginine esterase and clotting activity profiles of the six fractions (si to svi) obtained were determined. fraction siv from the gel filtration column was subjected to chromatography on sp-sephadex c-25. it was resolved into five subfractions (siv-sp1, to siv-sp5). fractions siv-sp1, siv-sp2 and siv-sp3 showed phospholipase a2 activity but, among these fractions, only siv-sp ... | 1995 | 7660366 |
| inhibition of proteases, myotoxins and phospholipases a2 from bothrops venoms by the heteromeric protein complex of didelphis albiventris opossum serum. | the antibothropic complex (abc) from opossum (species didelphis albiventris) serum was purified by chromatography on deae-sephacel. it showed an acidic character and two polypeptide chains of ca. 45 kda and 48 kda, respectively. lyophilized opossum serum or the abc (100 micrograms), as well as ethylenediamine tetraacetate (0.25 mumoles) were able to completely neutralise the hemorrhagic effect of 50 micrograms of the desiccated venoms of bothrops moojeni, bothrops pirajai and bothrops jararacuss ... | 1997 | 9415818 |
| amino acid sequence of piratoxin-i, a myotoxin from bothrops pirajai snake venom, and its biological activity after alkylation with p-bromophenacyl bromide. | the complete sequence of the 121 amino acid residues of piratoxin-i (prtx-i), a phospholipase a2 (pla2)-like myotoxin from bothrops pirajai snake (bahia jararacussu) venom, is reported. from the sequence, an m, of 13,825 and an approximate pi of 8.3 were calculated. prtx-i shows a high sequence homology with lys-49 myotoxins from other bothropic (approximately 95%) and nonbothropic (approximately 80%) venoms, but only 70-75% homology when aligned with the catalytically active asp-49 pla2s. when ... | 1998 | 9853687 |
| effects of bothrops pirajai venom on the mouse extensor digitorum longus (edl) muscle preparation. | the effects of bothrops pirajai snake venom on the mouse extensor digitorum longus (edl) preparation were examined using myographic, histopathological and biochemical approaches. b. pirajai venom (10, 25 or 50 microg/ml) dose dependently and irreversibly blocked the contractile response of indirectly stimulated edl muscle. histopathological analysis of edl muscle incubated with venom showed dose-dependent damage with a loss of the normal tissue structure and the appearance of highly dark, edemat ... | 1999 | 10400298 |
| inflammatory oedema induced by the lys-49 phospholipase a(2) homologue piratoxin-i in the rat and rabbit. effect of polyanions and p-bromophenacyl bromide. | piratoxin-i (prtx-i) is a lys-49 phospholipase (pla(2)) homologue, isolated from bothrops pirajai snake venom, that has no phospholipase activity. in this study, we investigated the in vivo oedematogenic activity of prtx-i in both the rat and the rabbit as well as the ability of prtx-i to activate rat mast cells in vitro. in the rat paw and skin, prtx-i (3-100 microg/paw) induced a dose-dependent oedema that was associated with extensive mast cell degranulation. the involvement of mast cells in ... | 2000 | 10736429 |
| leucocyte recruitment induced by type ii phospholipases a(2) into the rat pleural cavity. | bothropstoxin-i (bthtx-i) and bothropstoxin-ii (bthtx-ii) are lys-49 and asp-49 phospholipases a(2) (pla(2)s), respectively, isolated from bothrops jararacussu venom. piratoxin-i (prtx-i) is a lys-49 pla(2) isolated from bothrops pirajai venom. in this study, the ability of bthtx-i, bthtx-ii and prtx-i to recruit leucocytes into the rat pleural cavity and potential mechanisms underlying this effect were investigated. intrapleural injection of either bthtx-i or prtx-i (10-100 microg/cavity each) ... | 2000 | 10858516 |
