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Byambas Patrick - One of the best experts on this subject based on the ideXlab platform.

  • Vermiculture et volailles : Synthèse bibliographique sur les risques toxiques et les intoxinations liées à l’utilisation de vers de terre dans l’alimentation des volailles.
    2019
    Co-Authors: Byambas Patrick
    Abstract:

    Earthworms are part of natural diet of some farm animals such as poultry. They are a protein source. Unfortunately, earthworms can accumulate some toxic substances occurring in the soil and animals can be contaminated through feed containing these earthworms. The biological and nonbiological risks related to earthworms depend on the type of substrates through which they live. Earthworms are usually contaminated in polluted soil by various types of toxic and poisonous substance. The most common toxic compounds are heavy metals, pesticides and Microbial Toxins, which can lead to toxic or poisonous contamination of earthworms and then animals, such as poultry, fish and swine, through feeding. This risk cannot be identified in earthworm body without its destruction. But according to toxic substance targeted, there are many ways of risks detection, in soil, earthworms and animals. To protect farm animals, different technics are available. To limit heavy metal contamination, soil should be analyzed before collecting earthworms. Many treatments are available. By heating at 80°C for 2–4 h, microorganisms can be destroyed. Nevertheless, this technique needs to be adapted with certain types of bacteria whose enterotoxin withstands temperatures of 100°C for 30 min, or more. To limit all these risks, the use of earthworms reared from vermiculture can help to prevent contamination of poultry through feeding.Peer reviewe

  • Vermiculture et volailles : Synthèse bibliographique sur les risques toxiques et les intoxinations liées à l’utilisation de vers de terre dans l’alimentation des volailles.
    'Informa UK Limited', 2019
    Co-Authors: Byambas Patrick
    Abstract:

    peer reviewedaudience: researcher, professional, studentEarthworms are part of natural diet of some farm animals such as poultry. They are a protein source. Unfortunately, earthworms can accumulate some toxic substances occurring in the soil and animals can be contaminated through feed containing these earthworms. The biological and nonbiological risks related to earthworms depend on the type of substrates through which they live. Earthworms are usually contaminated in polluted soil by various types of toxic and poisonous substance. The most common toxic compounds are heavy metals, pesticides and Microbial Toxins, which can lead to toxic or poisonous contamination of earthworms and then animals, such as poultry, fish and swine, through feeding. This risk cannot be identified in earthworm body without its destruction. But according to toxic substance targeted, there are many ways of risks detection, in soil, earthworms and animals. To protect farm animals, different technics are available. To limit heavy metal contamination, soil should be analyzed before collecting earthworms. Many treatments are available. By heating at 80°C for 2–4 h, microorganisms can be destroyed. Nevertheless, this technique needs to be adapted with certain types of bacteria whose enterotoxin withstands temperatures of 100°C for 30 min, or more. To limit all these risks, the use of earthworms reared from vermiculture can help to prevent contamination of poultry through feeding

Victor Nizet - One of the best experts on this subject based on the ideXlab platform.

  • innate immunity gone awry linking Microbial infections to chronic inflammation and cancer
    Cell, 2006
    Co-Authors: Michael Karin, Toby Lawrence, Victor Nizet
    Abstract:

    Clinical and epidemiologic studies have suggested an association between infectious agents and chronic inflammatory disorders and cancer. Better understanding of Microbial pattern-recognition receptors and innate immune signaling pathways of the host is helping to elucidate the connection between Microbial infection and chronic disease. We propose that a key aspect of pathogenesis is an aberrant epithelial barrier that can be instigated by Microbial Toxins, environmental insults, or the genetic predisposition of the host. Loss of epithelial integrity results in activation of resident inflammatory cells by Microbial invaders or endogenous ligands. When coupled with a failure of normal control mechanisms that limit leukocyte activation, a cascade is established that induces chronic inflammation and its consequences. Here, we outline this mechanistic framework and briefly review how alteration of innate immune response genes in murine models can provide insights into the potential Microbial origins of diverse conditions including Crohn's disease, psoriasis, atherosclerosis, diabetes, and liver cancer.

  • genetic locus for streptolysin s production by group a streptococcus
    Infection and Immunity, 2000
    Co-Authors: Victor Nizet, Vivekananda Datta, Darrin J Bast, Bernard Beall, Laurie Kilburn, Donald E Low, Joyce C S De Azavedo
    Abstract:

    Group A streptococcus (GAS) is an important human pathogen that causes pharyngitis and invasive infections, including necrotizing fasciitis. Streptolysin S (SLS) is the cytolytic factor that creates the zone of betahemolysis surrounding GAS colonies grown on blood agar. We recently reported the discovery of a potential genetic determinant involved in SLS production, sagA, encoding a small peptide of 53 amino acids (S. D. Betschel, S. M. Borgia, N. L. Barg, D. E. Low, and J. C. De Azavedo, Infect. Immun. 66:1671‐1679, 1998). Using transposon mutagenesis, chromosomal walking steps, and data from the GAS genome sequencing project (www .genome.ou.edu/strep.html), we have now identified a contiguous nine-gene locus (sagA to sagI) involved in SLS production. The sag locus is conserved among GAS strains regardless of M protein type. Targeted plasmid integrational mutagenesis of each gene in the sag operon resulted in an SLS-negative phenotype. Targeted integrations (i) upstream of the sagA promoter and (ii) downstream of a terminator sequence after sagI did not affect SLS production, establishing the functional boundaries of the operon. A rho-independent terminator sequence between sagA and sagB appears to regulate the amount of sagA transcript produced versus transcript for the entire operon. Reintroduction of the nine-gene sag locus on a plasmid vector restored SLS activity to the nonhemolytic sagA knockout mutant. Finally, heterologous expression of the intact sag operon conferred the SLS beta-hemolytic phenotype to the nonhemolytic Lactococcus lactis. We conclude that gene products of the GAS sag operon are both necessary and sufficient for SLS production. Sequence homologies of sag operon gene products suggest that SLS is related to the bacteriocin family of Microbial Toxins. Group A streptococcus (GAS), specifically Streptococcus pyogenes, is a common cause of pharyngitis, impetigo, and many

Mohamed Abdo - One of the best experts on this subject based on the ideXlab platform.

