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MeSH Review

Bungarus

 
 
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Disease relevance of Bungarus

  • These observations confirm the importance of neurotoxic symptoms following bites by these species but also suggest a contributory role of generalized rhabdomyolysis in krait victims and emphasize the problem of severe local tissue necrosis in cobra victims [1].
  • The drug 3,4-diaminopyridine (DAP) is effective in other presynaptic paralytic conditions and was therefore tried in anaesthetized rabbits with respiratory paralysis induced by krait (Bungarus fasciatus) venom [2].
  • Brain death confirmed by Tc(99m) DTPA scan in a case of subarachnoid haemorrhage following a krait bite [3].
 

High impact information on Bungarus

  • These receptors are activated by acetylcholine and nicotine and are blocked by Bungarus toxin 3 [4].
  • Inhibition of neuronal acetylcholine sensitivity by alpha-toxins from Bungarus multicinctus venom [5].
  • The effects of alpha-toxins from Bungarus multicinctus (alpha BuTX) and Naja naja siamensis (alpha NTX) were studied on synaptic responses and on extrasynaptic responses to focally applied acetylcholine (ACh), histamine (Hm), gamma-aminobutyric acid (GABA), and glutamate (glu) in neurons of the marine mollusc, Aplysia californica [6].
  • Using CAT constructs, we found that a DNA fragment from the Bungarus AChE gene stimulates expression of the reporter protein, whereas a homologous fragment from the rat AChE gene had no influence [7].
  • The venom of the snake Bungarus fasciatus contains a hydrophilic, monomeric species of acetylcholinesterase (AChE), characterized by a C-terminal region that does not resemble the alternative T- or H-peptides [8].
 

Biological context of Bungarus

  • Thus, the Bungarus AChE gene possesses alternatively spliced T and S exons but no H exon; the absence of an H exon may be a common feature of AChE genes in reptiles and birds [8].
  • As deduced from cDNA clones, the catalytic domain of Bungarus fasciatus venom acetylcholinesterase (AChE) is highly homologous to those of other AChEs [9].
  • The NAD glycohydrolase from Bungarus fasciatus venom was less sensitive to inhibition by ADP-HPD, exhibiting an IC50 of 260 microM [10].
  • The nicotinic acetylcholine receptor (nAChR) carries two binding sites for snake venom neurotoxins. alpha-Bungarotoxin from the Southeast Asian banded krait, Bungarus multicinctus, is a long neurotoxin which competitively blocks the nAChR at the acetylcholine binding sites in a relatively irreversible manner [11].
  • The kinetics of thermal inactivation of acetylcholinesterase from the venom of the snake, Bungarus fasciatus, were studied at 45-54 degrees C. An Arrhenius plot reveals an activation energy of 113 kcal/mol [12].
 

Anatomical context of Bungarus

  • The neurotoxic phospholipase A(2), beta-bungarotoxin (beta-BuTx), is a component of the snake venom from the Taiwanese banded krait Bungarus multicinctus. beta-BuTx affects presynaptic nerve terminal function of the neuromuscular junction and induces widespread neuronal cell death throughout the mammalian and avian CNS [13].
  • Ceruleotoxin, a toxin component of Bungarus caeuleus venom, blocks in vivo the depolarisation caused by carbamylcholine on the isolated electroplaque from Electrophorus electricus and in vitro in increase of 22Na+ and 42K+ efflux caused by cholinergie agonists on excitable receptor-rich microsacs prepared from Torpedo marmorata electric organ [14].
  • The production of human AChE in transfected COS cells was increased nearly 2-fold with this modified construct, but still remained about 4-fold smaller than that of Bungarus AChE [15].
 

Associations of Bungarus with chemical compounds

  • Adenosine diphosphoribose transfer reactions catalyzed by Bungarus fasciatus venom NAD glycohydrolase [16].
  • Reactions catalyzed by purified Bungarus fasciatus venom NAD glycohydrolase were demonstrated to include ADP-ribose transfer from NAD to alcohols and to imidazole derivatives to produce a variety of ADP-ribosides [16].
  • The NAD glycohydrolase (NADase) (EC 3.2.2.5) from Bungarus fasciatus (banded krait) venom was purified (1000-fold) to electrophoretic homogeneity through a 3-step purification procedure, the last step being affinity chromatography on Cibacron blue agarose [17].
  • The recombinant Bungarus AChE, like the natural venom enzyme, showed a distinctive ladder pattern in nondenaturing electrophoresis, probably reflecting a variation in the number of sialic acids [9].
  • beta-Bungarotoxin (beta-BTX) isolated from the venom of Bungarus multicinctus has previously been reported to be a neurotoxic protein [18].
 

Gene context of Bungarus

  • Wild-type human AChE and its mutants Y337G and Y337W, as well as wild-type Bungarus fasciatus AChE and its mutants Y333G, Y333A and Y333W were studied [19].
  • Identification of a novel type of alternatively spliced exon from the acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of acetylcholinesterase in the snake liver and muscle [8].
  • We also observed a thioredoxin-specific reduction with other disulfide proteins of venom from Bungarus multicinctus, scorpion (Androctonus australis), and bee (Apis mellifera) [20].
  • However, modification of the conserved Trp-19 did not cause a precipitous drop in the enzymatic activity of Oh-DE-2 as observed with PLA2S from Naja naja atra and Bungarus multicinctus venoms [21].
  • Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of cooh-terminal domain; involvement of a positively charged residue in the peripheral site [9].
 

