Identification of alpha-bungarotoxin (A31) as the major postsynaptic neurotoxin, and complete nucleotide identity of a genomic DNA of Bungarus candidus from Java with exons of the Bungarus multicinctus alpha-bungarotoxin (A31) gene

Toxicon

Volumn 42, Issue 4, 2003, Pages 381-390

  Kuch, Ulrich ^a   Molles, Brian E ^b,e   Omori Satoh, Tamotsu ^c   Chanhome, Lawan ^c   Samejima, Yuji ^d   Mebs, Dietrich ^a  

^a UNIVERSITY HOSPITAL FRANKFURT   (Germany)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c THAI RED CROSS AIDS RESEARCH CENTRE   (Thailand)

^d HOSHI UNIVERSITY   (Japan)

^e INSTITUT PASTEUR   (France)

Author keywords

Alpha bungarotoxin; Bungarus multicinctus; Cytochrome b; Genomic DNA sequence; Malayan krait; Many banded krait; Mitochondrial DNA; Molecular evolution; Postsynaptic neurotoxins; Reptilia: Squamata: Elapidae: Bungarus candidus; Snake venom

Indexed keywords

ALPHA BUNGAROTOXIN; CYTOCHROME B; GENOMIC DNA; MITOCHONDRIAL DNA; NEUROTOXIN; NICOTINIC RECEPTOR; NUCLEOTIDE; SIGNAL PEPTIDE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DNA SEQUENCE; EXON; FEMALE; INTRON; LETHAL DOSE; MALE; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENY; POSTSYNAPTIC MEMBRANE; PRIORITY JOURNAL; RECEPTOR BINDING; SEQUENCE ANALYSIS; SNAKE;

BUNGARUS; BUNGARUS CANDIDUS; BUNGARUS FASCIATUS; BUNGARUS MULTICINCTUS; ELAPIDAE; REPTILIA; SERPENTES; SQUAMATA;

EID: 0141560247     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(03)00168-5     Document Type: Article

References (55)

1. Ackermann E.J., Taylor P. Nonidentity of the alpha-neurotoxin binding sites on the nicotinic acetylcholine receptor revealed by modification in alpha-neurotoxin and receptor structures. Biochemistry. 36:1997;12836-12844.
2. Afifiyan F., Armugam A., Tan C.H., Gopalakrishnakone P., Jeyaseelan K. Postsynaptic alpha-neurotoxin gene of the spitting cobra, Naja naja sputatrix: structure, organization, and phylogenetic analysis. Genome Res. 9:1999;259-266.
3. Blount P., Merlie J.P. Native folding of an acetylcholine receptor alpha subunit expressed in the absence of other receptor subunits. J. Biol. Chem. 263:1988;1072-1080.
4. Buonanno A., Mudd J., Merlie J.P. Isolation and characterization of the beta and epsilon subunit genes of mouse muscle acetylcholine receptor. J. Biol. Chem. 264:1989;7611-7616.
5. Campbell, B.N., 1997. Molecular phylogenetics and the Boidae (Serpentes: Booidea). PhD dissertation, Queen's University, Kingston, Canada.
6. Chang C.C. The action of snake venoms on nerve and muscle. Lee C.-Y. Snake Venoms. 1979;309-376 Springer, Berlin.
7. Chang Y.S., Huang F.L., Lo T.B. The complete nucleotide sequence and gene organization of carp (Cyprinus carpio) mitochondrial genome. J. Mol. Evol. 38:1994;138-155.
8. Chang L.S., Chou Y.C., Lin S.R., Wu B.N., Lin J., Hong E., Sun Y.J., Hsiao C.D. A novel neurotoxin, cobrotoxin b, from Naja naja atra (Taiwan cobra) venom: purification, characterization and gene organization. J. Biochem. (Tokyo). 122:1997;1252-1259.
9. Chang L.S., Lin J., Chou Y.C., Hong E. Genomic structures of cardiotoxin 4 and cobrotoxin from Naja naja atra (Taiwan cobra). Biochem. Biophys. Res. Commun. 239:1997;756-762.
10. Chang L.S., Lin S.K., Huang H.B., Hsiao M. Genetic organization of α-bungarotoxins from Bungarus multicinctus (Taiwan banded krait): evidence showing that the production of α-bungarotoxin isotoxins is not derived from edited mRNAs. Nucleic Acids Res. 27:1999;3970-3975.
11. Chippaux J.-P., Williams V., White J. Snake venom variability: methods of study, results and interpretation. Toxicon. 29:1991;1279-1303.
12. 2 isozymes. Toxicon. 38:2000;449-462.
13. Deshimaru M., Ogawa T., Nakashima K., Nobuhisa I., Chijiwa T., Shimohigashi Y., Fukumaki Y., Niwa M., Yamashina I., Hattori S., Ohno M. Accelerated evolution of crotalinae snake venom gland serine proteases. FEBS Lett. 397:1996;83-88.
14. 2 genes. Gene. 292:2002;225-231.
15. Gardner P.D. Nucleotide sequence of the epsilon-subunit of the mouse muscle nicotinic acetylcholine receptor. Nucleic Acids Res. 18:1990;6714.
16. Isenberg K.E., Mudd J., Shah V., Merlie J.P. Nucleotide sequence of the mouse muscle nicotinic acetylcholine receptor alpha subunit. Nucleic Acids Res. 14:1986;5111.
17. Iwamatsu A. S-carboxymethylation of proteins transferred onto polyvinylidene difluoride membranes followed by in situ protease digestion and amino acid microsequencing. Electrophoresis. 13:1992;142-147.
18. Keller S.H., Kreienkamp H.-J., Kawanishi C., Taylor P. Molecular determinants conferring alpha-toxin resistance in recombinant DNA-derived acetylcholine receptors. J. Biol. Chem. 270:1995;4165-4171.
19. Kocher T.D., Thomas W.K., Meyer A., Edwards S.V., Pääbo S., Villablanca F.X., Wilson A.C. Dynamics of mitochondrial DNA evolution in animals: amplification and sequencing with conserved primers. Proc. Natl. Acad. Sci. USA. 86:1989;6196-6200.
20. Kopstein F. Die Giftschlangen Javas und ihre Bedeutung für den Menschen. Zeitschrift für Morphologie und Ökologie der Tiere. 19:1930;339-363.
21. Kopstein F. Herpetologische Notizen V, Bungarus javanicus, eine neue Giftschlange von Java. Treubia. 14:1932;73-77.
22. Kosen P.A., Finer-Moore J., McCarthy M.P., Basus V.J. Structural studies of α-bungarotoxin. 3. Corrections in the primary sequence and X-ray structure and characterization of an isotoxic α-bungarotoxin. Biochemistry. 27:1988;2775-2781.
23. Kreienkamp H.-J., Sine S.M., Maeda R.K., Taylor P. Glycosylation sites selectively interfere with alpha-toxin binding. J. Biol. Chem. 269:1994;8108-8114.
24. Kuch, U., Stuart, B.L., in press. A review of the kraits of Laos, with range extensions for the Malayan krait, Bungarus candidus (Linnaeus 1758). Salamandra.
25. Kuch U., Pfenninger M., Bahl A. Laundry detergent effectively preserves amphibian and reptile blood and tissue for DNA isolation. Herpetol. Rev. 30:1999;80-82.
26. Kuhn P., Deacon A.M., Comoso S., Rajaseger G., Kini R.M., Uson I., Kolatkar P.R. The atomic resolution structure of bucandin, a novel toxin isolated from the Malayan krait, determined by direct methods. Acta Crystallogr. D: Biol. Crystallogr. 56:2000;1401-1407.
27. Lachumanan R., Armugam A., Tan C.-H., Jeyaseelan K. Structure and organization of the cardiotoxin genes in Naja naja sputatrix. FEBS Lett. 433:1998;119-124.
28. 4. Nature. 227:1970;680-685.
