Skip to main content

Toxic Proteins and Peptides

  • Chapter
Comparative Animal Biochemistry
  • 469 Accesses

Abstract

Many animals produce poisonous substances which, even at a relatively low dose, are deleterious or lethal to other organisms, including man. They may serve on the one hand to disable or kill prey, or on the other hand as a protection or defence against predators. These substances are mostly produced by special glands, and both poison reservoirs and specialized structures for delivering the secretion, e.g. stings or modified mouthparts or fangs, are usually also present. In accordance with the aims of this book, we will deal with the comparative biochemistry of the animal toxins as natural products with special structures and functions; a discussion of the mechanisms of their pharmacological effects and the highly complicated organ structures and behavioural patterns associated with natural poisons may be found in numerous monographs [5, 20, 36, 68, 69]. Toxic proteins and oligopeptides are known from many very different animals (Table 9.1); there is, however, a host of low molecular weight compounds with considerable toxicity which will be considered along with other non-toxic products of secondary metabolism in Chapter 19.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 109.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Adams M. E. et al.: Omega-agatoxins: Novel calcium channel antagonists of two subtypes from funnel web spider (Agelenopsis aperta) venom. J. Biol. Chem. 265: 861–867 (1990)

    PubMed  CAS  Google Scholar 

  2. Aird S. D. et al.: The amino acid sequence of the acidic subunit B-chain of crotoxin. Biochim. biophys. Acta 1040: 217–224 (1990)

    CAS  Google Scholar 

  3. Argiolas A. and Pisano J. J.: Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus. J. biol. Chem. 260: 1437–44 (1985)

    PubMed  CAS  Google Scholar 

  4. Barra D. et al.: Rohdei-litorin: a new peptide from the skin of Phyllomedusa rohdei. FEBS Letters 182: 53–56 (1985)

    Article  PubMed  CAS  Google Scholar 

  5. Bettipi S. (ed.): Arthropod venoms. Hb. exp. Pharmacol. Vol. 48. Springer, Berlin 1978

    Google Scholar 

  6. Bjarnason J. B. and Fox J. W.: Characterization of two hemorrhagic zinc proteinases, toxin c and toxin d, from western diamondback rattlesnake (Crotalus atrox) venom. Biochim. biophys. Acta 911: 356–363 (1987)

    CAS  Google Scholar 

  7. Bouchier C. et al.: Cloning and sequencing of cDNAs encoding the two subunits of crotoxin. Nucleic Acids Res. 16: 9050 (1988)

    Article  PubMed  CAS  Google Scholar 

  8. Bougis P. E., Rochat H. and Smith L. A.: Precursors of Androctonus australis scorpion neurotoxins. J. Biol. Chem. 264: 19259–65 (1989)

    PubMed  CAS  Google Scholar 

  9. Breckenridge R. and Dufton M. J.: The structural evolution of cobra venom cytotoxins. J. mol. Evol. 26: 274–283 (1987)

    Article  PubMed  CAS  Google Scholar 

  10. Brown M. R. et al: Amino acid sequence of versutoxin, a lethal neurotoxin from the venom of the funnel-web spider Atrax versutus. Biochem. J. 250: 401–405 (1988)

    PubMed  CAS  Google Scholar 

  11. Corfield P. W. R., Lee T. J. and Low B. W.: The crystal structure of erabutoxin a at 2.0 A resolution. J. Biol. Chem. 264: 9239–42 (1989)

    PubMed  CAS  Google Scholar 

  12. Dotimas E. M. et al.: Isolation and structure analysis of bee venom mast cell degranulating peptide. Biochim. biophys. Acta 911: 285–293 (1987)

    CAS  Google Scholar 

  13. Dufton M. J.: Classification of elapid snake neurotoxins and cytotoxins according to chain length: evolutionary implications. J. mol. Evol. 20: 128–134 (1984)

    Article  PubMed  CAS  Google Scholar 

  14. Eitan M. et al.: A scorpion venom neurotoxin paralytic to insects that affects sodium current inactivation: Purification, primary structure, and mode of action. Biochemistry 29: 5941–47 (1990)

    Article  PubMed  CAS  Google Scholar 

  15. Eng J. et al.: Purification and structure of exendin-3, a new pancreatic secretagogue isolated from Heloderma horridum venom. J. Biol. Chem. 265: 20259–62 (1990)

    PubMed  CAS  Google Scholar 

  16. Erspamer V. et al.: Amino acid composition and sequence of Crinia-angiotensin, an angiotensin-Il-like endecapeptide from the skin of the Australian frog Cri-nia georgiana. Experientia 35: 1132–33 (1979)

