Antibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: Phospholipase A 2 and l-amino acid oxidase

Toxicon

Volumn 55, Issue 4, 2010, Pages 795-804

  Costa Torres, Alba Fabiola ^a   Dantas, Rodrigo Tavares ^a   Toyama, Marcos H ^b   Filho, Eduardo Diz ^b,c   Zara, Fernando José ^b   Rodrigues de Queiroz, Maria Goretti ^a   Pinto Nogueira, Nadia Accioly ^a   Rosa de Oliveira, Márcia ^d   de Oliveira Toyama, Daniela ^e   Monteiro, Helena S A ^a   Martins, Alice M C ^a  

^a FEDERAL UNIVERSITY OF CEARÁ   (Brazil)

^b SÃO PAULO STATE UNIVERSITY UNESP   (Brazil)

^c INSTITUTO BIOLÓGICO   (Brazil)

^d FEDERAL UNIVERSITY OF PARAÍBA   (Brazil)

^e MACKENZIE PRESBYTERIAN UNIVERSITY   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

AMIKACIN; AMINO ACID OXIDASE; LYSINE; PHOSPHOLIPASE A2; SNAKE VENOM; ANTIINFECTIVE AGENT; ANTIPROTOZOAL AGENT;

AMINO ACID SEQUENCE; ANIMAL CELL; ANTIBACTERIAL ACTIVITY; ANTIPROTOZOAL ACTIVITY; ARTICLE; BACTERIAL STRAIN; BOTHROPS; CANDIDA ALBICANS; CONTROLLED STUDY; CYTOTOXICITY; ENZYME PURIFICATION; FEMALE; FUNGAL STRAIN; GENETIC CONSERVATION; GROWTH INHIBITION; IC 50; LEISHMANIA; LEISHMANIA CHAGASI; MACROPHAGE; MINIMUM INHIBITORY CONCENTRATION; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMASTIGOTE; PSEUDOMONAS AERUGINOSA; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SEQUENCE HOMOLOGY; STAPHYLOCOCCUS AUREUS; ANIMAL; CHEMISTRY; DRUG EFFECT; ENZYMOLOGY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ION EXCHANGE CHROMATOGRAPHY; MICROBIOLOGICAL EXAMINATION; MOLECULAR GENETICS; POLYACRYLAMIDE GEL ELECTROPHORESIS; SNAKE;

BACTERIA (MICROORGANISMS); BOTHROPS; BOTHROPS MARAJOENSIS; CANDIDA ALBICANS; LEISHMANIA SP.; PSEUDOMONAS AERUGINOSA; SERPENTES; STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; ANIMALS; ANTI-BACTERIAL AGENTS; ANTIPROTOZOAL AGENTS; BOTHROPS; CHROMATOGRAPHY, DEAE-CELLULOSE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CROTALID VENOMS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; L-AMINO ACID OXIDASE; MACROPHAGES; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; PHOSPHOLIPASES A2; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 77953383971     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2009.11.013     Document Type: Article

References (54)