| dissociation of enzymatic and pharmacological properties of piratoxins-i and -iii, two myotoxic phospholipases a2 from bothrops pirajai snake venom. | piratoxins (prtx) i and iii are phospholipases a2 (pla2s) or pla2 homologue myotoxins isolated from bothrops pirajai snake venom, which also induce myonecrosis, bactericidal activity against escherichia coli, disruption of artificial membranes, and edema. prtx-iii is a catalytically active hemolytic and anticoagulant asp49 pla2, while prtx-i is a lys49 pla2 homologue, which is catalytically inactive on artificial substrates, but promotes blockade of neuromuscular transmission. chemical modificat ... | 2001 | 11370840 |
| structural and functional analysis of bmjmip, a phospholipase a2 myotoxin inhibitor protein from bothrops moojeni snake plasma. | a protein, which neutralizes the enzymatic, toxic, and pharmacological activities of various basic and acidic phospholipases a(2) from the venoms of bothrops moojeni, bothrops pirajai, and bothrops jararacussu, was isolated from b. moojeni snake plasma by affinity chromatography using immobilized myotoxins on sepharose gel. biochemical characterization of this myotoxin inhibitor protein (bmjmip) showed it to be an oligomeric glycoprotein with a m(r) of 23,000-25,000 for the monomeric subunit. bm ... | 2003 | 12604331 |
| spectroscopic analysis of the stability of bothrops myotoxic phospholipases a2 to guanidine and urea denaturation. | spectrophotometric profiles representing the unfolding induced by guanidine on bothrops moojeni myotoxins-i (mjtx-i) and ii (mjtx-ii), bothrops jararacussu bothropstoxin-i (bthtx-i) and bothrops pirajai piratoxin-i (prtx-i) were obtained and compared with those obtained with bovine ribonuclease a (rnase) and trypsin. the molar (epsilon(1m)) and percent (epsilon(1%)) extinction coefficients were determined for the four myotoxins as well as for rnase and trypsin as reference parameters. these coef ... | 2003 | 12625831 |
| a new c-type animal lectin isolated from bothrops pirajai is responsible for the snake venom major effects in the isolated kidney. | we investigated the biochemical and biological effects of a new c-type galactoside specific lectin termed bpl that was isolated from the snake venom of bothrops pirajai. this lectin was purified using size exclusion hplc followed by an immobilized lactose affinity column. the purified bpl was homogeneous by reverse phase hplc and sds-page. we evaluated the nephrotoxicity of the whole venom of b. pirajai and its lectin. the whole venom of b. pirajai (10 microg/ml) showed similar results as those ... | 2005 | 15381156 |
| biochemical and functional characterization of an l-amino acid oxidase isolated from bothrops pirajai snake venom. | in this work we describe the isolation of a new l-amino acid oxidase (laao) referred to as bpirlaao-i from bothrops pirajai snake venom, which was highly purified using a combination of molecular exclusion, affinity, and hydrophobic chromatography steps. bpirlaao-i homodimeric acid glycoprotein (approximate mr and pi of 130,000 and 4.9, respectively) displays high specificity toward hydrophobic/aromatic amino acids, while deglycosylation does not alter its enzymatic activity. the n-terminal laao ... | 2006 | 16809041 |
| crystal structure of piratoxin-i: a calcium-independent, myotoxic phospholipase a2-homologue from bothrops pirajai venom. | the crystal structure of piratoxin-i (prtx-i) a lys49 homologue isolated from the venom of bothrops pirajai has been determined and refined at 2.8 a to a crystallographic residual of 19.7% (rfree = 29.7%). amino-acid sequence differences between catalytically active phospholipases and prtx-i in the putative ca2+-binding loop, specifically the substitutions tyr28 --> asn, gly32 --> leu and asp49 --> lys, result in an altered conformation of this loop. the analysis of the position of the epsilon-a ... | 1998 | 9723838 |
| inhibition of neurotoxic secretory phospholipases a(2) enzymatic, edematogenic, and myotoxic activities by harpalycin 2, an isoflavone isolated from harpalyce brasiliana benth. | secretory phospholipases a(2) (spla(2)) exert proinflammatory actions through lipid mediators. these enzymes have been found to be elevated in many inflammatory disorders such as rheumatoid arthritis, sepsis, and atherosclerosis. the aim of this study was to evaluate the effect of harpalycin 2 (har2), an isoflavone isolated from harpalyce brasiliana benth., in the enzymatic, edematogenic, and myotoxic activities of spla(2) from bothrops pirajai, crotalus durissus terrificus, apis mellifera, and ... | 2012 | 22899963 |