    Article  PubMed  CAS  Google Scholar 

  17. Farid T. M., Tu A. T. and El-Asmar E: Characterization of cerastobin, a thrombin-like enzyme from Cerastes vipera. Biochemistry 28: 371–377 (1989)

    Article  PubMed  CAS  Google Scholar 

  18. Fontecilla-Camps J. C.: Three-dimensional model of the insect-directed scorpion toxin from Androctonus australis Hector and its implication for the evolution of scorpion 38. toxins in general. J. mol. Evol. 29: 63–67 (1989)

    Article  PubMed  CAS  Google Scholar 

  19. Gray W. R., Olivera B. M. and Cruz L. J.: Peptide toxins from venomous Conus snails Annual Rev. Biochem. 57: 665–700 (1988)

    Article  CAS  Google Scholar 

  20. Habermehi G. G.: Toxic animals and their weapons (in German). 4th Ed. Springer, Berlin 1987

    Google Scholar 

  21. Hillyard D. R. et al.: A molluscivorous Conus toxin: 40. Conserved frameworks in conotoxins. Biochemistry 28: 358–361 (1989)

    Article  PubMed  CAS  Google Scholar 

  22. Hirabayashi J., Kusonoki T. and Kasai K.: Complete primary structure of a galactose-specific lectin from the venom of the rattlesnake Crotalus atrox: Homologies 41. with Ca-dependent-type lectins. J. Biol. Chem. 266: 2320–26 (1991)

    PubMed  CAS  Google Scholar 

  23. Ho C. L. and Ko J. L.: Hornetin: the lethal protein of the hornet (Vespa flavitarsus) venom. FEBS Letters 209: 18–22 (1986)

    Article  PubMed  CAS  Google Scholar 

  24. Ho C. L. and Hwang L. L.: Structure and biological 42. activities of a new mastoparan isolated from the venom of the hornet Vespa basalis. Biochem. J. 274: 453–456 (1991)

    PubMed  CAS  Google Scholar 

  25. Huang T. F. et al.: Purification and characterization of an antiplatelet peptide, arietin, from Bitis arietans 43. venom. Biochim. biophys. Acta 1074: 136–143 (1991)

    CAS  Google Scholar 

  26. Inoue S. et al: Amino acid sequence of a cytotoxinlike basic protein with low cytotoxic activity from the 44. venom of the Thailand cobra Naja naja siamensis. FEBS Letters 218: 17–21 (1987)

    Article  PubMed  CAS  Google Scholar 

  27. Inoue S. et al: Amino acid sequences of nerve growth 45. factors derived from cobra venoms. FEBS Letters 279: 38–40 (1991)

    Article  PubMed  CAS  Google Scholar 

  28. Itoh N. et al.: Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with 46. the trypsin/kallikrein gene family. J. Biol. Chem. 263: 7628–31 (1988)

    PubMed  CAS  Google Scholar 

  29. Junor L. R. et al.: The purification and amino acid sequence of the lethal neurotoxin Txl from the venom 47. of the Brasilian armed spider Phoneutria nigriventer. FEBS Letters 263: 251–253 (1990)

    Article  PubMed  Google Scholar 

  30. Kaiser I. I. et al.: The amino acid sequence of a myotoxic phospholipase from the venom of Bothrops 48. asper. Arch. Biochem. Biophys. 278: 319–325 (1990)

    Article  PubMed  CAS  Google Scholar 

  31. Kern W. R.: Structure and action of nemertine toxins. Amer. Zool. 25: 99–111 (1985)

    Google Scholar 

  32. Kemeny D. M. et al.: The purification and characteri- 49. zation of hyaluronidase from the venom of the honey bee, Apis mellifera. Eur. J. Biochem. 139: 217–223 (1984) 50.

    Google Scholar 

  33. King T. P., Kochoumian L and Joslyn A.: Wasp venom proteins: Phospholipase Al and B. Arch. B.ochem. Biophys. 230: 1–12 (1984)

    Article  CAS  Google Scholar 

  34. Kopeyan C. et al.: Primary structure of scorpion anti-insect toxins isolated from the venom of Leiurus quinquestriatus quinquestriatus. FEBS Letters 261: 423–426 (1990)

    Article  PubMed  CAS  Google Scholar 

  35. Kosen P. A. et al.: Structural studies of abungarotoxin. 3. Corrections in the primary sequence and X-ray structure and characterization of an isotoxic a-bungarotoxin. Biochemistry 27: 2775–81 (1988)