29. Laothong C., Sitprija V. Decreased parasympathetic activities in Malayan krait (Bungarus candidus) envenoming. Toxicon. 39:2001;1353-1357.
30. LaPolla R.J., Mayne K.M., Davidson N. Isolation and characterization of a cDNA clone for the complete protein coding region of the delta subunit of the mouse acetylcholine receptor. Proc. Natl. Acad. Sci. USA. 81:1984;7970-7974.
31. Lee B.S., Gunn R.B., Kopito R.R. Functional differences among nonerythroid anion exchangers expressed in a transfected human cell line. J. Biol. Chem. 266:1991;11448-11454.
32. Liu L.F., Chang C.C., Liau M.Y., Kuo K.W. Genetic characterization of the mRNAs encoding α-bungarotoxin: isoforms and RNA editing in Bungarus multicinctus gland cells. Nucleic Acids Res. 26:1998;5624-5629.
33. Looareesuwan S., Viravan C., Warrell D.A. Factors contributing to fatal snake bite in the rural tropics: analysis of 46 cases in Thailand. Trans. R. Soc. Trop. Med. Hyg. 82:1988;930-934.
34. Marinetti G.V. The action of phospholipase A on lipoproteins. Biochim. Biophys. Acta. 98:1965;554-565.
35. Mebs D. Toxicity in animals. Trends in evolution? Toxicon. 39:2001;87-96.
36. Mebs D., Narita K., Iwanaga S., Samejima Y., Lee C.Y. Amino acid sequence of α-bungarotoxin from the venom of Bungarus multicinctus. Biochem. Biophys. Res. Commun. 44:1971;711-716.
37. Mebs D., Narita K., Iwanaga S., Samejima Y., Lee C.Y. Purification, properties and amino acid sequence of α-bungarotoxin from the venom of Bungarus multicinctus. Hoppe-Seyler's Z. Physiol. Chem. 353:1972;243-262.
38. Molles B.E., Rezai P., Kline E.F., McArdle J.J., Sine S.M., Taylor P. Identification of residues at the alpha and epsilon subunit interfaces mediating species selectivity of Waglerin-1 for nicotinic acetylcholine receptors. J. Biol. Chem. 277:2002;5433-5440.
39. 2 isozyme genes. Proc. Natl. Acad. Sci. USA. 92:1995;5605-5609.
40. Ohno M., Ménez R., Ogawa T., Danse J.M., Shimohigashi Y., Fromen J., Ducancel F., Zinn-Justin S., Le Du M.H., Boulain J.-C., Tamiya T., Ménez A. Molecular evolution of snake toxins: is the functional diversity of snake toxins associated with a mechanism of accelerated evolution? Moldave K. Progress in Nucleic Acid Research and Molecular Biology. vol. 59:1998;307-364 Academic Press, New York.
41. Ohta M., Ohta K., Nishitani H., Hayashi K. Primary structure of α-bungarotoxin. Six amino acid residues differ from the previously reported sequence. FEBS Lett. 222:1987;79-82.
42. Pizzi M. Sampling variation of the fifty per cent end point, determined by the Reed-Muench (Behrens) method. Hum. Biol. 22:1950;151-190.
43. Pukrittayakamee S., Warrell D.A., Desakorn V., McMichael A.J., White N.J., Bunnag D. The hyaluronidase activities of some Southeast Asian snake venoms. Toxicon. 26:1988;629-637.
44. de Queiroz A., Lawson R., Lemos-Espinal J.A. Phylogenetic relationships of North American garter snakes (Thamnophis) based on four mitochondrial genes: How much DNA sequence is enough? Mol. Phylogenet. Evol. 22:2002;315-329.
45. Reed L.J., Muench H. A simple method of estimating fifty per cent endpoints. Am. J. Hyg. 27:1938;493-497.
46. Sine S.M. Molecular dissection of subunit interfaces in the acetylcholine receptor: identification of residues that determine curare selectivity. Proc. Natl. Acad. Sci. USA. 90:1993;9436-9440.
47. Sine S.M., Claudio T. Stable expression of the mouse nicotinic acetylcholine receptor in mouse fibroblasts. J. Biol. Chem. 266:1991; 13679-13689.
48. Sine S., Taylor P. Functional consequences of agonist-mediated state transitions in the cholinergic receptor. Studies in cultured muscle cells. J. Biol. Chem. 254:1979;3315-3325.
49. Slowinski J.B., Keogh S. Phylogenetic relationships of elapid snakes based on cytochrome b mtDNA sequences. Mol. Phylogenet. Evol. 15:2000;157-164.
50. Tan N.-H., Poh C.-H., Tan C.-S. The lethal and biochemical properties of Bungarus candidus (Malayan krait) venom and venom fractions. Toxicon. 27:1989;1065-1070.
51. Torres A.M., Kini R.M., Selvanayagam N., Kuchel P.W. NMR structure of bucandin, a neurotoxin from the venom of the Malayan krait (Bungarus candidus). Biochem. J. 360:2001;539-548.
52. 2 from the venom glands of Bungarus candidus: cloning and sequence-comparison. Toxicon. 40:2002;1363-1367.
53. Viravan C., Looareesuwan S., Kosakarn W., Wuthiekanun V., McCarthy C.J., Stimson A.F., Bunnag D., Harinasuta T., Warrell D.A. A national hospital-base survey of snakes responsible for bites in Thailand. Trans. R. Soc. Trop. Med. Hyg. 86:1992;100-106.
54. Warrell D.A. WHO/SEARO guidelines for the clinical management of snake bites in the Southeast Asian region. Southeast Asian J. Trop. Med. Public Health. 30:(Suppl 1):1999;1-85.
55. Warrell D.A., Looareesuwan S., White N.J., Theakston R.D.G., Warrell M.J., Kosakarn W., Reid H.A. Severe neurotoxic envenoming by the Malayan krait Bungarus candidus (Linnaeus): response to antivenom and anticholinesterase. Br. Med. J. 286:1983;678-680.