| biochemical characterization and comparative analysis of two distinct serine proteases from bothrops pirajai snake venom. | this study reports the isolation and biochemical characterization of two different serine proteases from bothrops pirajai snake venom, thus providing a comparative analysis of the enzymes. the isolation process consisted of three consecutive chromatographic steps (sephacryl s-200, benzamidine sepharose and c2/c18), resulting in two serine proteases, named bpirsp27 and bpirsp41 after their molecular masses by mass spectrometry (27,121 and 40,639 da, respectively). estimation by sds-page under den ... | 2012 | 22819993 |
| inhibition of enzymatic and pharmacological activities of some snake venoms and toxins by mandevilla velutina (apocynaceae) aqueous extract. | phospholipases a(2) (pla(2)) are multifunctional proteins which exhibit varied biological activities correlated to the structural diversities of the sub-classes. the crude aqueous extract from subterranean system of mandevilla velutina, a plant found in brazilian savanna, was assayed for its ability to inhibit biological activities of several snake venoms and isolated pla(2)s. the extract induced total inhibition of the phospholipase activity of crotalus durissus terrificus venom and only partia ... | 2003 | 14644557 |
| evaluation of the local inflammatory events induced by bpirmp, a metalloproteinase from bothrops pirajai venom. | in this study, we evaluated the edema and hyperalgesic response induced by bpirmp, a p-i class metalloproteinase isolated from bothrops pirajai snake venom. the animals were injected with the metalloproteinase or sterile pbs (control group) and evaluated for 1, 2, 3, 4, 5, 6 and 24h. the intraplantar injection of bpirmp (5-50μg/paw) induced a dose- and time-dependent response. bpirmp (50μg) induced paw edema in rats rapidly, with peak response two hours after injection of the toxin. also, bpirmp ... | 2015 | 26468034 |
| bothrops snake venoms and their isolated toxins, an l-amino acid oxidase and a serine protease, modulate human complement system pathways. | activation of the complement system plays an important role in the regulation of immune and inflammatory reactions, and contributes to inflammatory responses triggered by envenomation provoked by bothrops snakes. the present study aimed to assess whether bothrops jararacussu and bothrops pirajai crude venoms and their isolated toxins, namely serine protease (bjussusp-i) and l-amino acid oxidase (bpirlaao-i), modulate human complement system pathways. | 2015 | 26273289 |
| isolation and biochemical characterization of a new thrombin-like serine protease from bothrops pirajai snake venom. | this paper presents a novel serine protease (sp) isolated from bothrops pirajai, a venomous snake found solely in brazil that belongs to the viperidae family. the identified sp, named bpirsp-39, was isolated by three chromatographic steps (size exclusion, bioaffinity, and reverse phase chromatographies). the molecular mass of bpirsp-39 was estimated by sds-page and confirmed by mass spectrometry (39,408.32 da). the protein was able to form fibrin networks, which was not observed in the presence ... | 2014 | 24719874 |
| l-amino acid oxidase isolated from bothrops pirajai induces apoptosis in bcr-abl-positive cells and potentiates imatinib mesylate effect. | chronic myeloid leukaemia (cml) is a myeloproliferative disorder characterized by the presence of philadelphia chromosome and by bcr-abl1, which encodes the bcr-abl oncoprotein. although imatinib mesylate (im) is effective for cml treatment, patients in accelerated and blastic phases of the disease are often refractory to this therapy, and there are also cases of im resistance in patients in the chronic phase. therefore, potential new drugs are being investigated to improve the efficiency of the ... | 2013 | 23551499 |