  • Probiotics and plant-derived compounds as eco-friendly agents to inhibit Microbial Toxins in poultry feed: a comprehensive review
    Environmental Science and Pollution Research, 2018
    Co-Authors: Mohamed E. Abd El-hack, Dalia H. Samak, Ahmed E. Noreldin, Karima El-naggar, Mohamed Abdo
    Abstract:

    Some of pathogenic bacteria and fungi have the ability to produce fetal Toxins which may be the direct causes of cytotoxicity or cellular dysfunction in the colonization site. Biological and non-biological environmental factors, challenge and microbes influence the effect of Toxins on these pathogens. Modern research mentions that many natural materials can reduce the production of Toxins in pathogenic microbes. However, researches that explain the mechanical theories of their effects are meager. This review aimed to discuss the ameliorative potential role of plant-derived compounds and probiotics to reduce the toxin production of food-borne microbes either in poultry bodies or poultry feedstuff. Moreover, studies that highlight their own toxicological mechanisms have been discussed. Adding natural additives to feed has a clear positive effect on the enzymatic and microbiological appearance of the small intestine without any adverse effect on the liver. Studies in this respect were proposed to clarify the effects of these natural additives for feed. In conclusion, it could be suggested that the incorporation of probiotics, herbal extracts, and herbs in the poultry diets has some beneficial effects on productive performance, without a positive impact on economic efficiency. In addition, the use of these natural additives in feed has a useful impact on the microbiological appearance of the small intestine and do not have any adverse impacts on intestinal absorption or liver activity as evidenced by histological examination.

Rodrigues-simioni L. - One of the best experts on this subject based on the ideXlab platform.

  • Structural And Functional Properties Of Batx, A New Lys49 Phospholipase A2 Homologue Isolated From The Venom Of The Snake Bothrops Alternatus
    2015
    Co-Authors: Ponce-soto L.a., Rodrigues-simioni L., Lomonte B, Novello J.c., Gutierrez J.m., Marangoni S.
    Abstract:

    BaTX PLA2, a K49 phospholipase A2 homologue was purified from Bothrops alternatus venom after two chromatographic steps, molecular exclusion on Superdex 75 and reverse phase HPLC on μ-Bondapack C-18. A molecular mass of 13898.71 Da was determined by MALDI-TOF mass spectrometry. The amino acid composition showed that BaTX has a high content of Lys, Tyr, Gly, Pro, and 14 half-Cys residues, typical of a basic PLA2. The complete amino acid sequence of BaTX PLA2 contains 121 residues, resulting in a calculated pI value of 8.63. This sequence shows high identity values when compared to other K49 PLA2s isolated from the venoms of viperid snakes. Lower identity is observed in comparison to D49 PLA2s. The sequence was SLFELGKMIL QETGKNPAKS YGAYYCYCGW GGQGQPKDAT DRCCYVHKCC YKKLTGCNPK KDRYSYSWKD KTIVCGENNS CLKELCECDK AVAICLRENL NTYNKKYRYY LKPLCKKADA C. In mice, BaTX induced myonecrosis and edema, upon intramuscular or subcutaneous injections, respectively. The LD50 of BaTX was 7 μg/g body weight, by intravenous route. In vitro, the toxin caused a potent blockade of neuromuscular transmission in young chicken biventer cervicis preparations. The blockage 50% was achieved at a concentration of 0.03 μM: 40 ± 0.4 min and 0.07 μM: 35 ± 0.3 min. Moreover, this protein induced a rapid cytolytic effect upon mouse skeletal muscle myoblasts in culture. Thus, the combined structural and functional information obtained identify BaTX as a new member of the K49 PLA2 family, which presents the typical bioactivities described for such proteins. © 2006 Elsevier B.V. All rights reserved.17704585593Six, D.A., Dennis, E.A., The expanding superfamily of phospholipase A2 enzymes: classification and characterization (2000) Biochim. Biophys. Acta, 1488, pp. 1-19Kini, R.M., (1997) Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism, pp. 1-511. , Wiley, Chichester, EnglandKini, R.M., Chan, Y.M., Accelerated evolution and molecular surface of venom phospholipase A2 enzymes (1999) J. Mol. Evol., 48 (2), pp. 125-132Kordis, D., Gubensek, F., Bov-B long interspersed repeated DNA (LINE) sequences are present in Vipera ammodytes phospholipase A2 genes and in genomes of Viperidae snakes (1997) Eur. J. Biochem., 246 (3), pp. 772-779Kini, R.M., Excitement ahead: structure, function and mechanism of snake venom phospholipase A2 enzymes (2003) Toxicon, 42, pp. 827-840Gutiérrez, J.M., Ownby, C.L., Skeletal muscle degeneration induced by venom phospholipases A2: insights into the mechanisms of local and systemic myotoxicity (2003) Toxicon, 42, pp. 915-931Lomonte, B., Angulo, Y., Calderón, L., An overview of Lysine-49 phospholipase A2 myoToxins from crotalid snake venoms and their structural determinants of myotoxic action (2003) Toxicon, 42, pp. 885-901de Roodt, A.R., García, S.I., Salomon, O.D., Segre, L., Dolab, J.A., Funes, R.F., de Titto, E.H., Hemorrhagic activity of Bothrops venoms determined by two different methods and relationship with proteolytic activity on gelatin and lethality (2003) Toxicon, 41 (8), pp. 949-958Valerio, A.A., Corradini, A.C., Panunto, P.C., Mello, S.M., Hyslop, S., Purification and characterization of a phosphodiesterase from Bothrops alternatus snake venom (2002) J. Protein Chem., 21 (8), pp. 95-503Smolka, M.B., Marangoni, S., Oliveira, B., Novello, J.C., Purification and partial characterization of a thrombin-like enzyme, balterobin, from the venom of Bothrops alternatus (1998) Toxicon, 36, pp. 1059-1063Castro, H.C., Dutra, L.S., Oliveira-Carvalho, A.L., Zingali, R.B., Bothroalternin, a thrombin inhibitor from the venom of Bothrops alternatus (1998) Toxicon, 36 (12), pp. 1903-1912Acosta de Pérez, O., Koscinczuk, P., Negrette, M.S., Teibler, P., Ruiz, R., Effects of Bothrops alternatus venom from Argentina on muscle and different organs in mice (1996) Acta Physiol. Pharmacol. Ther. Latinoam., 46, pp. 97-102. , (Spanish)Cho, W., Kezdy, F.J., Chromogenic substrates and assay of phospholipases A2 (1991) Methods Enzymol., 197, pp. 75-79Holzer, M., Mackessy, S.P., An aqueous endpoint assay of snake venom phospholipase A2 (1996) Toxicon, 34, pp. 1149-1155Ponce-Soto, L.A., Toyama, M.H., Hyslop, S., Novello, J.C., Marangoni, S., Isolation and preliminary enzymatic characterization of a novel PLA2 from Crotalus durissus collilineatus venom (2002) J. Protein Chem., 21 (3), pp. 131-136Schägger, H., von Jagow, G., Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa (1987) Anal. Biochem., 166 (2), pp. 368-379Smolka, M.B., Zhou, H., Purkayastha, S., Aebersold, R., Optimization of the isotope-coded affinity tag-labeling procedure for quantitative proteome analysis (2001) Anal. Biochem., 297, pp. 25-31Heinrikson, R.L., Meredith, S.C., Amino acid analysis by reverse-phase high-performance liquid chromatography: precolumn derivatization with phenylisothiocyanate (1984) Anal. Biochem., 136 (1), pp. 65-74Toyama, M.H., Soares, A.M., Wen-Hwa, L., Polikarpov, I., Giglio, J.R., Marangoni, S., Amino acid sequence of piratoxin-II, a myotoxic lys49 phospholipase A2 homologue from Bothrops pirajai venom (2000) Biochimie, 82, pp. 245-250Yamakawa, M., Nozaki, M., Hokama, Z., Fractionation of Sakishima-habu (Trimeresurus elegans) venom, and lethal, hemorrhagic, and edema-forming activities of the fractions (1976) Animal, Plant and Microbial Toxins, pp. 97-109. , Ohsaka A., Hayashi K., and Sawai Y. (Eds), Plenum Press, New YorkGutiérrez, J.M., Lomonte, B., Chaves, F., Moreno, E., Cerdas, L., Pharmacological activities of a toxic phospholipase A isolated from the venom of the snake Bothrops asper (1986) Comp. Biochem. Physiol., 84 C, pp. 159-164World Health Organization, Progress in the characterization of venoms and standardization of antivenoms (1981) WHO Offset Publication, 58. , GenevaGinsborg, B.L., Warriner, J., The isolated chick biventer cervicis nerve-muscle preparation (1960) Br. J. Pharmacol. Chemother., 15, pp. 410-4111Lomonte, B., Angulo, Y., Rufini, S., Cho, W., Giglio, J.R., Ohno, M., Daniele, J.J., Gutiérrez, J.M., Comparative study of the cytolytic activity of myotoxic phospholipases A2 on mouse endothelial (tEnd) and skeletal muscle (C2C12) cells in vitro (1999) Toxicon, 37, pp. 145-158Valentin, E., Lambeau, G., What can venom phospholipases A2 tell us about the functional diversity of mammalian secreted phospholipases A2 (2000) Biochimie, 82, pp. 815-831Nisenbom, H.E., Perazzo, J.C., Monserrat, A.J., Vidal, J.C., Contribution of phospholipase A2 to the lethal potency of Bothrops alternatus (víbora de la cruz) venom (1986) Toxicon, 24, pp. 807-817Nisenbom, H.E., Seki, C., Vidal, J.C., Phospholipase A2 from Bothrops alternatus (víbora de la cruz) venom. Purification and some characteristic properties (1986) Toxicon, 24 (3), pp. 259-272Nisenbom, H.E., Perazzo, J.C., Monserrat, A.J., Vidal, J.C., Effect of chemical modification with p-bromophenacyl bromide on the enzymatic and lethal properties of phospholipase A2 from Bothrops alternatus (víbora de la cruz) venom (1988) Toxicon, 26 (12), pp. 1137-1144Gutiérrez, J.M., Lomonte, B., Phospholipase A2 myoToxins from Bothrops snake venoms (1995) Toxicon, 33 (11), pp. 1405-1424Gutiérrez, J.M., Lomonte, B., Phospholipase A2 myoToxins from Bothrops snake venoms (1997) Venom Phospholipase A2 Enzymes, Structure, Function and Mechanism, pp. 321-352. , Kini R.M. (Ed), John Wiley, New YorkSelistre de Araujo, H.S., White, S.P., Ownby, C.L., Sequence analysis of Lys49 phospholipase A2 myoToxins: a highly conserved class of proteins (1996) Toxicon, 34 (11-12), pp. 1237-1242Francis, B., Gutiérrez, J.M., Lomonte, B., Kaiser, I.I., Myotoxin II from Bothrops asper (Terciopelo) venom is a lysine-49 phospholipase A2 (1991) Arch. Biochem. Biophys., 284, pp. 352-359Tsai, I.H., Chen, Y.H., Wang, Y.M., Tu, M.C., Tu, A.T., Purification, sequencing, and phylogenetic analyses of novel Lys-49 phospholipases A2 from the venoms of rattlesnakes and other pit vipers (2001) Arch. Biochem. Biophys., 394, pp. 236-244Angulo, Y., Olamendi-Portugal, T., Alape-Girón, A., Possani, L.D., Lomonte, B., Structural characterization and phylogenetic relationships of myotoxin II from Atropoides (Bothrops) nummifer snake venom, a Lys49 phospholipase A2 homologue (2002) Int. J. Biochem. Cell Biol., 34, pp. 1268-1278Arni, R.K., Ward, R.J., Phospholipase A2: a structural review (1996) Toxicon, 34, pp. 827-841van den Bergh, C.J., Slotboom, A.J., Verheij, H.M., de Haas, G.H., The role of aspartic acid-49 in the active site of phospholipase A2. A site-specific mutagenesis study of porcine pancreatic phospholipase A2 and the rationale of the enzymatic activity of [lysine49] phospholipase A2 from Agkistrodon piscivorus piscivorus venom (1988) Eur. J. Biochem., 176, pp. 353-357Li, Y., Yu, B., Zhu, H., Jain, M., Tsai, M., Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-49 (1994) Biochemistry, 33, pp. 14714-14722Lee, W.H., da Silva Giotto, M.T., Marangoni, S., Toyama, M.H., Polikarpov, I., Garrat, R.C., Structural basis for low catalytic activity in Lys49 phospholipases A2-A hypothesis: the crystal structure of piratoxin II complexed to fatty acid (2001) Biochemistry, 40, pp. 28-36Chioato, L., Ward, R.J., Mapping structural determinants of biological activities in snake venom phospholipases A2 by sequence analysis and site directed mutagenesis (2003) Toxicon, 42, pp. 869-883Lomonte, B., Moreno, E., Tarkowski, A., Hanson, L.A., Maccarana, M., Neutralizing interaction between heparins and myotoxin II, a Lys-49 phospholipase A2 from Bothrops asper snake venom. Identification of a heparin-binding and cytolytic toxin region by the use of synthetic peptides and molecular modeling (1994) J. Biol. Chem., 269, pp. 29867-29873Dhillon, D.S., Condrea, E., Maraganore, J.M., Heinrikson, R.L., Benjamin, S., Rosenberg, P., Comparison of enzymatic and pharmacological activities of lysine-49 and aspartate-49 phospholipases A2 from Agkistrodon piscivorus piscivorus snake venom (1987) Biochem. Pharmacol., 36, pp. 1723-1730Soares, A.M., Guerra-Sá, R., Borja-Oliveira, C.R., Rodrigues, V.M., Rodrigues-Simioni, L., Rodrigues, V., Fontes, M.R., Giglio, J.R., Structural and functional characterization of BnSP-7, a Lys49 myotoxic Phospholipase A2 homologue from Bothrops neuwiedi pauloensis venom (2000) Arch. Biochem. Biophys., 378, pp. 201-209Oshima-Franco, Y., Leite, G.B., Silva, G.H., Cardoso, D.F., Hyslop, S., Giglio, J.R., da Cruz-Hofling, M.A., Rodrigues-Simioni, L., Neutralization of the pharmacological effects of bothropstoxin-I from Bothrops jararacussu (jararacucu) venom by crotoxin antiserum and heparin (2001) Toxicon, 39, pp. 1477-1485Oshima-Franco, Y., Leite, G.B., Dal Belo, C.A., Hyslop, S., Prado-Franceschi, J., A.C.O.Cintra, J.R., Giglio, M.A., da Cruz-Höfling, L., The presynaptic activity of bothropstoxin-I, a myotoxin from Bothrops jararacussu snake venom (2004) Basic. Clin. Pharmacol. Toxicol., 95 (4), pp. 175-182Borja-Oliveira, C.R., Durigon, A.M., Vallin, AC., Toyama, M.H., Souccar, C., Marangoni, S., Rodrigues-Simioni, L., The pharmacological effect of Bothrops neuwiedii pauloensis (jararaca-pintada) snake venom on avian neuromuscular transmission (2003) Braz. J. Med. Biol. Res., 36 (5), pp. 617-624Bonfim, V.L., Toyama, M.H., Novello, J.C., Hyslop, S., Oliveira, C.R.B., Rodrigues-Simioni, L., Marangoni, S., Isolation and enzymatic characterization of a basic phospholipase A2 from Bothrops jararacussu snake venom (2001) J. Protein Chem., 20, pp. 239-245Cavalcante, W.L., Silva, M.D., Gallacci, M., Influence of temperature upon paralyzing and myotoxic effects of bothropstoxin-I on mouse neuromuscular preparations (2005) Chem.-Biol. Interact., 15 (151 2), pp. 95-100Rosenberg, P., Lethal potency of snake venom phospholipase A2 enzymes. Pitfalls to avoid in the study of correlations between enzymatic activity and pharmacological properties of phospholipase A2 enzymes (1997) Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism, pp. 129-154. , Kini R.M. (Ed), Wiley, New YorkPáramo, L., Lomonte, B., Pizarro-Cerdá, J., Bengoechea, J.A., Gorvel, J.P., Moreno, E., Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from Bothrops asper snake venom. Synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region (1998) Eur. J. Biochem., 253, pp. 452-461Mora, R., Valverde, B., Díaz, C., Lomonte, B., Gutiérrez, J.M., A Lys-49 phospholipase A2 homologue from Bothrops asper snake venom induces proliferation, apoptosis and necrosis in a lymphoblastoid cell line (2005) Toxicon, 45, pp. 651-660Zuliani, J.P., Fernandes, C.M., Zamuner, S.R., Gutiérrez, J.M., Teixeira, C.F.P., Inflammatory events induced by Lys-49 and Asp-49 phospholipases A2 isolated from Bothrops asper snake venom: role of catalytic activity (2005) Toxicon., 45, pp. 335-346Fenard, D., Lambeau, G., Valentin, E., Lefebvre, J.C., Lazdunski, M., Doglio, A., Secreted phospholipases A2, a new class of HIV inhibitors that block virus entry into host cells (1999) J. Clin. Invest., 104, pp. 611-618Cintra, A.C.O., Marangoni, S., Oliveira, B., Giglio, J.R., Bothropstoxin-I: amino acid sequence and function (1993) J. Protein Chem., 12, pp. 57-64Soares, A.M., Rodrigues, V.M., Homsi-Brandeburgo, M.I., Toyama, M.H., Lombardi, F.R., Arni, R.K., Giglio, J.R., A rapid procedure for the isolation of the Lys-49 myotoxin II from Bothrops moojeni (caissaca) venom: biochemical characterization, crystallization, myotoxic and edematogenic activity (1998) Toxicon, 36, pp. 503-514Toyama, M.H., Soares, A.M., Vieira, C.A., Novello, J.C., Oliveira, B., Giglio, J.R., Marangoni, S., Amino acid sequence of piratoxin-I, a myotoxin from Bothrops pirajai snake venom and its biological activity after alkylation with p-bromophenacyl bromide (1998) J. Protein Chem., 17, pp. 713-728Rodrigues, V.M., Soares, A.M., Mancin, A.C., Fontes, M.R.M., Homsi-Brandeburgo, M.I., Giglio, J.R., Geographic variations in the composition of myoToxins from Bothrops neuwiedi snake venoms: biochemical characterization and biological activity (1998) Comp. Biochem. 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  • Effect Of Bothrops Insularis Venom On The Mouse And Chick Nerve-muscle Preparation
    2015
    Co-Authors: Cogo J.c., Prado-franceschi J., Corrado A.p., Rodrigues-simioni L.
    Abstract:

