Complementary DNA sequencing and identification of mRNAs from the venomous gland of Agkistrodon piscivorus leucostoma

Toxicon

Volumn 51, Issue 8, 2008, Pages 1457-1466

  Jia, Ying ^a   Cantu, Bruno A ^a   Sánchez, Elda E ^a   Pérez, John C ^a  

^a TEXAS A AND M UNIVERSITY KINGSVILLE   (United States)

Author keywords

Agkistrodon piscivorus leucostoma; cDNA library; ESTs; Phospholipase A2; Venoms

Indexed keywords

COMPLEMENTARY DNA; MESSENGER RNA; PHOSPHOLIPASE A; SNAKE VENOM;

AGKISTRODON; AGKISTRODON PISCIVORUS LEUCOSTOMA; AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DNA SEQUENCE; EXPRESSED SEQUENCE TAG; GENE EXPRESSION; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION; UNINDEXED SEQUENCE;

AGKISTRODON; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; CROTALID VENOMS; DNA, COMPLEMENTARY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; EXPRESSED SEQUENCE TAGS; GENE LIBRARY; MOLECULAR SEQUENCE DATA; PHOSPHOLIPASES A; RNA, MESSENGER; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA;

AGKISTRODON PISCIVORUS LEUCOSTOMA;

EID: 44649183300     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2008.03.028     Document Type: Article

References (47)