| effects of two serine proteases from bothrops pirajai snake venom on the complement system and the inflammatory response. | the present study aimed to evaluate the effects of two serine proteases from bothrops pirajai snake venom, named bpirsp27 and bpirsp41, on the complement system and the inflammatory response. the effects of these enzymes on the human complement system were assessed by kinetic hemolytic assays, evaluating the hemolysis promoted by the classical/lectin (cp/lp) and alternative (ap) pathways after incubation of normal human serum with the serine proteases. the results suggested that these enzymes we ... | 2013 | 23499645 |
| proteomic analysis of bothrops pirajai snake venom and characterization of bpirmp, a new p-i metalloproteinase. | bothrops pirajai snake venom was analyzed by a proteomic strategy. proteins were separated by rp-hplc, followed by sds-page, in-gel tryptic digestion, identification by maldi-tof/tof mass spectrometry, and assignment to known protein families by similarity. proteins belonging to six families were found in b. pirajai venom, including abundant pla2s and metalloproteinases, with the remaining proteins distributed among l-amino acid oxidase, serine proteinase, disintegrin and lectin-like families. a ... | 2013 | 23385358 |
| molecular characterization of an acidic phospholipase a(2) from bothrops pirajai snake venom: synthetic c-terminal peptide identifies its antiplatelet region. | this paper describes a biochemical and pharmacological characterization of bpirpla(2)-i, the first acidic asp49-pla(2) isolated from bothrops pirajai. bpirpla(2)-i caused hypotension in vivo, presented phospholipolytic activity upon artificial substrates and inhibitory effects on platelet aggregation in vitro. moreover, a synthetic peptide of bpirpla(2)-i, comprising residues of the c-terminal region, reproduced the antiplatelet activity of the intact protein. a cdna fragment of 366 bp encompass ... | 2011 | 21331602 |
| crystallization and preliminary x-ray diffraction studies of piratoxin iii, a d-49 phospholipase a2 from the venom of bothrops pirajai. | piratoxin iii (prtx-iii) is a phospholipase a2 (pla2, e.c. 3.1.1.4, phosphatide sn-2 acylhydrolase) isolated from bothrops pirajai. crystals of prtx-iii were obtained using the vapour-diffusion technique and x-ray diffraction data have been collected to 2.7 a resolution. the enzyme was crystallized in the space group c2 with unit-cell parameters a = 60.88, b = 100.75, c = 48.19 a, beta = 123. 89 degrees. a molecular-replacement solution of the structure has been found using bothropstoxin i from ... | 1999 | 10329793 |
| crystallization of piratoxin i, a myotoxic lys49-phospholipase a2 homologue isolated from the venom of bothrops pirajai. | large single crystals of piratoxin i. a lys49-pla2 homologue with low enzymatic activity, have been obtained. the crystals belong to the orthorhombic system space group p2(1)2(1)2(1), and diffract x-rays to a resolution of 2.8 a. preliminary analysis reveals the presence of two molecules in the crystallographic asymmetric unit. | 1998 | 9637374 |
| neutralization of proteases from bothrops snake venoms by the aqueous extract from casearia sylvestris (flacourtiaceae). | aqueous extract from casearia sylvestris leaves, a typical plant from brazilian open pastures, was able to neutralize the hemorrhagic activity caused by bothrops asper, bothrops jararacussu, bothrops moojeni, bothrops neuwiedi and bothrops pirajai venoms. it also neutralized two hemorrhagic metalloproteinases from bothrops asper venom. proteolytic activity on casein induced by bothropic venoms and by isolated proteases, including bn2 metalloproteinase from b. neuwiedi venom, was also inhibited b ... | 2001 | 11600149 |