Analytical, diagnostic and therapeutic context of Bungarus

References

  1. Envenoming by the common krait (Bungarus caeruleus) and Sri Lankan cobra (Naja naja naja): efficacy and complications of therapy with Haffkine antivenom. Theakston, R.D., Phillips, R.E., Warrell, D.A., Galagedera, Y., Abeysekera, D.T., Dissanayaka, P., de Silva, A., Aloysius, D.J. Trans. R. Soc. Trop. Med. Hyg. (1990) [Pubmed]
  2. 3,4-Diaminopyridine reverses respiratory paralysis induced by a presynaptically active snake venom and its major neurotoxin. Watt, G., Smith, C.D., Kaewsupo, A., Davis, T.M. Trans. R. Soc. Trop. Med. Hyg. (1994) [Pubmed]
  3. Brain death confirmed by Tc(99m) DTPA scan in a case of subarachnoid haemorrhage following a krait bite. Balasuriya, B.M., Nanayakara, D., Goonasekara, C.D. The Ceylon medical journal. (2005) [Pubmed]
  4. Functional expression of two neuronal nicotinic acetylcholine receptors from cDNA clones identifies a gene family. Boulter, J., Connolly, J., Deneris, E., Goldman, D., Heinemann, S., Patrick, J. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  5. Inhibition of neuronal acetylcholine sensitivity by alpha-toxins from Bungarus multicinctus venom. Ravdin, P.M., Berg, D.K. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  6. Snake alpha-toxin effects on cholinergic and noncholinergic responses of Aplysia californica neurons. Ono, J.K., Salvaterra, P.M. J. Neurosci. (1981) [Pubmed]
  7. Comparative expression of homologous proteins. A novel mode of transcriptional regulation by the coding sequence folding compatibility of chimeras. Morel, N., Massoulié, J. J. Biol. Chem. (2000) [Pubmed]
  8. Identification of a novel type of alternatively spliced exon from the acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of acetylcholinesterase in the snake liver and muscle. Cousin, X., Bon, S., Massoulié, J., Bon, C. J. Biol. Chem. (1998) [Pubmed]
  9. Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of cooh-terminal domain; involvement of a positively charged residue in the peripheral site. Cousin, X., Bon, S., Duval, N., Massoulié, J., Bon, C. J. Biol. Chem. (1996) [Pubmed]
  10. Specific inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol. Slama, J.T., Aboul-Ela, N., Goli, D.M., Cheesman, B.V., Simmons, A.M., Jacobson, M.K. J. Med. Chem. (1995) [Pubmed]
  11. Alpha-bungarotoxin binding to acetylcholine receptor membranes studied by low angle X-ray diffraction. Young, H.S., Herbette, L.G., Skita, V. Biophys. J. (2003) [Pubmed]
  12. Liposome-catalyzed unfolding of acetylcholinesterase from Bungarus fasciatus. Shin, I., Silman, I., Bon, C., Weiner, L. Biochemistry (1998) [Pubmed]
  13. Beta-bungarotoxin is a potent inducer of apoptosis in cultured rat neurons by receptor-mediated internalization. Herkert, M., Shakhman, O., Schweins, E., Becker, C.M. Eur. J. Neurosci. (2001) [Pubmed]
  14. Ceruleotoxin: a possible marker of the cholinergic ionophore. Bon, C., Changeux, J.P. Eur. J. Biochem. (1977) [Pubmed]
  15. Transcriptional regulation of gene expression by the coding sequence: An attempt to enhance expression of human AChE. Weill, C.O., Vorlová, S., Berna, N., Ayon, A., Massoulié, J. Biotechnol. Bioeng. (2002) [Pubmed]
  16. Adenosine diphosphoribose transfer reactions catalyzed by Bungarus fasciatus venom NAD glycohydrolase. Yost, D.A., Anderson, B.M. J. Biol. Chem. (1983) [Pubmed]
  17. Purification and properties of the soluble NAD glycohydrolase from Bungarus fasciatus venom. Yost, D.A., Anderson, B.M. J. Biol. Chem. (1981) [Pubmed]
  18. Potassium channel blockade by the B subunit of beta-bungarotoxin. Benishin, C.G. Mol. Pharmacol. (1990) [Pubmed]
  19. Substrate activation in acetylcholinesterase induced by low pH or mutation in the pi-cation subsite. Masson, P., Schopfer, L.M., Bartels, C.F., Froment, M.T., Ribes, F., Nachon, F., Lockridge, O. Biochim. Biophys. Acta (2002) [Pubmed]
  20. Thioredoxin-linked reductive inactivation of venom neurotoxins. Lozano, R.M., Yee, B.C., Buchanan, B.B. Arch. Biochem. Biophys. (1994) [Pubmed]
  21. Purification and characterization of a novel phospholipase A2 from king cobra (Ophiophagus hannah) venom. Chiou, J.Y., Chang, L.S., Chen, L.N., Chang, C.C. J. Protein Chem. (1995) [Pubmed]
  22. Role of the N-terminal region of the A chain in beta 1-bungarotoxin from the venom of Bungarus multicinctus (Taiwan-banded krait). Chang, L.S., Yang, C.C. J. Protein Chem. (1988) [Pubmed]
  23. Decreased parasympathetic activities in Malayan krait (Bungarus candidus) envenoming. Laothong, C., Sitprija, V. Toxicon (2001) [Pubmed]
  24. Antigenic relationships and relative immunogenicities of venom proteins from six poisonous snakes of Thailand. Chinonavanig, L., Billings, P.B., Matangkasombut, P., Ratanabanangkoon, K. Toxicon (1988) [Pubmed]
  25. Amino acid sequences of three beta-bungarotoxins (beta 3-, beta 4-, and beta 5- bungarotoxins) from Bungarus multicinctus venom. Amino acid substitutions in the A chains. Kondo, K., Toda, H., Narita, K., Lee, C.Y. J. Biochem. (1982) [Pubmed]
 
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