1. Adams M.D., Kelley J.M., Gocayne J.D., Dubnick M., Polymeropoulos M.H., Xiao H., Merryl C.R., Wu A., Olde B., Moreno R.F., Kerlavage A.R., McCombie W.R., and Venter J.C. Complementary DNA sequencing: expressed sequence tags and human genome project. Science 252 (1991) 1651-1656
2. Aird S.D. Ophidian envenomation strategies and the role of the purines. Toxicon 40 (2002) 335-393
3. Altschul S.F., Madden T.L., Schaffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 (1997) 3389-3402
4. Baravoma E.N., Shannon J.D., Bjarnason J.B., and Fox J.W. Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases. Arch. Biochem. Biophys. 275 (1989) 63-71
5. Beghini D.G., Damico D.C., da Cruz-Höfling M.A., Rodrigues-Simioni L., Delatorre M.C., Hyslop S., and Marangoni S. Ability of rabbit antiserum against crotapotin to neutralize the neurotoxic, myotoxic and phospholipase A2 activities of crotoxin from Crotalus durissus cascavella snake venom. Toxicol. In Vitro 22 (2008) 240-248
6. Bieber A.l. Metal and nonpretein constituents in snake venoms. In: Lee C.Y. (Ed). Snake Venoms, Handbook of Exp. Pharmacol vol. 52 (1979), Springer, Berlin 295-306
7. Chippaux J.P., Williams V., and White J. Snake venom variability: methods of study, results and interpretation. Toxicon 29 (1991) 1279-1303
8. Daltry J.C., Wuster W., and Thorpe R.S. Diet and snake venom evolution. Nature 379 (1996) 537-540
9. Deshimaru M., Ogawa T., Nakashima K., Nobuhisa I., Chijiwa T., Shimohigashi Y., Fukumaki Y., Niwa M., Yamashina I., Hattori S., and Ohno M. Accelerated evolution of crotalinae snake venom gland serine proteases. FEBS Lett. 397 (1996) 83-88
10. Francischetti I.M.B., My-Pham V., Harrison J., Garfield M.K., and Ribeiro J.M.C. Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the full-length transcripts (cDNA) and proteins. Gene 337 (2004) 55-69
11. Fuly A.L., Machado O.L., Alves E.W., and Carlini C.R. Mechanism of inhibitory action on platelet activation of a phospholipase A2 isolated from Lachesis muta (Bushmaster) snake venom. Thromb. Haemost. 78 (1997) 1372-1380
12. Gutierrez J.M., and Rucavado A. Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage. Biochimie 82 (2000) 841-850
13. Gutiérrez J.M., Ponce-Soto L.A., Marangoni S., and Lomonte B. Systemic and local myotoxicity induced by snake venom group II phospholipases A2: comparison between crotoxin, crotoxin B and a Lys49 PLA2 homologue. Toxicon 51 (2008) 80-92
14. Hodgson W.C., and Wickramaratna J.C. In vitro neuromuscular activity of snake venoms. Clin. Exp. Pharmacol. Physiol. 29 (2002) 807-814
15. 2 from the venom of the cottonmouth snake at 2.0-Å resolution. J. Biol. Chem. 265 (1990) 17649-17656
16. Huang T.-F., Sheu J.-R., and Teng C.-M. Mechanism of action of a potent antiplatelet peptide, triflavin from Trimeresurus flavoviridis snake venom. Thromb. Haemost. 66 (1991) 489-493
17. John T.R., Smith L.A., and Kaiser I.I. Genomic sequences encoding the acidic and basic subunits of Mojave toxin: unusually high sequence identity of non-coding regions. Gene 139 (1994) 229-234
18. Junqueira-de-Azevedo I.L.M., and Ho P.L. A survey of gene expression and diversity in the venom glands of the pitviper snake Bothrops insularis through the generation of expressed sequence tags (ESTs). Gene 299 (2002) 279-291
19. Karlsson E. Chemistry of protein toxins in snake venoms. In: Lee C.Y. (Ed). Snake Venoms, Handbook of Exp. Pharm. vol. 52 (1979), Springer, Berlin 159-212
20. 2. Biochimie 86 (2004) 211-219
21. Lizano S., Domont G., and Perales J. Natural phospholipase A2 myotoxin inhibitor proteins from snakes, mammals and plants. Toxicon 42 (2003) 963-977
22. Markland F.S. Snake venoms and the hemostatic system. Toxicon 36 (1998) 1749-1800
23. Nakashima K., Nobuhisa I., Deshimaru M., Nakai M., Ogawa T., Shimohigashi Y., Fukumaki Y., Hattori M., Sakaki Y., Hattori S., and Ohno M. Accelerated evolution in the protein-coding regions is universal in crotalinae snake venom gland phospholipase A2 isozyme genes. Proc. Natl. Acad. Sci. USA 92 (1995) 5602-5609
24. Narendra Sharath Chandra J.N., Ponnappa K.C., Sadashiva C.T., Priya B.S., Nanda B.L., Gowda T.V., Vishwanath B.S., and Rangappa K.S. Chemistry and structural evaluation of different phospholipase A2 inhibitors in arachidonic acid pathway mediated inflammation and snake venom toxicity. Curr. Top. Med. Chem. 7 (2007) 787-800
25. Newman T., de Bruijn F.J., Green P., Keegstra K., Kende H., Mcintosh L., Ohlrogge J., Raikhel N., Somerville S., Thomashow M., Retzel E., and Somerville C. Genes galore: a summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones. Plant Physiol. 106 (1994) 1241-1255
26. Niewiarowski S., Huang T.F., Rucinski B., Cook J.J., Williams J.A., Musial J., Edumunds Jr. L.H., Bush L., Shebuski R., and Friedman P.A. Potential application of RGD containing peptides from viper venoms (disintegrins) in antiplatelet therapy. Thromb. Haemost. 62 (1989) 319-329
27. Pahari S., Mackessy S.P., and Kini R.M. The venom gland transcriptome of the Desert Massasauga Rattlesnake (Sistrurus catenatus edwardsii): towards an understanding of venom composition among advanced snakes (Superfamily Colubroidea). BMC Mol. Biol. 8 (2007) 115-131
28. 2-II from Agkistrodon halys pallas. Biochim. Biophys. Acta 1431 (1999) 157-165
29. Perez J.C., and Sanchez E.E. Natural protease inhibitors to hemorrhagins in snake venoms and their potential use in medicine. Toxicon 37 (1990) 703-728
30. Pungercar J., and Krizaj I. Understanding the molecular mechanism underlying the presynaptic toxicity of secreted phospholipases A2. Toxicon 50 (2007) 871-892
31. Rosenberg P. Phospholipases. In: Shier W.T., and Mebs D. (Eds). Handbook of Toxinology (1991), Marcel Dekker, New York 67-277
32. Rossetto O., Rigoni M., and Montecucco C. Different mechanism of blockade of neuroexocytosis by presynaptic neurotoxins. Toxicol Lett. 149 (2004) 91-101
33. Rounsley S.D., Glodek A., Sutton G., Adams M.D., Somerville C.R., Venter J.C., and Kerlavage A.R. The construction of Arabidopsis expressed sequence tag assemblies. Plant Physiol. 112 (1996) 1177-1183
34. Selistre H.S., and Ownby C.L. Molecular cloning and sequence analysis of cDNAs for metalloproteinases from broad-banded copperhead Agkistrodon contortrix laticinctus. Arch. Biochem. Biophys. 320 (1995) 141-148
35. Takatsuka H., Sakurai Y., Yoshioka A., Kokubo T., Usami Y., Suzuki M., Matsui T., Titani K., Yagi H., Matsumoto M., and Fujimura Y. Molecular characterization of L-amino acid oxidase from Agkistrodon halys blomhoffii with special reference to platelet aggregation. Biochim. Biophys. Acta 1544 (2001) 267-277
36. Thimmegowda N.R., Dharmappa K.K., Kumar C.S., Sadashiva M.P., Sathish A.D., Nanda B.L., Vishwanath B.S., and Rangappa K.S. Synthesis and evaluation of tricyclic dipyrido diazepinone derivatives as inhibitors of secretory phospholipase A2 with anti-inflammatory activity. Curr. Top. Med. Chem. 7 (2007) 811-820
37. Thomas R.G., and Pough F.H. The effect of rattlesnake venom on digestion of prey. Toxicon 17 (1979) 221-228
38. Tomoo K., Ohishi H., Doi M., Ishida T., Inoue M., Ikeda K., Hata Y., and Samejima Y. Structure of acidic phospholipase A2 for the venom of Agkistrodon halys blomhoffii at 2.8 A resolution. Biochem. Biophys. Res. Commun. 184 (1992) 137-143
39. 2 from Callosellasma rhodostoma venom gland. Eur. J. Biochem. 267 (2000) 6684-6691
40. Tsai I.H., Wang Y.M., Chen Y.H., and Tu A.T. Geographic variations, cloning, and functional analyses of the venom acidic phospholipases A(2) of Crotalus viridis viridis. Arch. Biochem. Biophys. 411 (2003) 289-296
41. Tsetlin V. Snake venom alpha-neurotoxins and other 'three-finger' proteins. Eur. J. Biochem. 264 (1999) 281-286
42. Tu A.T. Reptile Venoms and Toxins, Handbook of Natural Toxins vol. 5 (1991), Marcel Dekker, New York pp. 107-145
43. 2?. Biochimie 82 (2000) 815-831
44. 1 integrin-binding motifs in venom metalloproteinases and a new group of putative toxins, renin-like aspartic proteases. Gene 377 (2006) 21-32
45. Welches W., Reardon I., and Heinrikson R.L. An examination of structural interactions presumed to be of importance in the stabilization of phospholipase A2 dimers based upon comparative protein sequence analysis of a monomeric and dimeric enzyme from the venom of Agkistrodon p. piscivorus. J. Protein Chem. 12 (1993) 187-193
46. Zhang Y., Gao R., Lee W.H., Zhu S.W., Xiong Y.L., and Wang W.Y. Characterization of a fibrinogen-clotting enzyme from Trimeresurus stejnegeri venom, and comparative study with other venom proteases. Toxicon 36 (1998) 131-142
47. Zhang B., Liu Q.H., Yin W., Zhang X.W., Huang Y.J., Luo Y.F., Qiu P.X., Su X.W., Yu J., Hu S.N., and Yan G.M. Transcriptome analysis of Deinagkistrodon acutus venomous gland focusing on cellular structure and functional aspects using expressed sequence tags. BMC Genom. 7 (2006) 152-162