Acta Med. 2006, 49: 3-11

https://doi.org/10.14712/18059694.2017.102

Protein Biotoxins of Military Significance

Jiří Patočkaa,b, Ladislav Středac

aUniversity of Defence, Faculty of Military Health Sciences, Department of Toxicology, Hradec Králové, Czech Republic
bUniversity of South Bohemia, Faculty of Health and Social Studies, Department of Radiology and Toxicology, Czech Republic
cState Office for Nuclear Safety, Department for Control of the Prohibition of Chemical Weapons, Czech Republic

Received June 1, 2005
Accepted March 1, 2006

References

1. Anderson MD, Fairweather N, Charles IG, Emsley P, Isaacs NW, MacDermott: Crystallographic characterization of tetanus toxin fragment. C. J Mol Biol 1993; 230:673–4. <https://doi.org/10.1006/jmbi.1993.1181>
2. Barbieri L, Zamboni M, Montanaro L, Sperti S, Stirpe F, Purification and properties of different forms of modeccin, the toxin of Adenia digitata. Separation of subunits with inhibitory and lectin activity. Biochem J 1980; 185:203–10. <https://doi.org/10.1042/bj1850203> <PubMed>
3. Brittain S, Mohamed ZA, Wang J, Lehmann VK, Carmichael WW, Rinehart KL, Isolation and characterization of microcystins from a river nile strain of oscillatoria tenuis Agardh ex Gomont. Toxicon 2000; 38:1759–7. <https://doi.org/10.1016/S0041-0101(00)00105-7>
4. Brynestad S, Granum PE, Clostridium perfringens and foodborne infections. Int J Food Microbiol 2002; 74:195–202. <https://doi.org/10.1016/S0168-1605(01)00680-8>
5. Castellino FJ, Prorok M. Conantokins: inhibitors of ion flow through the N-methyl- D-aspartate receptor channels. Curr Drug Targets 2000; 1: 219–35. <https://doi.org/10.2174/1389450003349218>
6. Chambery A, Di Maro A, Monti MM, Stirpe F, Parente A. Volkensin from Adenia volkensii Harms (kilyambiti plant), a type 2 ribosome-inactivating protein. Eur J Biochem 2004; 271:108–17. <https://doi.org/10.1046/j.1432-1033.2003.03909.x>
7. Chen YL, Chow LP, Tsugita A, Lin JY. The complete primary structure of abrina B chain. FEBS Lett 1992; 309:115–8. <https://doi.org/10.1016/0014-5793(92)81076-X>
8. Cherington M. Botulism: update and review. Semin Neurol 2004; 24:155–63. <https://doi.org/10.1055/s-2004-830901>
9. Cherla RP, Lee SY, Tesh VL. Shiga toxins and apoptosis. FEMS Microbiol Let. 2003; 228:159–66. <https://doi.org/10.1016/S0378-1097(03)00761-4>
10. Clark K. The Chemical Weapons Convention: Chemical and Toxin Warfare Agents and Disarmament. Royal Military College of Science, Cranfield University, August 1997.
11. Dawson RM. The toxicology of microcystins. Toxicon 1998; 36:953–62. <https://doi.org/10.1016/S0041-0101(97)00102-5>
12. De Haan L, Hirst TR. Cholera toxin: a paradigm for multi-functional engagement of cellular mechanisms (Review). Mol Membr Biol 2004; 21:77–92. <https://doi.org/10.1080/09687680410001663267>
13. Donelli G, Fiorentini C, Matarrese P, Falzano L, Cardines R, Mastrantonio P, Payne DW, Titball RW. Evidence for cytoskeletal changes secondary to plasma membrane functional alterations in the in vitro cell response to Clostridium perfringens epsilon-toxin. Comp Immunol Microbiol Infect Dis 2003; 26:145–56. <https://doi.org/10.1016/S0147-9571(02)00052-8>
14. Enomoto K, Gill DM. Cholera toxin activation of adenylate cyclase. Roles of nucleoside triphosphates and a macromolecular factor in the ADP ribosylation of the GTP-dependent regulatory component. J Biol Chem 1980; 255:1252–8.
15. Fegan D, Andresen D. Conus geographus envenomation. Lancet 1997; 349:1672. <https://doi.org/10.1016/S0140-6736(05)62639-6>
16. Freer JH, Arbuthnott JP. Toxins of Staphylococcus aureus. Pharmacol Ther 1982; 19:55–106. <https://doi.org/10.1016/0163-7258(82)90042-0>
17. Gasperi-Campani A, Barbieri L, Lorenzoni E, Montanaro L, Sperti S, Bonetti E. Modeccin, the toxin of Adenia digitata. Purification, toxicity and inhibition of protein synthesis in vitro. Biochem J 1978; 174:491–6. <https://doi.org/10.1042/bj1740491> <PubMed>
18. Gill DM. Bacterial toxins: a table of lethal amounts. Microbiol Rev 1982; 46: 86–94.
