Cloning, Characterization, and Expression of Animal Toxin Genes for Vaccine Development

References

• Cruz L.J., Gray W.R., Yoshikami D., Olivera B.M. Conus Venoms: Rich Source of Neuroactive Peptides. J. Toxicol.-Toxin Rev. 1985; 4: 107–132
   Web of Science ®Google Scholar
• Gray W.R., Olivera B.M., Cruz L.J. Peptide Toxins from Venomous Conus Snails. Annu. Rev. Biochem. 1988; 57: 665–700
   PubMed Web of Science ®Google Scholar
• Olivera B.M, Gray W.R., Cruz L.J. Marine Snail Venoms. Marine Toxins and Venoms, A.T. Tu. Marcel Dekker, Inc., New York 1988; 327, 352
   Google Scholar
• Walker M.J.A. Coelenterate and Echinoderm Toxins: Mechanisms and Actions. Marine Toxins and Venoms, A.T. Tu. Marcel Dekker, Inc., New York 1988; 279–325
   Google Scholar
• Nair M.S.R. Fish Skin Toxins. Marine Toxins and Venoms, A.T. Tu. Marcel Dekker, Inc., New York 1988; 211–226
   Google Scholar
• Ori M. Biology of and Poisonings by Spiders. Insect Poisons, Allergens, and Other Invertebrate Venoms, A.T. Tu. Marcel Dekker, Inc., New York 1988; 397–440
   Google Scholar
• Geren C.R. Neurotoxins and Necrotoxins of Spider Venoms. J. Toxicol.- Toxin Rev. 1986; 5: 161–170
   Web of Science ®Google Scholar
• Duchen L.W., Gomez S. Pharmacology of Spider Venoms. Insect Poisons, Allergens, and Other Invertebrate Venoms, A.T. Tu. Marcel Dekker, Inc., New York 1988; 483–512
   Google Scholar
• Jackson H., Parks T.N. Spider Toxins: Recent Applications in Neurobiology. Annu. Rev. Neurosci. 1989; 12: 405–414
   PubMed Web of Science ®Google Scholar
• Jacobsen T.F., Sand O., Bjoro T., Karlsen H.E., Iversen J-G. Effect of Diamphidia Toxin, a Bushman Arrow Poison, on Ionic Permeability in Nucleated Cells. Toxicon 1990; 28: 435–444
   PubMed Web of Science ®Google Scholar
• Watt D.D., Simard J.M. Neurotoxic Proteins in Scorpion Venom. J. Toxicol.-Toxin Rev. 1984; 3: 181–221
   Web of Science ®Google Scholar
• Possani L.D. Structure of Scorpion Toxins. Insect Poisons, Allergens, and Other Invertebrate Venoms, A.T. Tu. Marcel Dekker, Inc., New York 1988; 513–550
   Google Scholar
• Couraud F., Jover E. Mechanism of Action of Scorpion Toxins. Insect Poisons, Allergens, and Other Invertebrate Venoms, A.T. Tu. Marcel Dekker, Inc., New York 1988; 659–678
   Google Scholar
• Meldrum B.S. The Actions of Snake Venoms on Nerve and Muscle. The Pharmacology of Phospholipase A and of Polypeptide Toxins. Pharmacol. Rev. 1965; 17: 393–445
   PubMed Web of Science ®Google Scholar
• Lee C.Y. Chemistry and Pharmacology of Polypeptide Toxins in Snake Venoms. Annu. Rev. Pharmacol. 1972; 12: 265–286
   PubMedGoogle Scholar
• Tu A.T. Neurotoxins of Animal Venoms: Snakes. Annu. Rev. Biochem. 1973; 42: 235–258
   PubMed Web of Science ®Google Scholar
• Yang C.C. Chemistry and Biochemistry of Snake Venom Neurotoxins. Toxins: Animal, Plant, and Microbial, P. Rosenberg. Pergamon Press, New York 1978; 261–292
   Google Scholar
• Habermann E. Bee and Wasp Venoms. Science 1972; 177: 314–322
   PubMed Web of Science ®Google Scholar
• Shipolini R.A. Biochemistry of Bee Venom. Insect Poisons, Allergens, and Other Invertebrate Venoms, A.T. Tu. Marcel Dekker, Inc., New York 1988; 49–85
   Google Scholar
• Piek T. Pharmacology of Hymenoptera Venoms. Insect Poisons, Allergens, and Other Invertebrate Venoms, A.T. Tu. Marcel Dekker, Inc., New York 1988; 135–185
   Google Scholar
• Nakajima T., Yasuhara T., Erspamer V., Erspamer G.F., Negri L., Endean R. Phensalaemin- and Bombesin-Like Peptides in the Skin of the Australian Leptodactylid Frog. Uperoleia rugosa. Chem. Phar. Bul. 1980; 28: 689–695
   PubMed Web of Science ®Google Scholar
• Minton S.A. Venom Diseases. Charles Thomas, Springfield 1974
   Google Scholar
• Gans C. Biology of the Reptilia. Academic Press, London 1978; Vol. 8
   Google Scholar
• Arthropod Venoms, S. Bettini. Springer-Verlag, Berlin 1978
   Google Scholar
