An acidic phospholipase A2 with antibacterial activity from Porthidium nasutum snake venom

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 161, Issue 4, 2012, Pages 341-347

  Vargas, Leidy Johana ^a   Londoño, Mónica ^a   Quintana, Juan Carlos ^a   Rua, Carolina ^a   Segura, Cesar ^a   Lomonte, Bruno ^b   Núñez, Vitelbina ^a  

^a UNIVERSIDAD DE ANTIOQUIA   (Colombia)

^b UNIVERSIDAD DE COSTA RICA   (Costa Rica)

Author keywords

Antibacterial activity; Porthidium nasutum; S. aureus; Snake venom

Indexed keywords

BACTERICIDE; PHOSPHOLIPASE A2; PNPLA2 PROTEIN; SNAKE VENOM; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BACTERICIDAL ACTIVITY; DRUG ISOLATION; ELECTROSPRAY; ELECTROSPRAY MASS SPECTROMETRY; HEMOLYSIS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; MOLECULAR WEIGHT; MOUSE; NONHUMAN; NORMAL HUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PORTHIDIUM NASUTUM; PRIORITY JOURNAL; SNAKE; STAPHYLOCOCCUS AUREUS; TANDEM MASS SPECTROMETRY;

MURINAE; PORTHIDIUM NASUTUM; STAPHYLOCOCCUS AUREUS; VIPERIDAE;

EID: 84857237218     PISSN: 10964959     EISSN: 18791107     Source Type: Journal    
DOI: 10.1016/j.cbpb.2011.12.010     Document Type: Article

References (49)