1. Ali S.A., Stoeva S., Abbasi A., Alam J.M., Kayed R., Faigle M., Neumeister B., Voelter W. Isolation, structural, and functional characterization of an apoptosis-inducing l-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom. Arch. Biochem. Biophys 2000, 384:216-226.
2. Bailey P., Wilce J. Venom as a source of useful biologically active molecules. Emerg. Med. (Fremantle) 2001, 13:28-36.
3. 2 and apoptosis. Biochim. Biophys. Acta 2006, 1761:1344-1350.
4. Barbosa P.S., Martins A.M., Havt A., Toyama D.O., Evangelhista J.S., Ferreira D.P., Joazeiro P.P., Beriam L.O., Toyama M.H., Fonteles M.C., Monteiro H.S. A Renal and antibacterial effects induced by myotoxin I and II isolated from Bothrops jararacussu venom. Toxicon 2005, 46:376-386.
5. Bon C. Snake venom & pharmacopoeia. Snakes a Natural History 1997, 194-209. Sterling Publishing Co., New York. R. Bauchot (Ed.).
6. 2 from Bothrops jararacussu snake venom. J. Protein Chem. 2001, 20:239-245.
7. Bouza E., Garcia-Garrote F., Cercenado E., Marín M., Díaz M.S., Sánchez-Romero I., Vindel A. Pseudomonas aeruginosa: a multicenter study in 136 hospitals in Spain. Rev. Esp. Quimioter 2003, 16:41-52.
8. Braga M.D., Martins A.M., Amora D.N., De Menezes D.B., Toyama M.H., Toyama D.O., Marangoni S., Alves C.D., Barbosa P.S., De Souza Alves R., Fonteles M.C., Monteiro H.S. Purification and biological effects of l-amino acid oxidase isolated from Bothrops insularis venom. Toxicon 2008, 51:199-207.
9. 2 isoforms: a perspective. Cell. Signal 2003, 15:637-665.
10. De Oliveira D.G., Toyama M.H., Martins A.M., Havt A., Nobre A.C., Marangoni S., Câmara P.R., Antunes E., De Nucci G., Beliam L.O., Fonteles M.C., Monteiro H.S. Structural and biological characterization of a crotapotin isoform isolated from Crotalus durissus cascavella venom. Toxicon 2003, 42:53-62.
11. 2 from B. jararacussu. Int. J. Mol. Sci. 2008, 9(5):736-750.
12. Du X.Y., Clemetson K.J. Snake venom l-amino acid oxidases. Toxicon 2002, 40:659-665.
13. França S.C., Kashima S., Roberto P.G., Marins M., Ticli F.K., Pereira J.O., Astolfi-Filho S., Stábeli R.G., Magro A.J., Fontes M.R.M., Sampaio S.V., Soares A.M. Molecular approaches for structural characterization of Bothrops l-amino acid oxidases with antiprotozoal activity: cDNA cloning, comparative sequence analysis, and molecular modeling. Biochem. Biophys. Res. Commun 2007, 355:302-306.
14. Fridkin S.K., Gaynes R.P. Antimicrobial resistence in intensive care units. Clin. Chest Med 1999, 20:303-316.
15. Gonçalves A.R., Soares M.J., Souza W., De Damatta R.A., Alves E.W. Ultra structural alterations and growth inhibition of Trypanosoma cruzi and Leishmania major induced by Bothrops jararaca venom. Parasitol. Res. 2002, 88:598-602.
16. 2 from Bothrops leucurus (white-tailed-jararaca) snake venom. Biochimie 2006, 89:319-328.
17. Izidoro L.F.M., Ribeiro M.C., Souza G.R.L. Biochemical and functional characterization of an l-amino acid oxidase isolated from Bothrops pirajai snake venom. Bioorg. Med. Chem. 2006, 14:7034-7043.
18. 2 enzymes. Toxicon 2003, 42:827-840.
19. Kishimoto M., Takahashi T. A spectrophotometric microplate assay for l-amino acid oxidase. Anal. Biochem 2001, 298:136-139.
20. 2 from Bothrops asper snake venom. Identification of heparin-binding and cytolytic toxin region by the use of synthetic peptides and molecular modeling. J. Biol. Chem. 1994, 269:29867-29873.
21. 2 myotoxins from crotalid snake venoms and their structural determinants of myotoxic action. Toxicon 2003, 42:885-901.
22. Lu Q.M., Wei Q., Jin Y., Wei J.F., Wang W.Y., Xiong Y.L. l-amino acid oxidase from Trimeresurus jerdonii snake venom: purification, characterization, platelet aggregation-inducing and antibacterial effects. J. Nat. Toxins 2002, 11:345-352.
23. Lu Q., Clemetson J.M., Clemetson K.J. Snake venoms and hemostasis. J. Thromb. Haemost 2005, 3:1791-1799.
24. Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity. J. Immunol. Methods 1983, 65:55-63.
25. NCCLS, 2003a. Performance Standards for Antimicrobial Disk Susceptibility Tests; Approved Standard-Eighth Edition. NCCLS document M2-A8 (ISBN 1-56238-485-6). NCCLS, 940 West Valley Road, Suite 1400, Wayne, Pennsylvania 19087-1898 USA.
26. NCCLS, 2003b. Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria That Grow Aerobically; Approved Standard-Sixth Edition. NCCLS document M7-A6 (ISBN 1-56238-486-4). NCCLS, 940 West Valley Road, Suite 1400, Wayne, Pennsylvania 19087-1898 USA.
27. 2 homologue from the venom of the snake Bothrops atrox. Toxicon 2004, 44:91-101.