• Handbook of Experimental Pharmacology, C.Y. Lee. Snake Venoms, Springer-Verlag, New York 1979; Vol. 52
   Google Scholar
• Sutherland S.K. Australian Animal Toxins. Oxford University Press, New York 1983
   Google Scholar
• Russell F.E. Snake Venom Poisoning. Lippincott, New York 1980
   Google Scholar
• Rattlesnake Venoms: Their Action and Treatment, A.T. Tu. Marcel Dekker Inc., New York 1982
   Google Scholar
• Handbook of Natural Toxins, A.T. Tu. Insect Poisons, Allergens, and Other Invertebrate Venoms, Marcel Dekker, Inc., New York 1988; Handbook of Natural Toxins
   Google Scholar
• Handbook of Natural Toxins, A.T. Tu. Marine Toxins and Venoms, Marcel Dekker, Inc., New York 1988; Vol. 3
   Google Scholar
• Tu A.T. Local Tissue Damaging (Hemorrhage and Myonecrosis) Toxins from Rattlesnake and Other Pit Viper Venoms. J. Toxicol.-Toxin Rev. 1983; 2: 205–234
   Web of Science ®Google Scholar
• Catterall W.A. The Molecular Basis of Neuronal Excitability. Science 1984; 223: 653–661
   PubMed Web of Science ®Google Scholar
• Couraud F., Jover E., Dubois J.M., Rochat H. Two Types of Scorpion Toxin Receptor Sites, One Related to the Activation, the Other to the Inactivation of the Action Potential Sodium Channel. Toxicon 1982; 20: 9–16
   PubMed Web of Science ®Google Scholar
• Alsen C. Biological Significance of Peptides from Anemonia sulcata. Fed. Proc. 1983; 42: 101–108
   PubMedGoogle Scholar
• Olivera B.M., Gray W.R., Zeikus R., McIntosh J.M., Varga J., Rivier J., Santos V., Cruz L.J. Peptide Neurotoxins from Fish-Hunting Cone Snails. Science 1985; 230: 1338–1343
   PubMed Web of Science ®Google Scholar
• Lazdunski M. Apamin, a Neurotoxin Specific for One Class of Ca2+-Dependent K+ Channels. Cell Calcium 1983; 4: 421–428
   PubMed Web of Science ®Google Scholar
• Harvey A.L., Anderson A.J., Mbugua P.M., Karlsson E. Toxins from Mamba Venoms that Facilitate Neuromuscular Transmission. J. Toxicol.-Toxin Rev. 1984; 3: 91–137
   Web of Science ®Google Scholar
• Miller C., Moczydlowski E., Latorre R., Phillips M. Charybdo-toxin, a Protein Inhibitor of Single Ca2+-Activated K+ Channels from Mammalian Skeletal Muscle. Nature 1985; 313: 316–318
   PubMed Web of Science ®Google Scholar
• Valdivia H.H., Smith J.S., Martin B.M., Coronado R., Possini L.D. Charybdotoxin and Noxiustoxin, Two Homologous Peptide Inhibitors of the K+(Ca2+) Channel. FEBS Lett. 1988; 226: 280–284
   PubMed Web of Science ®Google Scholar
• Sugimori M., Llinas R. Spider Venom Blockade of Dendritic Calcium Spiking in Purkinje Cells Studied in vitro. Soc. Neurosci. Abstr. 1987; 13: 228
   Google Scholar
• Geren C.R., Odell G.V. The Biochemistry of Spider Venoms. Insect Poisons, Allergens, and Other Invertebrate Venoms, A.T. Tu. Marcel Dekker, Inc., New York 1988; 441–481
   Google Scholar
• Harris J.B., Karlsson E., Thesleff S. Effects of an Isolated Toxin from Australian Tiger Snake (Notechis scutatus scutatus) Venom at the Mammalian Neuromuscular Junction. Br. J. Pharmacol. 1973; 47: 141–146
   PubMed Web of Science ®Google Scholar
• Gopalakrishnakone P., Hawgood B.J., Holbrooke S.E., Marsh N.A., Santana de Sa S., Tu A.T. Site of Action of Mojave Toxin Isolated from the Venom of the Mojave Rattlesnake. Br. J. Pharmacol. 1980; 69: 421–431
   PubMed Web of Science ®Google Scholar
• Chang C.C., Chen T.F., Lee C.Y. Studies of the Presynaptic Effect of β-Bungarotoxin on Neuromuscular Transmission. J. Pharmac. Exp.Ther. 1973; 184: 339–345
   PubMed Web of Science ®Google Scholar
• Su M.J., Chang C.C. Presynaptic Effects of Snake Venom Toxins Which Have Phospholipase A2 Activity (β-Bungarotoxin, Taipoxin, Crotoxin). Toxicon 1984; 22: 631–640
   PubMed Web of Science ®Google Scholar
• Kamenskaya M.A., Thesleff S. The Neuromuscular Blocking Action of an Isolated Toxin from the Elapid Oxyuranus scutellatus. Acta Physiol. Scand. 1974; 90: 716–724
   PubMedGoogle Scholar