    J. C. Cogo, J. Prado-Franceschi, M. A. Cruz-Hofling, A. P. Corrado and L. Rodrigues-Simioni. Effect of Bothrops insularis venom on the mouse and chick nerve-muscle preparation. Toxicon 31, 1237-1247, 1993.-The effects of Bothrops insularis venom were examined in vivo in mice and chicks and in vitro using the mouse phrenic nerve diaphragm and chick biventer cervicis muscle preparations. Incubation of the indirectly or directly stimulated mouse preparation with B. insularis venom (20-80 μg/ml) produced an initial increase in twitch tension followed by irreversible blockade. With direct stimulation in the presence of d-tubocurarine, no increase in twitch tension was observed prior to the onset of blockade. A venom-induced effect on presynaptic activity was suggested by the marked increase in the frequency of the mepps recorded in vitro 5-15 min after venom addition. A direct muscular effect was shown by the dose- and time-dependent reduction in the resting membrane potential of the diaphragm. Chick preparations were more sensitive than those of the mouse. In the isolated chick biventer cervicis muscle preparation, B. insularis venom induced a contracture and a dose-dependent block of responses to indirect stimulation. At low venom concentrations (1-5 μg/ml), no significant release of creatine kinase (CK) was observed from this preparation. However, a dose-dependent release of CK was detected at higher doses (10-80 μg/ml). For morphological studies, B. insularis venom was injected into the chick left pectoralis muscle. At low doses (0.4 μg), only an inflammatory reaction was present, while at high doses (20-80 μg) increasing numbers of necrotic fibers were observed as well as occlusive thrombosis and hemorrhage. 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Res., 20, pp. 821-824Moreno, Gutiérrez, Body distribution of Bothrops asper (terciopelo) snake venom myotoxin and its relationship to pathological changes (1988) Toxicon, 26, pp. 403-409Nakada, Uezu, Ohshiro, Miyagi, Relation between serum creatine phosphokinase activity and the amount of Habu (Trimeresurus flavoviridis) snake venom injected in thigh muscle in rabbits (1980) Toxicon, 18, pp. 351-355Ownby, Odell, Woods, Coleberg, Ability of antiserum to myotoxin a from prairie rattlesnake (Crotalus viridis viridis) venom to neutralize local myotoxicity and lethal effects of myotoxin a and homologous crude venom (1983) Toxicon, 21, pp. 35-45Queiroz, Santo Neto, Rodrigues-Simioni, Prado-Franceschi, Muscle necrosis and regeneration after envenomation by Bothrops jararacussu snake venom (1983) Toxicon, 22, pp. 339-346Queiroz, Santo Neto, Assakura, Reichl, Mandelbaum, Muscular lesions induced by a hemorrhagic factor from Bothrops neuwiedi snake venom (1985) Braz. J. Med. Biol. Res., 18, pp. 337-340Queiroz, Santo Neto, Assakura, Reichl, Mandelbaum, Pathological changes in muscle caused by hemorrhagic and proteolytic factors from Bothrops jararaca snake venom (1985) Toxicon, 23, pp. 341-345Rodrigues-Simioni, Borgese, Ceccarelli, The effects of Bothrops jararacussu venom and its components on frog nerve muscle preparation (1983) Neuroscience, 10, pp. 475-489Selistre, Giglio, Isolation and characterization of a thrombin-like enzyme from venom of the snake Bothrops insularis (jararaca ilhôa) (1987) Toxicon, 25, pp. 1135-1144Selistre, Queiroz, Cunha, Souza, Giglio, Isolation and characterization of hemorrhagic, myonecrotic and edema-inducing Toxins from Bothrops insularis (jararaca ilhôa) snake venom (1990) Toxicon, 28, pp. 261-273Vital Brazil, Peçonhas (1982) Farmacodinâmica, pp. 1044-1074. , C.E. Corbett, Guanabara Koogan S.A, Rio de JaneiroVital Brazil, Fontana, Açôes pré-juncionais e pós-juncionais da peçonha da cobra coral Micrurus corallinus na junção neuromuscular (1983) Mem. Inst. Butantan., 47-48, pp. 13-26Weil, Tables for convenient calculation of median-effective doses (ld50 or ed50) and instructions for their use (1953) Biometrics, 8, pp. 249-26