1. 2 from Bothrops jararacussu snake venom. Biochem. Pharmacol. 2002, 64:723-732.
2. 2 from Bothrops jararacussu. Toxicon 2008, 15:538-546.
3. 2 from Bothrops lanceolatus (fer de lance) venom: molecular and enzymatic properties. Toxicon 1994, 32:1069-1081.
4. 2-a structural review. Toxicon 1996, 34:827-841.
5. 2 and apoptosis. Biochim. Biophys. Acta 2006, 1761:1344-1350.
6. Bauer A.W., Kirby W.M., Sherris J.C., Turck M. Antibiotic susceptibility testing by a standardized single disk method. Am. J. Clin. Pathol. 1966, 45:493-496.
7. Burke A. Antibiotic resistance. Med. Clinic North Am 2000, 84:1407-1429.
8. 2 structure/function, mechanism, and signaling. J. Lipid Res. 2009, 50(Suppl):S237-S242.
9. Campbell J.A., Lamar W.W. Porthidium nasutum. The Venomous Reptiles of the Western Hemisphere 2004, vol. 1:468-469.
10. 2 isoforms: a perspective. Cell. Signal. 2003, 15:637-665.
11. 2 from the venom of Bothrops insularis (Jararaca ilhoa). Biochimie 2006, 88:1947-1959.
12. 2 from the venom of the snake Bothrops asper of Costa Rica: biochemical and toxicological characterization. Biochimie 2010, 92:273-283.
13. 2 isolated from Lachesis muta (Bushmaster) snake venom. Toxicon 2000, 38:961-972.
14. 2 isoenzyme isolated from Lachesis muta snake venom. Biochem. Pharmacol. 2002, 63:1589-1597.
15. 2 isolated from Lachesis muta snake venom. Comparison with lysophosphatidylcholine. Int. J. Biochem. Cell Biol. 2003, 35:1470-1481.
16. 2 Ba SpII RP4 of the Bothrops alternatus snake venom from Argentina. Toxicon 2010, 56:64-74.
17. Girón M.E., Estrella A., Sánchez E.E., Galán J., Tao W.A., Guerrero B., Salazar A.M., Rodríguez-Acosta A. Purification and characterization of a metalloproteinase, Porthidin-1, from the venom of Lansberg's hog-nosed pitvipers (Porthidium lansbergii hutmanni). Toxicon 2011, 57:608-618.
18. Gutiérrez J.M., Avila C., Rojas E., Cerdas L. Na alternative in vitro method for testing the potency of the polyvalent antivenom produced in Costa Rica. Toxicon 1988, 26:411-413.
19. 2 myotoxins from Bothrops snake venoms. Toxicon 1995, 33:1405-1424.
20. Hancock R., Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 1998, 16:82-88.
21. 2 from Bothrops leucurus (white-tailed-jararaca) snake venom. Biochimie 2006, 89:319-328.
22. 2 isolated from Porthidium hyoprora snake venom. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2011, 154:108-119.
23. 2 Enzymes: Structure 1997, 1-28. Function and Mechanism, Wiley, England. R.M. Kini (Ed.).
24. 2 enzymes. Toxicon 2003, 42:827-840.
25. Koh D.C., Armugam A., Jeyaseelan K. Snake venom components and their applications in biomedicine. Cell. Mol. Life Sci. 2006, 63:3030-3041.
26. 2. J. Biol. Chem. 2002, 277:5849-5857.
27. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
28. 12) cells in vitro. Toxicon 1999, 37:145-158.
29. 2 from snake venoms. Toxicon 2003, 42:307-312.
30. 2 homologues of snake venoms: biological activities and their possible adaptive roles. Protein Pept. Lett. 2009, 16:860-876.
31. 2 from Bothrops erythromelas venom: isolation, cloning and characterization as potent anti-platelet and inductor of prostaglandin I2 release by endothelial cells. Biochem. Pharmacol. 2006, 72:377-384.
32. NCCLS Performance standards for antimicrobial susceptibility testing, nineteenth informational supplement. Approved Standard M100-S19 National Committee for Clinical Standards. Wayne, PA, January 2009.
33. Nevalainen T.J., Graham G.G., Scott K.F. Actions of secreted phospholipases A2. Review. Biochim. Biophys. Acta 2008, 1781:1-9.
34. Nunes, D.C., Rodrigues, R.S., Lucena, M.N., Cologna, C.T., Oliveira, A.C., Hamaguchi, A., Homsi-Brandeburgo, MI., Arantes, E.C., Teixeira, D.N., Ueira-Vieira, C., Rodrigues, V.M., 2011. Isolation and functional characterization of proinflammatory acidic phospholipase A(2) from Bothrops leucurus snake venom. Comp Biochem Physiol C Toxicol Pharmacol.
35. 2 homologue from the venom of the snake Bothrops atrox. Toxicon 2004, 44:91-101.
36. 2 from Bothrops asper snake venom: synthetic Lys-49 myotoxin II-(115-129) peptide identifies its bactericidal region. Eur. J. Biochem. 1998, 53:452-461.
37. Pérez-Santos C., Moreno A.G. Monografie VI. Ofidios de Colombia. Museo regionale di scienze naturali. Torino 1988, 357.
38. 2 cDNA from Bothrops jararacussu venom gland. Protein Expr. Purif. 2004, 37:102-108.
39. 2 from Bothrops pauloensis snake venom. Toxicon 2007, 50:153-165.
40. 2 from the venom of Agkistrodon halys (Chinese pallas). Biochimie 2008, 90:1372-1388.
41. 2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal region. Toxicon 2005, 45:807-815.
42. 2, from the venom of the snake Bothrops jararaca: purification, primary structure analysis, and its characterization as a platelet-aggregation-inhibiting factor. Arch. Biochem. Biophys. 1999, 367:26-32.
43. 2 myotoxins from Bothrops snake venoms: structure-function relationship. Curr. Org. Chem. 2004, 8:1677-1690.
44. 2 homologue: an example of function versatility of snake venom proteins. Comp. Biochem. Physiol. C 2006, 142:371-381.
45. Stiles B., Sexton F., Weinstein S. 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.
46. Teixeira, S.S., Silveira, L.B., da Silva, F.M., Marchi-Salvador, D.P., Silva, F.P. Jr., Izidoro, L.F., Fuly, A.L., Juliano, M.A., Dos Santos, C.R., Murakami, M.T., Sampaio, S.V., da Silva, S.L., Soares, A.M., 2011. Molecular characterization of an acidic phospholipase A2 from Bothrops pirajai snake venom: synthetic C-terminal peptide identifies its antiplatelet region. Arch Toxicol.
47. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
48. WHO WHO global strategy for containment of antimicrobial resistance. Executive Summary. (Consulted on February 11 of 2008) 2001, http://whqlibdoc.who.int/hq/2001/WHO_CDS_CSR_DRS_2001.2a.pdf.
49. WHO Día Mundial de la Salud - 7 de abril de 2011. Resistencia a los antimicrobianos: si no actuamos hoy, no habrá cura mañana. (Consulted on April 10 of 2011) 2011, http://www.who.int/world-health-day/2011/es/index.html.