• Hayashi K., Endo T., Nakanishi M., Furukawa S., Jorbert F.J., Nagaki Y., Nomoto H., Tamiya N. On the Mode of Action of Postsynaptic Neurotoxins. J. Toxicol.-Toxin Rev. 1986; 5: 95–104
   Web of Science ®Google Scholar
• Tamiya N., Arai H. Studies on Sea-Snake Venoms. Biochem. J. 1966; 99: 624–630
   PubMed Web of Science ®Google Scholar
• Lester H.A. Blockade of Acetylcholine Receptors by Cobra Toxin: Electrophysiological Studies. Mol. Pharmacol. 1972; 6: 623–631
   Google Scholar
• Jiang M-S., Fletcher J.E., Smith L.A. Factors Influencing the Hemolysis of Human Erythrocytes by Cardiotoxins from Naja naia kaouthia. and Naja naja atra Venoms, and a Phospholipase A2 with Cardiotoxin-Like Activities from Bungarus fasciatus Venom. Toxicon 1989; 27: 247–257
   PubMed Web of Science ®Google Scholar
• Jiang M-S., Fletcher J.E., Smith L.A. Effects of Divalent Cations on Snake Venom Cardiotoxin-Induced Hemolysis and 3H-Deoxyglucose-6-Phosphate Released from Human Red Blood Cells. Toxicon 1989; 27: 1297–1305
   PubMed Web of Science ®Google Scholar
• Bjarnason J.B., Fox J.W. Hemorrhagic Toxins from Snake Venoms. J. Toxicol.-Toxin Rev. 1989; 7: 121–209
   Web of Science ®Google Scholar
• Longenecker G.L., Longenecker H.E, Jr. Interactions of Venoms and Venom Components with Blood Platelets. J. Toxicol.-Toxin Rev. 1984; 3: 223–251
   Web of Science ®Google Scholar
• Brown C.H., III, Bell W.R., Shreiner D.P., Jackson D.P. Effects of Arvin on Blood Platelets. In Vitro and In Vivo Studies. J. Lab. Clin. Med. 1972; 79: 758–768
   PubMed Web of Science ®Google Scholar
• Holleman W.H., Weiss L.J. The Thrombin-Like Enzyme from Bothrops atrox Snake Venom. J. Biol. Chem. 1976; 251: 1663–1669
   PubMed Web of Science ®Google Scholar
• Gan Z-R., Gould R.J., Jacobs J.W., Friedman P.A., Polokoff M.A. Echistatin: A Potent Platelet Aggregation Inhibitor from the Venom of the Viper, Echis carinatus. J. Biol. Chem. 1988; 263: 19827–19832
   PubMed Web of Science ®Google Scholar
• Meldolesi J., Scheer H., Madeddu L., Wanke E. Mechanism of Action of α-Latrotoxin: the Presynaptic Stimulatory Toxin of the Black Widow Spider Venom. Trends Pharmacol. Sci. 1986; 7: 151–155
   Web of Science ®Google Scholar
• Rodriquez-Ithurralde D., Silveira R., Barbeito L., Dajas F. Fasciculin, a Powerful Anticholineasterase Polypeptide from Dendroaspis angusticeps Venom. Neurochem. Internat 1983; 5: 267–274
   Google Scholar
• Reynolds R.P., Scott N.J. Use of a Mammalian Resource by a Chihuahuan Snake Community, in Herpetological Communities. U.S. Dept. of the Interior, Fish and Wildlife Service, Washington, D.C. 1982
   Google Scholar
• Eaker D., Halpert J., Fohlman J., Karlsson E. Structural Nature of Presynaptic Neurotoxins from the Venoms of the Australian Tiger Snake, Notechis scutatus scutatus. and the Taipan Oxyuranus scutellatus scutellatus. Animal Plant and Microbial Toxins Chemistry, Pharmacology, and Immunology, A. Ohsaka, K. Hayashi, Y. Sawai. Plenum Press, New York 1976; Vol. 2: 27–45
   Google Scholar
• Halpert J., Eaker D. Isolation of a Non-Neurotoxic, Non-Enzymatic Phospholipase A Homologue from the Venom of the Australian Tiger Snake Notachis scutatus scutatus. FEBS Lett. 1976; 71: 91–95
   Web of Science ®Google Scholar
• Halpert J., Eaker D. Isolation and Amino Acid Sequence of a Neurotoxic Phospholipase A from the Venom of the Australian Tiger Snake Notachis scutatus scutatus. J. Biol. Chem. 1976; 251: 7343–7347
   PubMed Web of Science ®Google Scholar
• Schmidt J.J., Middlebrook J.L. Purification, Sequencing and Characterization of Pseudexin Phospholipases A2 from Pseudechis porphyriacus (Australian Red-Bellied Black Snake). Toxicon 1989; 27: 805–818
   PubMed Web of Science ®Google Scholar
• Ritonja A., Gubensek F., Ammodytoxin A. a Highly Lethal Phospholipase A2 from Vipera ammodytes ammodytes Venom. Biochim. Biophy. Acta 1985; 828: 306–312
   PubMed Web of Science ®Google Scholar