  • Fractionation Of Bothrops Jararacussu Snake Venom: Partial Chemical Characterization And Biological Activity Of Bothropstoxin
    2015
    Co-Authors: Homsi-brandeburgo M.i., Santo Neto H., Queiroz L.s., Rodrigues-simioni L.
    Abstract:

    A myotoxin, bothropstoxin (BthTX), showing no detectable phospholipase A2 activity, was purified to homogeneity from the venom of the Brazilian snake Bothrops jararacussu by a combination of gel filtration on Sephadex G-75 and ion-exchange chromatography on SP-Sephadex C-25. Four phospholipases (SIII-SPI to SIII-SPIV) were also isolated, the latter showing, similarly to BthTX (SIII-SPV) myonecrotic activity. Approximate mol. wts, as determined by SDS-PAGE, and pI of SIII-SPI to SIII-SPIV are: 22,400-4.2; 15,500-4.8; 13,800-6.9; and 13,200-7.7, respectively. BthTX is a single chain protein, approximate mol. wt 13,000, with 16 half-cystine residues, pI = 8.2 and LD50 = 7.5 mg/kg (i.p.) and 4.8 mg/kg (i.v.) for 20 g mice. The ten first N-terminal amino acid residues show a significant homology to other Toxins with phospholipase structure. BthTX is specifically myotoxic, contrary to crude B. jararacussu venom which, although also myotoxic, affects intramuscular arteries and veins leading to thrombosis. BthTX and SIII-SPIV also differ from Toxins isolated from the venom of other Brazilian snakes which are strongly hemorrhagic. © 1988.267615627Alonzo, Hirs, Automation of sample application in amino acid analysers (1968) Anal. 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Timasheff, Academic Press, New York, part BGutiérrez, Ownby, Odell, Isolation of a myotoxin from Bothrops asper venom: partial characterization and action on skeletal muscle (1984) Toxicon, 22, p. 115Gutiérrez, Lomonte, Cerdas, Isolation and partial characterization of a myotoxin from the venom of the snake Bothrops nummifer (1986) Toxicon, 24, p. 885Itzhaki, Gill, A micro-biuret method for estimating proteins (1964) Anal. Biochem., 9, p. 401Jimenez-Porras, Reptile Toxins (1973) Biology Data Book, 2, p. 697. , 2nd edn, Federation of American Societies for Experimental Biology (FASEB), Bethesda, MD., U.S.AKarlsson, Chemistry of protein toxin in snake venoms (1979) Handbook of Experimental Pharmacology, 52, p. 159. , C.Y. Lee, Springer-Verlag, BerlinKlobusitzky, Coagulant and anticoagulant agents in snake venoms (1961) Am. J. Med. Sci., 242, p. 107Lee, Recent advances in the chemistry and pharmacology of snake Toxins (1979) Advances in Cytopharmacology, 3, p. 1. , B. Ceccarelli, F. Clementi, Raven Press, New YorkMandelbaum, Reichl, Assakura, Some physical and biochemical characteristics of HF2, one of the hemorrhagic factors in the venom of Bothrops jararaca (1976) Animal, Plant and Microbial Toxins, 1, p. 111. , A. Ohsaka, K. Hayashi, Y. Sawai, Plenum Press, LondonMandelbaum, Reichl, Assakura, Isolation and characterization of a proteolytic enzyme from the venom of the snake Bothrops jararaca (jararaca) (1982) Toxicon, 20, p. 955Mandelbaum, Assakura, Reichl, Characterization of two hemorrhagic factors isolated from the venom of Bothrops neuwiedi (jararaca pintada) (1984) Toxicon, 22, p. 193Marinetti, The action of phospholipase A on lipoproteins (1965) Biochim. biophys. Acta, 98, p. 554Mebs, Samejima, Isolation and characterization of myotoxic phospholipase A2 from crotalid venoms (1986) Toxicon, 24, p. 161Moore, Stein, A modified ninhydrin reagent for the photometric determination of amino acids and related compounds (1954) J. biol. Chem., 211, p. 907Nisenbom, Seki, Vidal, Phospholipase A2 from Bothrops alternatus (vibora de la cruz) venom. Purification and some characteristic properties (1986) Toxicon, 24, p. 259Nisenbom, Perazzo, Monserrat, Vidal, Contribution of phospholipase A2 to the lethal potency of Bothrops alternatus (vibora de la cruz) venom (1986) Toxicon, 24, p. 807Ownby, Bjarnason, Tu, Hemorrhagic Toxins from rattlesnake (Crotalus atrox) venom. Pathogenesis of hemorrhage induced by three purified Toxins (1978) Am. J. Pathol., 93, p. 201Penke, Ferenczi, Kovaes, A new acid hydrolysis method for determining tryptophan in peptides and proteins (1974) Anal. Biochem., 60, p. 45Queiroz, Santo Neto, Rodrigues-Simioni, Prado-Franceschi, Muscle necrosis and regeneration after envenomation by Bothrops jararacussu snake venom (1984) Toxicon, 22, p. 339Queiroz, Santo Neto, Assakura, Reichl, Mandelbaum, Pathological changes in muscle caused by haemorrhagic and proteolytic factors from Bothrops jararaca snake venom (1985) Toxicon, 23, p. 341Reimerdes, Klostermeyer, Determination of proteolytic activities on casein substrates (1976) Methods in Enzymology, 45, p. 26. , L. Lorand, Academic Press, New YorkReisfeld, Lewis, Williams, Disk electrophoresis of basic proteins and peptides on polyacrylamide gels (1962) Nature, 195, p. 281Rodrigues-Simioni, Borgese, Ceccarelli, The effects of Bothrops jararacussu venom and its components on frog nerve-muscle preparation (1983) Neuroscience, 10, p. 475Rosenfeld, Symptomatology, pathology and treatment of snake bites in South America (1971) Venomous Animals and Their Venoms, 2, p. 345. , W. Bücherl, E.E. Buckley, Academic Press, New YorkRothschild, Rothschild, Liberation of pharmacologically active substances by snake venoms (1979) Snake Venoms, p. 541. , C.Y. Lee, Springer Verlag, New YorkSelistre, Giglio, Isolation and characterization of a thrombin-like enzyme from the venom of the snake Bothrops insularis (jararaca ilhoa) (1987) Toxicon, 25, p. 1135Shapiro, Vinuela, Matzel, Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels (1967) Biochem. biophys. Res. Commun., 28, p. 815Spackman, Stein, Moore, Automatic recording apparatus for use in the cromatography of amino acids (1958) Anal. Chem., 30, p. 1190Strydom, The evolution of Toxins found in snake venoms (1979) Snakes Venoms, p. 258. , C.Y. Lee, Springer Verlag, BerlinTu, Blood Coagulation (1977) Venoms — Chemistry and Molecular Biology, , John Wiley, New YorkVesterberg, Isoelectric focusing of protein in polyacrylamide gels (1972) Biochim. biophys. 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  • Histopathological Changes In Avian Kidney Caused By Bothrops Insularis (jararaca Ilhôa) Venom And A Phospholipase A2-containing Fraction
    2015
    Co-Authors: Da Cruz-hofling, Rodrigues-simioni L., Cogo J.c., Paronetto C.c.l., D'abreu A.c.f.
    Abstract:

    The histopathological changes induced in avian kidney by the intramuscular injection of Bothrops insularis (jararaca ilhôa) venom and its phospholipase A2 (PLA2)-containing fraction were examined. Acute experiments (3 h and 24 h) with B. insularis crude venom (20 μg and 80 μg) or its PLA2-containing fraction (10 μg and 40 μg) resulted in significant structural damage to the kidneys of 5-12-day-old chicks. Histopathological analysis indicated that the venom and its fraction acted on the renal tubules and glomeruli. The morphological changes, although widespread, varied in intensity from cell to cell, and from tubule to tubule in venom-injected chicks. The tubular and glomerular changes produced by the venom and its PLA2-containing fraction may be the result of a direct cytotoxic effect potentiated by ischemia-related disturbances in the regional hemodynamics. The venom and its fraction affected more segments along reptilian-type nephrons than along mammalian ones. This divergent sensitivity to the venom and its fraction may reflect the species-specific characteristics of B. insularis snake, an example of geographical isolation influencing its diet which is almost exclusively avian.161185195Amaral, A., Excursão à Ilha da Queimada Grande (1918) Col. Trab. Inst. Butantan, 2, pp. 49-55Amaral, A., Contribuição à biologia dos ofídos brasileiros (habitat, hábitos e alimentação) - Primeira nota prévia (1924) Col. dos Trab. do I. Butantan, 2, pp. 177-181Amaral, C.F.S., Da Silva, O.A., Godoy, P., Miranda, D., Renal cortical necrosis following Bothrops jararaca and B. jararacussu bite (1985) Toxicon, 23, pp. 877-885Amorim, M.F., Mello, R.F., Intermediate nephron nephrosis from snake poisoning in man. Histopathological study (1954) Am. J. Pathol., 30, pp. 470-499Aung-Khin, M., Histological and ultrastructural changes of the kidney in renal failure after viper envenomation (1978) Toxicon, 16, pp. 71-75Boer-Lima, P., Gontijo, J.A.R., Cruz-Höfling, M.A., Histological and functional alterations in the kidneys induced in rats by Bothrops moojeni venom (1999) Am. J. Trop. Med. Hyg., 61, pp. 698-706Borkow, G., Gutiérrez, J.M., Ovadia, M., Isolation and characterization of synergistic hemorrhagins from the venom of Bothrops asper (1993) Toxicon, 31, pp. 1137-1150Chapman, D., The symptomatology, pathology and treatment of the bites of venomous snakes of Central and Southern Africa (1968) Venomous Animals and their Venoms, pp. 463-527. , Bücherl W., Buckley E.E. and Deulofeu V. (ed). Academic Press. New York, LondonChugh, K.S., Aikat, B.K., Sharma, B.K., Rash, S.C., Mathew, M.T., Das, K.C., Acute renal failure following snake bite (1975) Am. J. Trop. Med. Hyg., 24, pp. 692-697Cintra, A.C.D., Laure, O.B., Prado-Franceschi, J., Giglio, J.R., Bradykinin potentiating-peptides from the venom of Bothrops insularis. Isolation and primary structure (1984) Arq. Biol. Tecnol., 27, p. 248. , (Abstract)Cogo, J.C., Prado-Franceschi, J., Cruz-Höfling, M.A., Corrado, A.P., Rodrigues-Simioni, L., Effects of Bothrops insularis venom on the mouse and chick nerve-muscle preparation (1993) Toxicon, 31, pp. 1237-1247Cogo, J.C., Prado-Franceschi, J., Giglio, J.R., Corrado, A.P., Cruz-Höfling, M.A., Donato, J.L., Leite, G.B., Rodrigues-Simioni, L., An unusual presynaptic action of Bothrops insularis snake venom mediated by a phospholipase A2 fraction (1998) Toxicon, 36, pp. 1323-1332Cruz-Höfling, M.A., Cogo, J.C., Rodrigues-Simioni, L., Vascular changes induced by Bothrops insularis venom (1992) Proceedings of the IV Pan-American Symposium on Animal, Plant and Microbial Toxins, Campinas, SP, Brazil, p. 129. , (Abstract)Da Silva, O.A., López, M., Godoy, P., Bilateral cortical necrosis and calcification of the kidneys following snakebite: A case report (1979) Clin. Nephrol., 55, pp. 136-139Da Silva, O.A., López, M., Godoy, P., Intensive care unit treatment of acute renal failure following snake bite (1979) Am. J. Trop. Med. Hyg., 28, pp. 401-407Date, A., Shastry, J.C.M., Renal ultrastructure in acute tubular necrosis following Russel's viper envenomation (1982) J. Pathol., 137, pp. 225-241Furtado, M.F.D., Colletto, G.M.D.D., Dias Da Silva, W., Controle de qualidade dos venenos animais e dos correspondentes antivenenos. 1. Padronização dos métodos de ensaio das atividades bioquímicas e farmacológicas dos venenos de algumas espécies do gênero Bothrops e Crotalus usando amostras secas à temperatura ambiente ou liofilizadas (1991) Mem. Inst. Butantan, 53, pp. 149-159Gutiérrez, J.M., Lomonte, B., Phospholipase A2 myoToxins from Bothrops snake venoms (1995) Toxicon, 33, pp. 1405-1424Gutiérrez, J.M., Romero, M., Díaz, C., Borkow, G., Ovadia, M., Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (Terciopelo) (1995) Toxicon, 33, pp. 19-29Johnson, O.W., Relative thickness of the renal medulla in birds (1974) J. Morphol., 142, pp. 277-284Johnson, O.W., Skadhauge, E., Structural-functional correlation in the kidneys and observations of colon and cloacal morphology in certain Australian birds (1975) J. Anat., 120, pp. 495-505Kamiguti, A.S., Theakston, R.D.G., Desmond, N., Nutton, R.S., Systemic haemorrhage in rats induced by a haemorrhagic fraction from B. jararaca venom (1991) Toxicon, 29, pp. 1097-1105Kini, R.M., Evans, H.J., A model to explain the pharmacological effects of snake venom phospholipases A2 (1989) Toxicon, 27, pp. 613-635Mebs, D., A comparative study of enzyme activities in snake venoms (1970) Int. J. Biochem., 1, p. 335Pearce, R.M., An experimental glomerular lesion caused by venom (Crotalus adamanteus) (1909) J. Exp. Med., 11, pp. 532-540Pearce, R.M., An experimental study of the late glomerular lesions caused by Crotalus venom (1913) J. Exp. Med., 18, pp. 149-155Racusen, L.C., Biology of disease. Alterations in tubular epithelial cell adhesion and mechanism of acute renal failure (1992) Lab. Invest., 67, pp. 158-165Rezende, N.A., Amaral, C.F.S., Bambirra, E.A., Lachatt, J.J., Coimbra, T.M., Functional and histopathological renal changes induced in rats by Bothrops jararaca venom (1989) Braz. J. Med. Biol. Res., 22, pp. 407-416Riddel, C., Urinary system (1987) Am. Assoc. Avian Pathol. Publ., pp. 67-73. , In: Avian pathology. Riddel C. (ed)Rosenfeld, G., Symptomatology, pathology and treatment of snake bite on South America (1971) Venomous Animals and Their Venoms, pp. 345-384. , Bücherl W., Buckley E.E. and Deulofeu V. (ed). Academic Press. New York, LondonSakurai, N., Sugimoto, K., Sugihara, H., Shirasawa, H., Muro, H., Kaneko, M., Nikai, T., Shibata, K., Glomerular injury in mice induced by Agkistrodon venom (1986) Am. J. Pathol., 122, pp. 240-251Sánchez, E.F., Costa, M.I.E., Chávez-Olortegui, C., Assakura, M., Mandelbaum, F.R., Diniz, C.R., Characterization of a hemorrhagic factor, LHF-1, isolated from the bushmaster snake (Lachesis muta muta) venom (1995) Toxicon, 33, pp. 1653-1667Acidentes por animais peçonhentos. identificação, diagnóstico e tratamento (1993) Manual de Vigilância Epidemiológica, p. 61Seegers, W.H., Ouyang, C., Snake venoms and blood coagulation (1978) Hand. 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  • Microbial pest control agents use patterns registration requirements and mammalian toxicity
    Hayes' Handbook of Pesticide Toxicology (Third Edition), 2010
    Co-Authors: Andrew L Rubin
    Abstract:

    Publisher Summary This chapter reviews the regulatory system in place in the United States for assessing the toxicity, infectivity, and pathogenicity of MPCAs to humans. In addition, toxicologic overviews for several prominent or proposed MPCAs are provided. These overviews are directed primarily at toxicity and pathogenicity issues arising from exposure to viable Microbial organisms, although individual Microbial Toxins are considered in some cases. Concern for the safety of agricultural workers and the public, as well as for the integrity of ecosystems, has fueled an interest in the use of microbes as pest control agents. In addition to such pest management dividends as low toxicity and low environmental impacts, Microbial pest control agents (MPCAs) offer high target selectivity and extended pest control in cases where establishment of the microbe occurs in local habitats. The promise of Microbial pest control agents resides in their host organism specificity and in their relatively benign ecosystem and human health impacts. It is possible that hazards to humans posed by living organisms could be missed in animal studies. Particular attention must be paid to the welfare of sensitive human subpopulations such as those who are diseased or immunocompromised or who might be allergic to specific microorganisms. Attention to strain type is always important and even more so when the microbe in question belongs to a medically significant species or genus. In the final analysis, continued monitoring of the health effects of MPCAs under conditions of actual pesticidal manufacture and use is warranted to ensure the safety of this fascinating and viable approach to pest control.

  • chapter 40 mammalian toxicity of Microbial pest control agents
    Handbook of Pesticide Toxicology (Second Edition), 2001
    Co-Authors: Andrew L Rubin
    Abstract:

    Concern for the safety of agricultural workers and the public, as well as for the integrity of ecosystems, has fueled an interest in the use of microbes as pest control agents. This is evident from high increase in products listing Microbial pest control agents (MPCAs) as active ingredients, thus greater human exposure to MPCAs under both occupational and nonoccupational scenarios is a reasonable expectation. This chapter reviews the current regulatory system in the United States for assessing the potential for toxicity, infectivity, and pathogenicity of Microbial Pest Control Agents (MPCAs) in humans. The requirements for toxicity testing of these agents in the United States under Subdivision M of the Federal Insecticide, Fungicide, and Rodenticide Act are designed to provide a fast and efficacious means to identify problematic MPCAs, while moving the rest toward registration. The chapter presents toxicological overviews for several prominent or proposed MPCAs, including Bacillus thuringiensis, Bacillus cereus, Burkholderia Cepacia, Beauveria bassiana, Gliocladium virens, Lagenidium Giganteum, Baculoviruses, Rabbit hemorrhagic disease virus (RHDV) , and Metarhizium Anisopliae . These overviews are directed primarily at toxicity and pathogenicity issues arising from exposure to viable Microbial organisms, though individual Microbial Toxins are considered in some cases.