28. Oliveira M.R., Tafuri W.L., Nicoli J., Vieira E.C., Melo M.N., Vieira L.Q. Influence of microbiota in experimental cutaneous leishmaniasis in Swiss mice. Rev. Inst. Med. Trop. S. Paulo 1999, 42:87-94.
29. 2 isolated from Crotalus durissus terrificus venom. J. Protein Chem. 2002, 21:161-168.
30. 2 from Bothrops asper snake venom - synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region. Eur. J. Biochem 1998, 253:452-461.
31. Passero L.F.D., Tomokane T.Y., Corbett C.E.P., Laurenti M.D., Toyama M.H. Comparative studies of the anti-leishmanial activity of three Crotalus durissus ssp. venoms. Parasitol. Res. 2007, 101:1365-1371.
32. 2 from Crotalus durissus collilineatus on Leishmania (Leishmania) amazonensis infection. Parasitol. Res. 2008, 102:1025-1033.
33. 2 enzymes. J. Appl. Microbiol. 2007, 102:650-659.
34. Polgár J., Magnenat E.M., Peitsch M.C., Wells T.N., Clemetson K.J. Asp-49 is not an absolute prerequisite for the enzymic activity of low-M(r) phospholipase A2: purification, characterization and computer modelling of an enzymically active Ser-49 phospholiase A2, ecarpholin S, from the venom of Echis carinatus sochureki (saw-scaled viper). Biochem J 1996, 319:961-968.
35. 2 from Bothrops jararacussu venom. Protein J 2004, 23:273-285.
36. 2 from Bothrops neuwiedi puloensis snake venom. Toxicon 2004, 44:305-314.
37. 2. Antimicrob. Agents Chemother 2005, 49:1340-1345.
38. Schagger H., Von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal. Biochem 1987, 166:368-379.
39. 2 subunit of crotoxin from Crotalus durissus terrificus snake venom, on its enzymatic and pharmacological activities. Int. J. Biochem. Cell Biol. 2001, 33:877-888.
40. Stábeli R.S., Marcussi S., Carlos G.B., Pietro R.C., Slistre-de-araújo H.S., Giglio J.R., Oliveira E.B., Soares A.M. Platelet aggregation and antibacterial effects an l-amino acid oxidase purified from Bothrops alternatus snake venom. Bioorg. Med. Chem. 2004, 12:2881-2886.
41. 2 homologue: an example of function versatility of snake venom proteins. Comp. Biochem. Physiol. C Toxicol. Pharmacol 2006, 142:371-381.
42. Stiles B.G., Sexton F.W., Weinstein S.A. Antibacterial effects of different snake venoms: purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom. Toxicon 1991, 29:1129-1141.
43. Suhr S.M., Kim D.S. Identification of the snake venom substance that indices apoptosis. Biochem. Biophys. Res. Commun 1996, 224:134-139.
44. Takasuka H., Sakurai Y., Yoshioka A., Kokubo T., Usami Y., Suzuki M., Matsui T., Titani K., Yagi H., Matsumoto M., Fujimura Y. Molecular characterization of l-amino acid oxidase from Agkistrodon halys blomhoffii with special reference to platelet aggregation. Biochim. Biophys. Acta 2001, 1544:267-277.
45. Tempone A.G., Andrade H.F., Spencer P.J., Lourenço C.O., Rogero J.R., Nascimento N. Bothrops moojeni venom kills Leishmania spp. with hydrogen generated by its l-amino acid oxidase. Biochem. Biophys. Res. Commun 2001, 280:620-624.
46. Torii S., Naito M., Tsoruo T. Apoxin I, a novel apoptosis-inducing factor with l-amino acid oxidase activity purified form western diamondback rattlesnake venom. J. Biol. Chem. 1997, 272:9539-9542.
47. Torres A.M., Wong H.Y., Desai M., Moochhala S., Kuchel P.W., Kini R.M. Identification of a novel family of proteins in snake venoms. Purification and structural characterization of nawaprin from Naja nigricollis snake venom. J. Biol. Chem. 2003, 278:40097-40104.
48. Toyama M.H., Mancuso L.C., Giglio J.R., Novello J.C., Oliveira B., Marangoni S. A quick procedure for the isolation of dimeric piratoxins I and II, two myotoxins from Bothrops pirajai snake venom. N-terminal sequencing. Biochem. Mol. Biol. Int 1995, 37(6):1047-1055.
49. Toyama M.H., Carneiro E.M., Marangoni S., Amaral M.E.C., Velloso L.A., Boschero A.C. Isolation and characterization of a convulxin-like protein from Crotalus durissus collilineatus venom. J. Protein Chem. 2001, 20:585-591.
50. 2 isoform from Crotalus durissus terrificus venom. Toxicon 2003, 41:1033-1038.
51. Toyama M.H., Toyama D.O., Passero L.F.D., Laurenti M.D., Corbett C.E., Tomokane T.Y., Fonseca F.V., Antunes E., Joazeiro P.P., Beriam L.O.S., Martins A.M.C., Monteiro H.S.A., Fonteles M.C. Isolation of a new l-amino acid oxidase from Crotalus durissus cascavella venom. Toxicon 2006, 47:47-57.
52. Wei J.F., Wei Q., Lu Q.M., Tai H., Jin Y., Wang W.Y., Xiong Y.L. Purification, characterization and biological activity of l-amino acid oxidase from Trimeresurus mucrosquamatus venom. Acta Biochim. Biophys. Sin 2002, 35:219-224.
53. 2 from the venom of Bothrops pirajai. Acta Crystallogr. D Biol. Crystallogr 1999, 55:1229-1230.
54. 2 from Bungarus fasciatus venom. Peptides 2007, 28:969-973.