• Ritonja A., Machleidt W., Turk V., Gubensek F. Amino-Acid Sequence of Ammodytoxin B Partially Reveals the Location of the Site of Toxicity of Ammodytoxins. Biol. Chem., Hoppe-Seyler 1986; 367: 919–923
   PubMed Web of Science ®Google Scholar
• Krizaj I., Turk D., Ritonja A., Gubensek F. Primary Structure of Ammodytoxin C Further Reveals the Toxic Site of Ammodytoxin. Biochim. Biophy. Acta 1989; 999: 198–202
   PubMed Web of Science ®Google Scholar
• Lee C.Y., Chang S.L., Kau S.T., Luh S-H. Chromatographic Separation of the Venom of Bungarus multicinctus and Characterization of its Components. J. Chromatogr. 1972; 72: 71–82
   PubMed Web of Science ®Google Scholar
• Kondo K., Narita K., Lee C.Y. Amino Acid Sequences of the Two Polypeptide Chains in b1-Bungarotoxin from the Venom of Bungarus multicinctus. J. Biochem. (Tokyo) 1978; 83: 101–115
   PubMed Web of Science ®Google Scholar
• Faure G., Bon C. Crotoxin, a Phospholipase A2 Neurotoxin from the South American Rattlesnake Crotalus durissus terrificus: Purification of Several Isoforms and Comparison of Their Molecular Structure and of Their Biological Activities. Biochemistry 1988; 27: 730–738
   PubMed Web of Science ®Google Scholar
• Cate R.L., Bieber A.L. Purification and Characterization of Mojave (Crotalus scutulatus scutulatus) Toxin and Its Subunits. Arch. Biochem. Biophys. 1978; 189: 397–408
   PubMed Web of Science ®Google Scholar
• Fohlman J., Eaker D., Karlsson E., Thesleff S. Taipoxin, An Extremely Potent Presynaptic Neurotoxin from the Venom of the Australian Snake Taipan (Oxyuranus s. scutellatus). Eur. J. Biochem. 1976; 68: 457–469
   PubMedGoogle Scholar
• Tyler M.I., Barnett D., Nicholson P., Spence I., Howden E.H. Studies on the Subunit Structure of Textilotoxin, a Potent Neurotoxin from the Venom of the Australian Common Brown Snake (Pseudonaja textilis). Biochim. Biophy. Acta 1987; 915: 210–216
   PubMed Web of Science ®Google Scholar
• Rochat H., Rochat C., Sampieri F., Miranda F. The Amino-Acid Sequence of Neurotoxin II of Androctonus australis Hector. Eur. J. Biochem. 1972; 28: 381–388
   PubMedGoogle Scholar
• Chuang L.Y., Lin S.R., Chang S.F., Chang C.C. Preparation and Characterization of Monoclonal Antibody Specific for α-Bungarotoxin and Localization of the Epitope. Toxicon 1989; 27: 211–219
   PubMed Web of Science ®Google Scholar
• Kosen P.A., Finer-Moore J., McCarthy M.P., Basus V.J. Structural Studies of α-Bungarotoxin. Corrections in the Primary Sequence and X-Ray Structure and Characterization of an Isotoxic α-Bungarotoxin. Biochemistry 1988; 27: 2775–2781
   PubMed Web of Science ®Google Scholar
• Rochat H., Bernard P., Courand F. Scorpion Toxins: Chemistry and Mode of Action. Adv. Cytopharmacol. 1979; 3: 325–334
   PubMedGoogle Scholar
• Wunderer G., Fritz H., Wachter E., Machleidt W. Amino-Acid Sequence of a Coelenterate Toxin: Toxin II from Anemonia Sulcata. Eur. J. Biochem. 1976; 68: 193–198
   PubMedGoogle Scholar
• Eipper B.A., Mains R.E. Peptide a-Amidation. Ann. Rev. Physiol. 1988; 50: 333–344
   PubMed Web of Science ®Google Scholar
• Eipper B.A., Mains R.E., Herbert E. Peptides in the Nervous System. Trends Neurosci. 1986; 9: 463–468
   Web of Science ®Google Scholar
• Joubert F.J., Taljaard N. Snake Venoms: The Amino Acid Sequences of Two Proteinase Inhibitor Homologues from Dendroaspis angusticeps Venom. Hoppe-Seylers Z. Physiol. Chem. 1980; 361: 661–674
   PubMedGoogle Scholar
• Aird S.D., Kaiser I.I., Lewis R.V., Kruggel W.G. Rattlesnake Presynaptic Neurotoxins: Primary Structure and Evolutionary Origin of the Acidic Subunit. Biochemistry 1985; 24: 7054–7058
   PubMed Web of Science ®Google Scholar
• Aird S.D., Yates J.R., III, Martino P.A., Shabanowitz J., Hunt D.F., Kaiser I.I. The Amino Acid Sequence of the Acidic Subunit B Chain of Crotoxin, personal communication
   Google Scholar