    Article  PubMed  CAS  Google Scholar 

  36. Lee C. Y. (ed.): Snake venoms. Hb. exp. Pharmacol. Vol 52. Springer, Berlin 1979

    Google Scholar 

  37. Lind P. and Eaker D: Amino-acid sequence of the a-subunit of taipoxin, an extremely potent presynaptic neurotoxin from the Australian snake taipan (Oxyuranus s. scutellatus). Eur. J. Biochem. 124: 441–447 (1982)

    Article  PubMed  CAS  Google Scholar 

  38. Liu C. S. et al.: The amino acid sequence and properties of an edema-inducing Lysphospholipase-A2 homolog from the venom of Trimesurus mucrosquamatus. Biochim. biophys. Acta 1077: 362–370 (1991)

    CAS  Google Scholar 

  39. Lomonte B. et al.: Isolation of a galactose-binding lectin from the venom of the snake Bothrops godmani (Godman pi viper). Toxicon 28: 75–81 (1990)

    Article  PubMed  CAS  Google Scholar 

  40. Loret E. P. et al.: An anti-insect toxin purified from the scorpion Androctonus australis Hector also acts on the a-sites and 13-sites of the mammalian sodium channel: Sequence and circular dichroism. Biochemistry 30: 633–640 (1991)

    Article  PubMed  CAS  Google Scholar 

  41. Manchewa I. et al.: Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of phospholipase A2 of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes). Biol. Chem. Hoppe-Seyler 368: 343–352 (1987)

    Article  Google Scholar 

  42. Maraganore J. M. and Heinrikson R. L.: The lysine-49 phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus. Relation of structure and function to other phospholipases A2. J. biol. Chem. 261: 4797–4804 (1986)

    PubMed  CAS  Google Scholar 

  43. Massefski W jr. et al.: Molecular structure of charybdotoxin, a pore-directed inhibitor of potassium ion channels. Science 249: 521–524 (1990)

    Article  PubMed  CAS  Google Scholar 

  44. McMullen B. A., Fujikawa K. and Kisiel W.: Primary structure of a protein C activator from Agkistrodon contortrix venom. Biochemistry 28: 674–679 (1989)

    Article  PubMed  CAS  Google Scholar 

  45. Metrione R. M., Schweitz H. and Walsh K. A.: The amino acid sequence of toxin Rp111 from the sea anemone, Radianthus paumotensis. FEBS Letters 218: 59–62 (1987)

    Article  PubMed  CAS  Google Scholar 

  46. Mochcamorales J., Martin B. M. and Possani L. D.: Isolation and characterization of helothermin, a novel toxin from Heloderma horridum horridum (Mexican beaded lizard) venom. Toxicon 28: 299–309 (1990)

    Article  CAS  Google Scholar 

  47. Montecucchi P. C., Gozzini L and Erspamer V.: Primary structure determination of a tryptophancontaining tridecapeptide from Phyllomedusa rohdei. Int. J. Peptide Protein Res. 27: 175–182 (1986)

    Article  CAS  Google Scholar 

  48. Mori N. and Tu A. T.: Isolation and primary structure of the major toxin from sea snake, Acalyptophis peronii, venom. Arch. Biochem. Biophys. 260: 10–17 (1988)

    Article  PubMed  CAS  Google Scholar 

  49. Nishida S. et al: Amino acid sequence of a sea anemone toxin from Parasicyonis actinostoloides. Eur. J. Biochem. 150: 171–173 (1985)

    Article  PubMed  CAS  Google Scholar 

  50. Ohtani Y. et al.: Some properties of a kininogenase from the venom of Agkistrodon caliginosus (KankokuMamushi). Toxicon 26: 903–912 (1988)

    Article  PubMed  CAS  Google Scholar 

  51. Olivera B. M. et al.: Diversity of Conus neuropeptides. Science 249: 257–263 (1990)

    Article  PubMed  CAS  Google Scholar 

  52. Pearson J. A. et al.: Studies on the subunit structure of textilotoxin, a potent presyaptic neurotoxin from the venom of the Australian common brown snake (Pseudonaja textilis). 2. The amino acid sequence and toxicity studies of subunit-D. Biochim. biophys. Acta 1077: 147–150 (1991)

    CAS  Google Scholar 

  53. Pungercar J. et al: Amino acid sequence of ammodytoxin C as deduced from cDNA. Nucleic Acids Res. 17: 43–67 (1989)

    Article  Google Scholar 

  54. Savel-Niemann A.: Tarantula (Eurypelma californi-cum) venom, a multicomponent system. Biol. Chem. Hoppe-Seyler 370: 485–498 (1989)