| crystallization and preliminary x-ray diffraction studies of piratoxin ii, a phospholipase a2 isolated from the venom of bothrops pirajai. | the phospholipases a2 (pla2, e.c. 3.1.1.4, phosphatide sn2 acylhydrolases) are the major components of the venom of several snakes. they are responsible for several important pharmacological effects observed in ophidian incidents. pla2 piratoxin ii from bothrops pirajai has been crystallized by the vapour-diffusion technique. x-ray diffraction data have been collected to 2.04 a resolution (90.2% complete, rmerge = 0.070). the space group is p21 and the cell parameters are a = 46.19, b = 60.36, c ... | 1998 | 10089531 |
| amino acid sequence of piratoxin-ii, a myotoxic lys49 phospholipase a(2) homologue from bothrops pirajai venom. | the complete amino acid sequence of the 121 amino acid residues of piratoxin ii, a phospholipase a(2) like myotoxin from bothrops pirajai venom, is reported. prtx-ii is a basic protein with a molecular mass of 13740 da, a calculated pi of 9.03, but an experimental pi of 8.4 +/- 0.2, showing sequence similarity with other bothropic (90-99%) or non-bothropic ( approximately 80%) lys49 pla(2)-like myotoxins. this similarity falls to approximately 70% when this sequence is aligned with that of asp49 ... | 2000 | 10863008 |
| purification and amino acid sequence of mp-iii 4r d49 phospholipase a2 from bothrops pirajai snake venom, a toxin with moderate pla2 and anticoagulant activities and high myotoxic activity. | mp-iii 4r pla2 was purified from the venom of bothrops pirajai venom (bahia's jararacussu) after three chromatographic steps which started with rp-hplc. the complete amino acid sequence of mp-iii 4r pla2 from bothrops pirajai was determined by amino acid sequencing of reduced and carboxymethylated mp-iii 4r and the isolated peptides from clostripain and protease v8 digestion. mp-iii 4r is a d49 pla2 with 121 amino acid residues and has a molecular weight estimated at 13,800 da, with 14 half-cyst ... | 1999 | 10395455 |
| a quick procedure for the isolation of dimeric piratoxins-i and ii, two myotoxins from bothrops pirajai snake venom. n-terminal sequencing. | two myotoxins, mp-i and mp-ii, from bothrops pirajai snake venom, have been purified by a quick high performance liquid chromatography (hplc) procedure. based on the hplc coelution profile, amino acid composition, n-terminal sequence, polyacrylamide gel electrophoresis (page) migration, as well as lack of phospholipase-a2 (pla2) and proteolytic activities, mp-i and mp-ii were identified as piratoxin-i (prtx-i) and ii (prtx-ii), respectively. this procedure affords, aside the reduced operation ti ... | 1995 | 8747534 |
| in silico molecular studies of antiophidic properties of the amazonian tree cordia nodosa lam. | we carried out surveys on the use of cordia nodosa lam. in the jungles of bobonaza (ecuador). we documented this knowledge to prevent its loss under the framework of the convention on biological diversity and the nagoya protocol. we conducted bibliographic research and identified quercetrin as a significant bioactive molecule. we studied its in silico biological activity. the selected methodology was virtual docking experiments with the proteins responsible for the venomous action of snakes. the ... | 2019 | 31744153 |
| corrigendum: complement system inhibition modulates the pro-inflammatory effects of a snake venom metalloproteinase. | [this corrects the article doi: 10.3389/fimmu.2019.01137.]. | 2020 | 31333670 |
| complement system inhibition modulates the pro-inflammatory effects of a snake venom metalloproteinase. | envenomation by bothrops snakes causes prominent local effects, including pain, oedema, local bleeding, blistering and necrosis, and systemic manifestations, such as hemorrhage, hypotension, shock and acute renal failure. these snake venoms are able to activate the complement system and induce the generation of anaphylatoxins, whose mechanisms include the direct cleavage of complement components by snake venom metalloproteinases and serine proteinases present in the venoms. a metalloproteinase a ... | 2019 | 31231362 |
| p-i snake venom metalloproteinase is able to activate the complement system by direct cleavage of central components of the cascade. | snake venom metalloproteinases (svmps) are amongst the key enzymes that contribute to the high toxicity of snake venom. we have recently shown that snake venoms from the bothrops genus activate the complement system (c) by promoting direct cleavage of c-components and generating anaphylatoxins, thereby contributing to the pathology and spread of the venom. the aim of the present study was to isolate and characterize the c-activating protease from bothrops pirajai venom. | 2013 | 24205428 |
| harpalycin 2 inhibits the enzymatic and platelet aggregation activities of prtx-iii, a d49 phospholipase a2 from bothrops pirajai venom. | harpalycin 2 (hp-2) is an isoflavone isolated from the leaves of harpalyce brasiliana benth., a snakeroot found in northeast region of brazil and used in folk medicine to treat snakebite. its leaves are said to be anti-inflammatory. secretory phospholipases a2 are important toxins found in snake venom and are structurally related to those found in inflammatory conditions in mammals, as in arthritis and atherosclerosis, and for this reason can be valuable tools for searching new anti-phospholipas ... | 2012 | 22925825 |
| crystallization and preliminary x-ray diffraction analysis of a lys49-phospholipase a2 complexed with caffeic acid, a molecule with inhibitory properties against snake venoms. | phospholipases a(2) (pla(2)s) are one of the main components of bothropic venoms; in addition to their phospholipid hydrolysis action, they are involved in a wide spectrum of pharmacological activities, including neurotoxicity, myotoxicity and cardiotoxicity. caffeic acid is an inhibitor that is present in several plants and is employed for the treatment of ophidian envenomations in the folk medicine of many developing countries; as bothropic snake bites are not efficiently neutralized by conven ... | 2011 | 21301098 |
| crystallization and preliminary x-ray crystallographic studies of a lys49-phospholipase a2 homologue from bothrops pirajai venom complexed with rosmarinic acid. | prtx-i, a noncatalytic and myotoxic lys49-phospholipase a(2) from bothrops pirajai venom, was crystallized in the presence of the inhibitor rosmarinic acid (ra). this is the active compound in the methanolic extract of cordia verbenacea, a plant that is largely used in brazilian folk medicine. the crystals diffracted x-rays to 1.8 a resolution and the structure was solved by molecular-replacement techniques, showing electron density that corresponds to ra molecules at the entrance to the hydroph ... | 2010 | 20516603 |
| preliminary x-ray crystallographic studies of a lys49-phospholipase a2 homologue from bothrops pirajai venom complexed with p-bromo-phenacyl bromide and alpha-tocopherol inhibitors. | prtx-i, a non-catalytic and myotoxic lys49-pla(2) from bothrops pirajai venom has been crystallized alone and in complex with bromophenacyl bromide (bpb), alpha tocopherol and alpha tocopherol acetate inhibitors. these crystals have shown to diffract x-rays between 2.34 and 1.65 a resolution. all complexes crystals are isomorphous and belong to the space group p2(1) whereas native prtx-i crystals belong to the p3(1)21. | 2007 | 17897096 |
| the structure of the d49 phospholipase a2 piratoxin iii from bothrops pirajai reveals unprecedented structural displacement of the calcium-binding loop: possiblerelationship to cooperative substrate binding. | snake venoms are rich sources of phospholipase a(2) homologues, both active calcium-binding asp49 enzymes and essentially inactive lys49 proteins. they are responsible for multiple pharmacological effects, some of which are dependent on catalytic activity and others of which are not. here, the 2.4 a x-ray crystal structure of an active asp49 phospholipase a(2) from the venom of the snake bothrops pirajai, refined to conventional and free r values of 20.1 and 25.5%, respectively, is reported. unu ... | 2003 | 12554936 |