• Bieber A.L., Becker R.R., McParland R., Hunt D.F., Shabanowitz J., Yates J.R., III, Martino P.A., Johnson G.R. The Complete Sequence of the Acidic Subunit from Mojave Toxin Determined by Edman Degradation and Mass Spectrometry. Biochim. Biophys. Acta 1990; 1037: 413–421
   PubMed Web of Science ®Google Scholar
• Austen B.M. Predicted Secondary Structures of Amino-Terminal Extension Sequences of Secreted Proteins. FEBS Lett. 1979; 103: 308–313
   PubMed Web of Science ®Google Scholar
• Molecular Cloning: A Laboratory Manual, J. Sambrook, E.F. Fritsch, T. Maniatis. Cold Spring Harbor Laboratories, Cold Spring Harbor, New York 1989; 1, 2, and 3
   Google Scholar
• Current Protocols in Molecular Biology, F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, K. Struhl. John Wiley and Sons, New York 1989; Vols. 1 and 2
   Google Scholar
• Perbal B. A Practical Guide to Molecular Cloning. John Wiley and Sons, New York 1988
   Google Scholar
• DNA Cloning, D.M. Glover. IRL Press, Oxford 1986; Vol.1
   Google Scholar
• Vectors: A survey of Molecular Cloning Vectors and Their Uses, R.L. Rodriguez, D.T. Denhardt. Butterworths Publishers, Boston 1988
   Google Scholar
• Pouwels P.H., Enger-Valk B.E., Brammar W.J. Cloning Vectors: A Laboratory Manual. Elsevier Science Publishers, New York 1978
   Google Scholar
• Eukaryotic Viral Vectors, Y. Gluzman. Cold Spring Harbor Laboratories, Cold Spring Harbor, New York 1982
   Google Scholar
• Miller J.H., Calos M.P. Gene Transfer Vectors for Mammalian Cells. Cold Spring Harbor Laboratories, Cold Spring Harbor, New York 1987
   Google Scholar
• Huse W.D., Hansen C. cDNA Cloning Redefined: A Rapid, Efficient, Directional Method. Strategies 1988; 1: 1–3
   Google Scholar
• Short J.M., Fernandez J.M., Sorge J.A, Huse W.D. λ Zap: A Bacteriophage I Expression Vector with In-Vivo Excision Preperties. Nucleic Acids Res. 1988; 16: 7583–7600
   PubMed Web of Science ®Google Scholar
• Huynh T.V., Young R.A., Davis R.W. Construction and Screening cDNA Libraries in lgt10 and lgt11. DNA Cloning: A Practical Approach, D.M. Glover. IRL Press, Oxford 1985; Vol. 1: 49–78
   Google Scholar
• Glenn J.L., Straight R.C. Mojave Rattlesnake Crotalus scutulatus scutulatus Venom: Variation in Toxicity With Geographical Origin. Toxicon 1978; 16: 81–84
   PubMed Web of Science ®Google Scholar
• Vandenplas M.L., Vandenplas S., Brebner K., Bester A.J., Boyd C.D. Characterization of the Messenger RNA Population Coding for Components of Viperid Snake Venom. Toxicon 1985; 23: 289–305
   PubMed Web of Science ®Google Scholar
• Feramisco J.R., Helfman D.M., Smart J.E., Burridge, Thomas G.P. Coexistence of Vinculin-Like Protein of Higher Molecular Weight in Smooth Muscle. J. Biol. Chem. 1982; 257: 11024–11031
   PubMed Web of Science ®Google Scholar
• Aviv H., Leder P. Purification of Biologically Active Globin Messenger RNA by Chromatography on Oligothymidylic Acid-Cellulose. Proc. Natl. Acad. Sci. U.S.A. 1972; 69: 1408–1412
   PubMed Web of Science ®Google Scholar
• Gubler U., Hoffman B.J. A Simple and Very Efficient Method for Generating cDNA Libraries. Gene 1983; 25: 263–269
   PubMed Web of Science ®Google Scholar
• Okayama H., Berg P. High-Efficiency Cloning of Full-Length cDNA. Mol. Cell. Biol. 1982; 2: 161–170
   PubMed Web of Science ®Google Scholar
• Okayama H., Berg P. A cDNA Cloning Vector That Permits Expression of cDNA Inserts in Mammalian Cells. Mol. Cell. Biol. 1983; 3: 280–289
   PubMed Web of Science ®Google Scholar
• Maxam A.M., Gilbert W. Sequencing End-Labeled DNA with Base-Specific Chemical Cleavages. Methods in Enzymology, L. Grossman, K. Moldave. Academic Press, New York 1980; Vol. 65: 499–560
   Google Scholar
• Sanger F., Nicklen S., Coulson A.R. DNA Sequencing with Chain-Terminating Inhibitors. Proc. Natl. Acad. Sci. U.S.A. 1977; 74: 5463–5467
   PubMed Web of Science ®Google Scholar
• Heidecker G., Messing J., Gronenbom B. A Versatile Primer for DNA Sequencing in the M13mp2 Cloning System. Gene 1980; 10: 69–73
   PubMed Web of Science ®Google Scholar
• Protocols and Application Guide. Promega Corp., Madison, WI 1989
   Google Scholar
• Henikoff S. Unidirectional Digestion with Exonuclease III Creates Targeted Breakpoints for DNA Sequencing. Gene 1984; 28: 351–359
   PubMed Web of Science ®Google Scholar
• Harris T.J.R. Expression of Eukaryotic Genes. E. coli. in Genetic Engineering, R. Williamson. Academic Press, New York 1983; Vol. 4: 127–186
   Google Scholar
• Remaut E., Stanssens P., Fiers W. Plasmid Vectors for High-Efficiency Expression Controlled by the pL Promoter of Coliphage Lambda. Gene 1981; 15: 81–93
   PubMed Web of Science ®Google Scholar
• Ruther U. Construction and Properties of a New Cloning Vehicle, Allowing Direct Screening for Recombinant Plasmids. Mol. Gen. Genet. 1980; 178: 475–477
   PubMedGoogle Scholar
• Vernet T., Dignard D., Thomas D.Y. A Family of Yeast Expression Vectors Containing the Phage f1 Intergenic Region. Gene 1987; 52: 225–233
   PubMed Web of Science ®Google Scholar
• Mackett M., Smith G.L., Moss B. The Construction and Characteristics of Vaccinia Virus Recombinants Expressing Foreign Genes. DNA Cloning: A Practical Approach, D.M. Glover. IRL Press, Oxford 1985; Vol. II: 191–211
   Google Scholar
• Miller D.W., Safer P., Miller L.K. An Insect Baculovirus Host-Vector System for High-Level Expression of Foreign Genes. Genetic Engineering: Principles and Methods, J.K. Setlow, A. Hollaender. Plenum Press, New York 1986; Vol. 8: 277–298
   Google Scholar
• Gorman C. High Efficiency Gene Transfer into Mammalian Cells. DNA Cloning: A Practical Approach, D.M. Glover. IRL Press, Oxford 1985; Vol. II: 143–190
   Google Scholar
• Bebbington C.R., Hentschel C.C. The Use of Vector Based on Gene-Amplification for the Expression of Cloned Genes in Mammalian Cells. DNA Cloning: A Practical Approach, D.M. Glover. IRL Press, Oxford 1985; Vol. III: 163–188
   Google Scholar
• Moss B., Flexner C. Vaccinia Virus Expression Vectors. Annu. Rev. Immunol. 1987; 5: 305–324
   PubMed Web of Science ®Google Scholar
• Cochran M.A., Ericson B.L., Knell J.D., Smith G.E. Use of Baculovirus Recombinants as a General Method for the Production of Subunit Vaccines. Vaccines 87. Cold Spring Harbor Laboratory Laboratories, Cold Spring Harbor, New York 1987; 384–388
   Google Scholar
• Luckow V.A., Summers M.D. Trends in the Development of Baculovirus Expression Vectors. Biotechnology 1988; 6: 47–55
   Web of Science ®Google Scholar
• Kaufman R.J., Sharp P.A. Amplification and Expression of Sequences Cotransfected with a Modular Dihydrofolate Reductase Complementary DNA Gene. J. Mol. Biol. 1982; 159: 601–621
   PubMed Web of Science ®Google Scholar
• Stephens P.E., Hentschel C.C. The Bovine Papilloma Virus Genome and Its Uses as a Eukaryotic Vector. Biochem. J. 1987; 248: 1–11
   PubMed Web of Science ®Google Scholar
• Experimental Manipulation of Gene Expression, M. Inouye. Academic Press, New York 1983
   Google Scholar
• Guignery-Frelat G., Duncancel F., Menez A., Boulain J-C. Sequence of a cDNA Encoding a Snake Venom Phospholipase A2. Nucleic Acids Res. 1987; 15: 5892
   PubMed Web of Science ®Google Scholar
• Duncancel F., Guignery-Frelat G., Bouchier C., Menez A., Boulain J-C. Sequence Analysis of a cDNA Encoding a PLA2 from the Sea-Snake Aipysurus laevis. Nucleic Acids Res. 1988; 16: 9048
   PubMed Web of Science ®Google Scholar
• Duncancel F., Guignery-Frelat G., Bouchier C., Menez A., Boulain J-C. Complete Amino Acid Sequence of a PLA2 from the Tiger Snake Notechis scutatus scutatus as Deduced from a Complementary DNA. Nucleic Acids Res. 1988; 16: 9049
   PubMedGoogle Scholar
• Bouchier C., Ducancel F., Guignery-Frelat G., Bon C., Boulain J-C., Menez A. Cloning and Sequencing of cDNAs Encoding the Two Subunits of Crotoxin. Nucleic Acids Res. 1988; 16: 9050
   PubMed Web of Science ®Google Scholar
• Pungercar J., Kordis D., Jerala R., Trstenjak-Prebanda M., Dolinar M., Curin-Serbec V., Komel R., Gubensek F. Amino Acid Sequence of Ammodytoxin C as Deduced from cDNA. Nucleic Acids Res. 1989; 17: 4367
   PubMed Web of Science ®Google Scholar
• Smith L.A., unpublished results
   Google Scholar
• Chang C.C. Neurotoxins with Phospholipase A2 Activity in Snake Venoms. Proc. Natl. Sci. Counc. Repub. China [B] 1985; 9: 126–142
   PubMedGoogle Scholar
• Gubensek F., personal communication
   Google Scholar
• Aird S.D., Kaiser I.I., Lewis R.V., Kruggel W.G. A Complete Amino Acid Sequence for the Basic Subunit of Crotoxin. Arch. Biochem. Biophys. 1986; 249: 296–300
   PubMed Web of Science ®Google Scholar
• Aird S., Kruggel W., Kaiser I.I. Amino Acid Sequence of the Basic Subunit of Mojave Toxin from the Venom of the Mojave Rattlesnake. Crotalus scutulatus scutulatus, in press
   Google Scholar
• Tamiya T., Lamouroux A., Julien J-F., Grima B., Mallet J., Fromageot P., Menez A. Cloning and Sequence Analysis of the cDNA Encoding a Snake Neurotoxin Precursor. Biochimie 1985; 67: 185–189
   PubMed Web of Science ®Google Scholar
• Obara K., Fuse N., Tsuchiya T., Nonomura Y., Menez A., Tamiya T. Sequence Analysis of a cDNA Encoding a Erabutoxin b from the Sea-Snake Laticauda semifasciata. Nucleic Acids Res. 1989; 17: 10490
   PubMed Web of Science ®Google Scholar
• Duncancel F., Guignery-Frelat G., Boulain J-C., Menez A. Nucleotide Sequence and Structure Analysis of cDNAs Encoding Short-Chain Neurotoxins from Venom Glands of a Sea Snake (Aipysurus laevis). Toxicon 1990; 28: 119–123
   PubMed Web of Science ®Google Scholar
• Maeda N., Tamiya N. Isolation, Properties and Amino Acid Sequences of Three Neurotoxins from the Venom of the Sea Snake. Aipysurus laevis. Biochem. J. 1976; 153: 79–87
   PubMed Web of Science ®Google Scholar
• Smith L.A. Nucleotide Sequence of a cDNA Encoding Toxin C from Dendroaspis polylepis. Presented at the 21st Annual Meeting of the American Society for Neurochemistry, Phoenix, Arizona, 1990
   Google Scholar
• Loridan C., Middlebrook J. Cloning and Sequencing of the cDNA Coding for Myotoxin A. Toxicon 1988; 27: 60
   Google Scholar
• Smith L.A., Schmidt J.J. Cloning and Nucleotide Sequences of Crotamine Genes. Toxicon 1990; 28: 575–585
   PubMed Web of Science ®Google Scholar
• Itoh N., Tanaka N., Mihashi S., Yamashina I. Molecular Cloning and Sequence Analysis od cDNA for Batroxobin, a Thrombin-Like Snake Venom Enzyme. J. Biol. Chem. 1987; 262: 3132–3135
   PubMed Web of Science ®Google Scholar
• Itoh N., Tanaka FunakoshiI., Kawasaki T.N., Mihashi S., Yamashina I. Organization of the Gene for Batroxobin, a Thrombin-Like Snake Venom Enzyme. J. Biol. Chem. 1988; 263: 7628–7631
   PubMed Web of Science ®Google Scholar
• Filho PellegriniA., Brazil VitalO., Fontana M.D., Laure C.J. The Action of Crotamine on Skeletal Muscle: an Electrophysiological Study. Toxins: Animal, Plant and Microbial. Proceedings of the 5th International Symposium on Animal, Plant and Microbial Toxins, P. Rosenberg. Pergamon Press, London 1978; 375–382
   Google Scholar
• Laure C.J. Die Primarstruktur des Crotamins. Hoppe-Seyler's Z. Physiol. Chem. 1975; 356: 213–215
   PubMedGoogle Scholar
• Bougis P.E., Rochat H., Smith L.A. Scorpion Venom Neurotoxins: cDNA Cloning and Expression. Natural Toxins: Characterization, Pharmacology and Therapeutics, C.L. Ownby, G.V. Odell. Pergamon Press, New York 1989
   Google Scholar
• Bougis P.E., Rochat H., Smith L.A. Precursors of Androctonus australis Scorpion Neurotoxins. J. Biol. Chem. 1989; 264: 19259–19265
   PubMed Web of Science ®Google Scholar
• Krell G., Mollay C., Kaschnitz R., Haiml L., Vilas U. Prepromellitin: Specific Cleavage of the Pre- and the Propeptide In Vitro. Ann. N.Y. Acad. Sci. 1980; 343: 338–346
   PubMedGoogle Scholar
• Woodward S.R., Cruz L.J., Olivera B.M., Hillyard D.R. Constant and Hypervariable Regions in Conotoxin Propeptides. EMBO J. 1990; 9: 1015–1021
   PubMed Web of Science ®Google Scholar
• Vlasak R., Unger-Ullmann C., Kreil G., Frischauf A-M. Nucleotide Sequence of Cloned cDNA Coding for Honeybee Prepromellitin. Eur. J. Biochem. 1983; 135: 123–126
   PubMedGoogle Scholar
• Kuchler K., Gmachl M., Sippl M.J., Kreil G. Analysis of the cDNA for Phospholipase A2 from Honeybee Venom Glands. Eur. J. Biochem. 1989; 184: 249–254
   PubMedGoogle Scholar
• Hillyard D.R., Olivera B.M., Woodward S., Corpuz G.P., Gray W.R., Ramilo C.A., Cruz L.J. A Molluscivorous Conus Toxin: Conserved Frameworks in Conotoxins. Biochemistry 1989; 28: 358–361
   PubMed Web of Science ®Google Scholar
• Dulubova I.E., Kiyatkin N.I., Chekhovskaya I.V., Grishin E.V. Structural Analysis of Black Widow Spider Neurotoxin Gene. Presented at the Second Asia-Pacific Congress on Animal, Plant and Microbial Toxins, Varanasi-221005, India, 1990, 24, Abstracts
   Google Scholar
• Gan Z-R., Condra J.H., Gould R.J., Zivin R.A., Bennett C.D., Jacobs J.W., Friedman P.A., Polokoff M.A. High-Level Expression in Escherichia coli of a Chemically Synthesized Gene for [Leu-28]Echistatin. Gene 1989; 79: 159–166
   PubMed Web of Science ®Google Scholar
• Howell M.L., Blumenthal K.M. Cloning and Expression of a Synthetic Gene for Cerebratulus lacteus Neurotoxin B-IV. J. Biol. Chem. 1989; 264: 15268–15273
   PubMed Web of Science ®Google Scholar
• Ducancel F., Boulain J-C., Tremeau O., Menez A. Direct Expression in E coli of a Functionally Active Protein A-Snake Toxin Fusion Protein. Protein Engineering. 1989; Vol. 3: 139–143
   Google Scholar
• De Geus P., van den Bergh C.J., Kuipers O., Verheij H.M., Hoekstra W.P.M., De Haas G.H. Expression of Porcine Pancreatic Phospholipase A2. Generation of Active Enzyme by Sequential Specific Cleavage of a Hybrid Protein from Escherichia coli. Nucleic Acids Res. 1987; 15: 3743–3759
   PubMed Web of Science ®Google Scholar
• Blumenthal K.M., Keim P.S., Heinrikson R.L., Kem W.R. Structure and Action of Heteronemertine Polypeptide Toxins. J. Biol. Chem. 1981; 256: 9063–9067
   PubMed Web of Science ®Google Scholar
• Yanisch-Perron C., Vieira J., Messing J. Improved M13 Phage Cloning Vectors and Host Strains: Nucleotide Sequences of the M13mp18 and pUC19 Vectors. Gene 1985; 33: 103–119
   PubMed Web of Science ®Google Scholar
• Thannhauser T.W., Scheraga H.A. Reversible Blocking of Half-Cystine Residues of Proteins and an Irreversible Specific Deamidation of Asparagine-67 of S-Sulforibonuclease Under Mild Conditions. Biochemistry 1985; 24: 7681–7688
   PubMed Web of Science ®Google Scholar
• Nilsson B., Abrahmsen L., Uhlen M. Immobilization and Purification of Enzymes With Staphylococcal Protein A Gene Fusion Vectors. EMBO J. 1985; 4: 1075–1080
   PubMed Web of Science ®Google Scholar
• Carbonell L.F., Hodge M.R., Tomalski M.D., Miller L.K. Synthesis of a Gene Coding for an Insect-Specific Scorpion Neurotoxin and Attempts to Express it Using Baculovirus Vectors. Gene 1988; 73: 409–418
   PubMed Web of Science ®Google Scholar
• Dee A., Belagaje R.M., Ward K., Chio E., Lai M-H.T. Expression and Secretion of a Functional Scorpion Insecticidal Toxin in Cultured Mouse Cells. Biotechnology 1990; 8: 339–342
   PubMedGoogle Scholar
• Zlotkin E. Insect Selective Toxins Derived from Scorpion Venoms. Insect. Biochem. 1983; 13: 219–236
   Google Scholar
• Smith G.E., Summers M.D., Fraser M.J. Production of Human β-Interferon in Insect Cells Infected With a Baculovirus Expression Vector. Mol. Cell. Biol. 1983; 3: 2156–2165
   PubMed Web of Science ®Google Scholar
• Stratowa C., Doehmer J., Wang Y., Hofschneider P.H. Recombinant Retroviral DNA Yielding High Expression of Hepatitis B Surface Antigen. EMBO J. 1982; 1: 1573–1578
   PubMed Web of Science ®Google Scholar
• Ratner M. Protein Expression in Yeast. Biotechnology 1989; 7: 1129–1133
   Google Scholar