19. Gordjani N, Sutor AH, Zimmerhackl LB, Brandis M. Hemolytic uremic syndromes in childhood. Semin Thromb Hemost 1997; 23:281–93. <https://doi.org/10.1055/s-2007-996101>
20. Gransden WR, Damm MA, Anderson JD, et al. Further evidence associating hemolytic- uremic syndrome with infection by Verotoxin-producing Escherichia coli 0157:H7. J Infect Dis 1986; 154:522–4. <https://doi.org/10.1093/infdis/154.3.522>
21. Greenfield RA, Brown BR, Hutchins JB et al. Microbiological, biological, and chemical weapons of warfare and terrorism. Am J Med Sci 2002; 323:326–40. <https://doi.org/10.1097/00000441-200206000-00005>
22. Haas LF. Emil Adolph von Behring (1854–1917) and Shibasaburo Kitasato (1852–1931). J Neurol Neurosurg Psychiatry 2001; 71:62. <https://doi.org/10.1136/jnnp.71.1.62> <PubMed>
23. Hartley MR, Lord JM. Cytotoxic ribosome-inactivating lectins from plants. Biochim Biophys Acta 2004; 1701:1–14. <https://doi.org/10.1016/j.bbapap.2004.06.004>
24. Helting TB, Zwisler O, Wiegandt H. Structure of tetanus toxin. II. Toxin binding to ganglioside. J Biol Chem. 1977; 252:194–8.
25. Hildebrand A, Pohl M, Bhakdi S. Staphylococcus aureus alpha-toxin. Dual mechanism of binding to target cells. J Biol Chem 1991; 266:17195–200.
26. Holmes RK: Biology and molecular epidemiology of diphtheria toxin and the tox gene. J Infect Dis 2000; 181, Suppl 1:156–67. <https://doi.org/10.1086/315554>
27. Karmali MA. Infection by Shiga toxin-producing Escherichia coli: an overview. Mol Biotechnol 2004; 26:117–22. <https://doi.org/10.1385/MB:26:2:117>
28. Kassis S, Hagmann J, Fishman PH, Chang PP, Moss J. Mechanism of action of cholera toxin on intact cells. Generation of A1 peptide and activation of adenylate cyclase. J Biol Chem 1982; 257:12148–52.
29. Katzin BJ, Collins EJ, Robertus JD. Structure of ricin A-chain at 2.5 A. Proteins 1991; 10:251–9. <https://doi.org/10.1002/prot.340100309>
30. Kimura M, Sumizawa T, Funatsu G: The complete amino acid sequences of the B-chains of abrin-a and abrin-b, toxic proteins from the seeds of Abrus precatorius. Biosci Biotechnol Biochem 1993; 57:166–9. <https://doi.org/10.1271/bbb.57.166>
31. Krauspenhaar R, Eschenburg S, Perbandt M et al. Crystal structure of mistletoe lectin I from Viscum album. Biochem Biophys Res Commun 1999; 257:418–24. <https://doi.org/10.1006/bbrc.1999.0470>
32. Lewis RJ. Conotoxins as selective inhibitors of neuronal ion channels, receptors and transporters. IUBMB Life 2004; 56:89–93. <https://doi.org/10.1080/15216540410001668055>
33. Lord JM, Roberts LM, Robertus JD. Ricin: structure, mode of action, and some current applications. FASEB J 1994; 8:201–8. <https://doi.org/10.1096/fasebj.8.2.8119491>
34. Low DK, Freer JH, Arbuthnott JP, Mollby R, Wadstrom T. Consequences of sphingomyelin degradation in erythrocyte ghost membranes by staphylococcal beta-toxin (sphingomyelinase C). Toxicon 1974; 12:279–85. <https://doi.org/10.1016/0041-0101(74)90070-1>
35. Mátlová J, Krejčí V, Patočka J. Cyanotoxins and their effect on human health (Article in Czech). Kontakt 2004; 6(1): 43–51.
36. Merritt EA, Kuhn P, Sarfaty S, Erbe JL, Holmes RK, Hol WG. The 1.25 A resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site. J Mol Biol 1998; 282:1043–59. <https://doi.org/10.1006/jmbi.1998.2076>
37. Merritt EA, Sarfaty S, van den Akker F, L’Hoir C, Martial JA, Hol WG. Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide. Protein Sci 1994; 3:166–75. <https://doi.org/10.1002/pro.5560030202> <PubMed>
38. Montfort W, Villafranca JE, Monzingo AF et al. The three-dimensional structure of ricin at 2.8 A. J Biol Chem 1987; 262:5398–403.
39. Morris KN, Wool IG. Analysis of the contribution of an amphiphilic alpha-helix to the structure and to the function of ricin A chain. Proc Natl Acad Sci USA 1994; 91:7530–3. <https://doi.org/10.1073/pnas.91.16.7530> <PubMed>
40. O’Brien AD, Tesh VL, Donohue-Rolfe A, et al. Shiga toxin: biochemistry, genetics, mode of action, and role in pathogenesis. Curr Topics Microbiol Immunol 1992; 180:65–94.
41. Ochi S, Oda M, Nagahama M, Sakurai J. Clostridium perfringens alpha-toxin-induced hemolysis of horse erythrocytes is dependent on Ca2+ uptake. Biochim Biophys Acta 2003; 1613:79–86. <https://doi.org/10.1016/S0005-2736(03)00140-8>
42. Ohizumi Y, Matsunaga K. Chemical structures and the mechanism of action of peptide toxins from cone shells (Article in Japanese). Tanpakushitsu Kakusan Koso 2001; 46, Suppl l4:449–54.
43. Olsnes S, Haylett T, Sandvig K. The toxic lectin modeccin. Methods Enzymol 1982; 83:357–62. <https://doi.org/10.1016/0076-6879(82)83030-9>
44. Olsnes S, Kozlov JV: Ricin. Toxicon 2001; 39:1723–8. <https://doi.org/10.1016/S0041-0101(01)00158-1>
45. Olsnes S, Pihl A. Kinetics of binding of the toxic lectins abrin and ricin to surface receptors of human cells. J Biol Chem 1976; 251:3977–84.
46. Olsnes S, Sandvig K, Eiklid K, Pihl A. Properties and action mechanism of the toxic lectin modeccin: interaction with cell lines resistant to modeccin, abrin, and ricin. J Supramol Struct 1978; 9:15–25. <https://doi.org/10.1002/jss.400090103>
47. Olsnes S. The history of ricin, abrin and related toxins. Toxicon 2004; 44:361–70. <https://doi.org/10.1016/j.toxicon.2004.05.003>
48. Patočka J. Abrin and ricin – two dangerous poisonous proteins. ASA Newsletter 2001; 85:205–8.
49. Patočka J, Špliňo M. Botulinum toxin: from poison to medicinal agent. ASA Newsletter 2002; 88:14–9.
50. Patočka J, Špliňo M, Měrka V. Botulism and bioterrorism: How serious is this problem? Acta Medica (Hradec Kralove) 2005; 48:23–8. <https://doi.org/10.14712/18059694.2018.24>
51. Patočka J, Středa L. Brief review of natural nonprotein neurotoxins. ASA Newsletter 2002; 89:16–24.
52. Patočka J, Středa L. Plant toxic proteins and their current significance for warfare and medicine. J Appl Biomed 2003; 1:141–7.
53. Patočka J. The toxins of cyanobacteria. Acta Medica (Hradec Kralove) 2001; 44:69–75.
54. Patocka J: Toxicological characteristic of ricin (Article in Czech). Voj Zdrav Listy 1998; 67:166–8.
55. Petit L, Gibert M, Gourch A, Bens M, Vandewalle A, Popoff MR. Clostridium perfringens epsilon toxin rapidly decreases membrane barrier permeability of polarized MDCK cells. Cell Microbiol. 2003; 5:155–64. <https://doi.org/10.1046/j.1462-5822.2003.00262.x>
56. Refsnes K, Haylett T, Sandvig K, Olsnes S. Modeccin – a plant toxin inhibiting protein synthesis. Biochem Biophys Res Commun 1977; 79:1176–83. <https://doi.org/10.1016/0006-291X(77)91130-5>
57. Robinson RF, Nahata MC. Management of botulism. Ann Pharmacother 2003; 37:127–31. <https://doi.org/10.1345/aph.1C034>
58. Rutenber E, Robertus JD. Structure of ricin B-chain at 2.5 A resolution. Proteins 1991; 10:260–9. <https://doi.org/10.1002/prot.340100310>
59. Schmid DI, Kohan DE. Effect of shigatoxin-1 on arachidonic acid release by human glomerular epithelial cells. Kidney Int 2001; 60:1026–36. <https://doi.org/10.1046/j.1523-1755.2001.0600031026.x>
60. Sharon N, Lis H. Cell-agglutinating and sugar-specific proteins. Science 1972; 177:949–59. <https://doi.org/10.1126/science.177.4053.949>
61. Slater LN, Greenfield RA. Biological toxins as potential agents of bioterrorism. J Okla State Med Assoc 2003; 96:73–6.
62. Smedley JG, Fisher DJ, Sayeed S, Chakrabarti G, McClane BA. The enteric toxins of Clostridium perfringens. Rev Physiol Biochem Pharmacol 2004; 152:183–204. <https://doi.org/10.1007/s10254-004-0036-2>
63. Stirpe F. Ribosome-inactivating proteins. Toxicon 2004; 44:371–83. <https://doi.org/10.1016/j.toxicon.2004.05.004>
64. Thelestam M, Blomqvist L. Staphylococcal alpha toxin—recent advances. Toxicon 1988; 26:55–65. <https://doi.org/10.1016/0041-0101(88)90137-7>
65. Turton K, Chaddock JA, Acharya KR. Botulinum and tetanus neurotoxins: structure, function and therapeutic utility. Trends Biochem Sci 2002; 27:552–8. <https://doi.org/10.1016/S0968-0004(02)02177-1>
66. Wang KY, Xu Q. Lectins and Toxins. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 2000; 32:201–5.
67. Zapor M, Fishbain JT. Aerosolized biologic toxins as agents of warfare and terrorism. Respir Care Clin N Am 2004; 10:111–22. <https://doi.org/10.1016/S1078-5337(03)00054-6>
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