    Article  PubMed  CAS  Google Scholar 

  55. Schmidt J. O.: Biochemistry of insect venoms. Annual Rev. Entomol. 27: 339–368 (1982)

    Article  CAS  Google Scholar 

  56. Schweitz H. et al.: Purification, sequence and pharmacological properties of sea anemone toxins from Radianthus paumatoensis. A new class of sea anemone toxins acting on sodium channel. Biochemistry 24: 3554–61 (1985)

    Article  PubMed  CAS  Google Scholar 

  57. Shafquat J. et al.: Primary structure and functional properties of cobra (Naja naja naja) venom Kunitz-type trypsin inhibitor. Eur. J. Biochem. 194: 337–341 (1990)

    Article  Google Scholar 

  58. Shafquat J. et al.: Extensive multiplicity of the miscellaneous types of neurotoxins from the venom of the cobra Naja naja naja and structural characterization of major components. FEBS Letters 284: 70–72 (1991)

    Article  Google Scholar 

  59. Shai Y. et al.: Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea moses sole with ionophore activity. FEBS Letters 242: 161–166 (1988)

    Article  PubMed  CAS  Google Scholar 

  60. Simmaco M. et al.: A family of bombinin-related peptides from the skin of Bombina variegata. Eur. J. Biochem. 199: 217–222 (1991)

    Article  PubMed  CAS  Google Scholar 

  61. Simpson R. J. et al.: Complete amino acid sequence of tenebrosin-C, a cardiac stimulatory and haemolytic protein from the sea anemone Actinia tenebrosa. Eur. J. Biochem. 190: 319–328 (1990)

    Article  PubMed  CAS  Google Scholar 

  62. Skinner W. S. et al.: Purification and characterization of two classes of neurotoxins from the funnel web spider, Agelenopsis aperta. J. Biol. Chem. 264: 2150–55 (1989)

    PubMed  CAS  Google Scholar 

  63. Smith L. A. and Schmidt J. J.: Cloning and nucleotide sequences of crotamine genes. Toxicon 28: 575–585 (1990)

    Article  PubMed  CAS  Google Scholar 

  64. Stapleton A. et al.: Curtatoxins. Neurotoxic insecticidal polypeptides isolated from the funnel-web spider Hololena curta. J. Biol. Chem. 265: 2054–59 (1990)

    PubMed  CAS  Google Scholar 

  65. Takeya H. et al.: The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis. J. Biol. Chem. 265: 16068–73 (1990)

    PubMed  CAS  Google Scholar 

  66. Tamiya T. et al.: Cloning and sequence analysis of the cDNA encoding for a snake neurotoxin precursor. Biochimie 67: 185–189 (1985)

    Article  PubMed  CAS  Google Scholar 

  67. Terwilliger T. C. and Eisenberg D.: The structure of melittin. J. biol. Chem. 257: 6016–22 (1982)

    PubMed  CAS  Google Scholar 

  68. Teuscher E. and Lindequist U.: Biogenic Toxins (in German). G. Fischer, Stuttgart 1987

    Google Scholar 

  69. Tu A. T. (ed.): Insect poisons, allergens and other invertebrate venoms. Handbook of natural Toxins Vol. 2. M. Dekker, New York 1984

    Google Scholar 

  70. Tyler M. I. et al.: Pseudonajatoxin b: unusual amino acid sequence of a lethal neurotoxin from the venom of the Australian common brown snake, Pseudonaja textilis. Eur. J. Biochem. 166: 139–143 (1987)

    Article  PubMed  CAS  Google Scholar 

  71. Ueda M., Chang C. C. and Ohno M.: Purification and characterization of the L-amino acid oxidase from the venom of Trimeresurus mucrosquamatus (Taiwan habu snake). Toxicon 26: 695–706 (1988)

    Article  PubMed  CAS  Google Scholar 

  72. Vandermeers A. et al.: Differences in primary structure among 5 phospholipases-A2 from Heloderma suspectum. Eur. J. Biochem. 196: 537–544 (1991)

    Article  PubMed  CAS  Google Scholar 

  73. Vlasak R. et al.: Nucleotide sequence of cloned cDNA coding for honeybee prepromelittin. Eur. J. Biochem. 135: 123–126 (1983)

    Article  PubMed  CAS  Google Scholar 

  74. Yanagawa Y. et al.: A novel sodium channel inhibitor from Conus geographus: Purification, structure and pharmacological properties. Biochemistry 27: 6256–62 (1988)

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

Copyright information

© 1994 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

Urich, K. (1994). Toxic Proteins and Peptides. In: Comparative Animal Biochemistry. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-06303-3_9

Download citation

  • DOI: https://doi.org/10.1007/978-3-662-06303-3_9

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-08181-1

  • Online ISBN: 978-3-662-06303-3

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics