Neutralization of venom-induced hemorrhage by equine antibodies raised by immunization with a plasmid encoding a novel P-II metalloproteinase from the lancehead pitviper Bothrops asper

Vaccine

Volumn 27, Issue 3, 2009, Pages 460-466

  Arce Estrada, Viviana ^a   Azofeifa Cordero, Gabriela ^a   Estrada, Ricardo ^a   Alape Girón, Alberto ^a   Flores Díaz, Marietta ^a  

^a UNIVERSIDAD DE COSTA RICA   (Costa Rica)

Author keywords

Bothrops asper; DNA immunization; Gene Gun; Metalloproteinase; Therapeutic antivenom

Indexed keywords

ANTIBODY; INTERLEUKIN 2; INTERLEUKIN 6; METALLOPROTEINASE; METALLOPROTEINASE II; PLASMID VECTOR; SNAKE VENOM; TUNGSTEN; UNCLASSIFIED DRUG; VIPER VENOM;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIBODY PRODUCTION; ARTICLE; BLEEDING; BOTHROPS ASPER; CONTROLLED STUDY; CROSS REACTION; DNA IMMUNIZATION; HORSE; LACHESIS STENOPHRYS; MOLECULAR CLONING; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SNAKE; WESTERN BLOTTING;

AMINO ACID SEQUENCE; ANIMALS; ANTIDOTES; ANTIVENINS; BASE SEQUENCE; BOTHROPS; CLONING, MOLECULAR; CROTALID VENOMS; DNA, COMPLEMENTARY; HEMORRHAGE; HORSES; METALLOPROTEASES; MICE; MOLECULAR SEQUENCE DATA; NEUTRALIZATION TESTS; PLASMIDS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; VACCINES, DNA;

EID: 57649221923     PISSN: 0264410X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vaccine.2008.10.066     Document Type: Article

References (31)

1. Kasturiratne A, Wickremasinghe AR, de Silva N, Gunawardena NK, Pathmeswaran A, Premaratna R, Savioli L, Lalloo DG, de Silva HJ. 2008. The global burden of snakebite: A literature analysis and modelling based on regional estimates of envenoming and deaths. PLoS Med. 5:e218.
2. Gutiérrez J.M., Lomonte B., León G., Rucavado A., Chaves F., and Angulo Y. Trends in snakebite envenomation therapy: scientific, technological and public health considerations. Curr Pharm Des 13 (2007) 2935-2950
3. Serrano S.M., Shannon J.D., Wang D., Camargo A.C., and Fox J.W. A multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: an approach to understanding venom proteomics. Proteomics 5 (2005) 501-510
4. Harrison R.A., Moura-Da-Silva A.M., Laing G.D., Wu Y., Richards A., Broadhead A., et al. Antibody from mice immunized with DNA encoding the carboxyl-disintegrin and cysteine-rich domain (JD9) of the haemorrhagic metalloprotease, Jararhagin, inhibits the main lethal component of viper venom. Clin Exp Immunol 121 (2000) 358-363
5. Harrison R.A. Development of venom toxin-specific antibodies by DNA immunisation: rationale and strategies to improve therapy of viper envenoming. Vaccine 22 (2004) 1648-1655
6. Gutiérrez J.M., and Rucavado A. Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage. Biochimie 82 (2000) 841-850
7. Fox J.W., and Serrano S.M. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 45 (2005) 969-985
8. Gutiérrez J.M. Clinical toxicology of snake bites in Central America. In: Meier J., and White J. (Eds). Handbook of clinical toxicology of animal venoms and poisons (1995), CRC Press, Florida 645-665
9. Watanabe L., Shannon J.D., Valente R.H., Rucavado A., Alape A., Kamiguti A.S., et al. Amino acid sequence and crystal structure of BaPI, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue damaging activities. Protein Sci 12 (2003) 2273-2281
10. Loría G.D., Rucavado A., Kamiguti A.S., Theakston R.D., Fox J.W., Alape A., et al. Characterization of basparin A, a prothrombin activating metalloproteinase, from the venom of the snake Bothrops asper that inhibits platelet aggregation and induces defibrination and thrombosis. Arch Biochem Biophys 418 (2003) 13-24
11. Gutiérrez J.M., Romero M., Díaz C., Borkow G., and Ovadía M. Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper. Toxicon 33 (1995) 19-29
12. Franceschi A., Rucavado A., Mora N., and Gutiérrez J.M. Purification and characterization of BaH4, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper. Toxicon 38 (2000) 63-77
13. Altschul S.F., Gish W., Miller W., Myers E.W., and Lipman D.J. Basic local alignment search tools. J Mol Biol 215 (1990) 403-410
14. Higgins D.G., Thompson J.D., and Gidson T.J. Using CLUSTAL for multiple sequence alignments. Meth Enzymol 266 (1996) 383-402
15. Gutiérrez J.M., Gené J.A., Rojas G., and Cerdas L. Neutralization of proteolytic and hemorrhagic activities of Costa Rican snake venoms by a polyvalent antivenom. Toxicon 23 (1985) 887-893
16. Hooper N. Families of zinc metalloproteases. FEBS Lett 354 (1994) 1-6
17. Van Wart H., and Birkedal-Hansen E.H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci U S A 87 (1990) 5578-5582
18. Hite L., Jia L., Bjarnason J., and Fox J. cDNA Sequences for four snake venom metalloproteinases: structure, classification and their relationship to mammalian reproductive proteins. Arch Biochem Biophys 38 (1994) 182-191
19. Tsai I., Wang Y., and Lee Y. Characterization of a cDNA encoding the precursor of platelet aggregation inhibitor and metalloproteinase from Trimeresurus mucrosquamatus venom. Biochem Biophys Acta 1200 (1994) 337-340
20. Kang I.C., Chung K.H., Lee S.J., Yun Y., Moon H.M., and Kim D.S. Purification and molecular cloning of a platelet aggregation inhibitor from the snake Agkistrodon halys brevicaudus venom. Thromb Res 91 (1998) 65-73
21. Takeya H., Nishida S., Nishino N., Makinose Y., Omori-Satoh T., Nikai T., et al. Primary structures of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhagic metalloproteinases and new fluorogenic peptide substrates for these enzymes. J Biochem 113 (1993) 473-483
22. Dennis M.S., Henzel W.J., Pitti R.M., Lipari M.T., Napier M.A., Deisher T.A., et al. Platelet glycoprotein IIb-IIIa protein antagonists from snake venoms: evidence for a family of platelet-aggregation inhibitors. Proc Natl Acad Sci U S A 87 (1990) 2471-2475
23. Scaloni A., Di Martino E., Miraglia N., Pelagalli A., Della Morte R., Stalano N., et al. Amino acid sequence and molecular modeling of glycoprotein IIb/IIIa and fibronectin receptor iso-antagonists from Trimeresurus elegans venom. Biochem J 319 (1996) 775-782
24. Alape-Girón A, Sanz L, Escolano J, Flores-Díaz M, Madrigal M, Sasa M, Calvete JJ. Snake venomics of the lancehead pitviper Bothrops asper: geographic, individual, and ontogenetic variations. J Proteome Res, 7:3556-71.
25. Chow Y.H., Chiang B.L., Chi W.K., Lin W.C., Chen Y.T., and Tao M.H. Development of Th1 and Th2 populations and the nature of immune responses to Hepatitis B virus DNA vaccines can be modulated by codelivery of various cytokine genes. J Immunol 160 (1998) 1320-1329
26. Xin K.Q., Hamajima K., Sasaki S., Honsho A., Tsuji T., Ishii N., et al. Intranasal administration of human immunodeficiency virus type-1(HIV-1) DNA vaccine with interleukin-expression plasmid enhances cell-mediated immunity against HIV-1. Immunology 94 (1998) 438-444
27. Larsen D., Dybdahl N., McGregor M., Drape R., Neumann V., Swain W., et al. Coadministration of DNA encoding interleukin-6 and hemagglutinin confers protection from influenza virus challenge in mice. J Virol 72 (1998) 1704-1708
28. Harrison R.A., Richards A., Laing G.D., and Theakston R.D.G. Simultaneous GeneGun immunization with plasmid encoding antigen and GM-CSF: significant enhancement of murine antivenom IgG1 titres. Vaccine 20 (2002) 1702-1706
29. Olsen C.W. DNA vaccination against influenza viruses: a review with emphasis on equine and swine influenza. Vet Microbiol 74 (2000) 149-164
30. Rucavado A., Borkow G., Ovadia M., and Gutiérrez J.M. Immunological studies on BaH1 and BaP1, two hemorrhagic metalloproteinases from the venom of the snake Bothrops asper. Toxicon 33 (1995) 1103-1106
31. Borkow G., Gutiérrez J.M., and Ovadia M. Isolation and characterization of synergistic hemorrhagins from the venom of the snake Bothrops asper. Toxicon 31 (1993) 1137-1150